|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-596 |
0e+00 |
|
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: 533.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 122 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEGQVTELRS 179
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 180 RVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVK 259
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 260 altreqeKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE 339
Cdd:pfam07888 161 -------KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 340 PLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV 419
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 420 EAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEY 499
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 500 MRKLEARLEKVADEKWNEDATTEDEEAavglscPAALTDSEDESPEDMRLPP----YGLCERG-----DPGSSPAGPREA 570
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERP------DSPLSDSEDENPEALQPPRplghYSLCEQGqpdslLLATPPPSPRDP 467
|
490 500
....*....|....*....|....*.
gi 14149742 571 SPLVVISQPAPISPHlsgpaEDSSSD 596
Cdd:pfam07888 468 ESTVVISQPAPLSSP-----HQSSSD 488
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-118 |
6.41e-40 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 141.61 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 15 VNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWssVPESTTDGSPIHTSVQFQASYLPKPG 94
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 14149742 95 AQLYQFRYVNRQGQVCGQSPPFQF 118
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-542 |
1.37e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 174 VTELRSRVQELERALATAR--QEHTELMEQYKGISRSHgeiteERDILSRQQGDHVARILELEDDIQTISEKVLTKEVEL 251
Cdd:COG1196 195 LGELERQLEPLERQAEKAEryRELKEELKELEAELLLL-----KLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQA 331
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKE 411
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 412 RAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQE 491
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA----ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 14149742 492 EKQELLEYMRKLEARL--EKVADEKWNEDATTEDEEAAVGLSCPAALTDSEDE 542
Cdd:COG1196 506 FLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-529 |
6.68e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 224
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 225 DHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAK 304
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 305 SWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSR 384
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 385 LEVAEVNGRLAELGLHLKEEKCQ-----WSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKD 459
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 460 SSLVQ-LSESKRELTELRSALRV--------LQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVG 529
Cdd:COG1196 546 AALQNiVVEDDEVAAAAIEYLKAakagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-491 |
1.01e-17 |
|
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: 87.82 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 167 KLQLEGQVTELRSRVQELERALATARQEHT-------ELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQT 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 240 ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA----------DKEQSEAELQVAQQENHHLNLDLKEAKSWQEE 309
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 310 QSAQAQRlKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAE 389
Cdd:TIGR02169 829 EYLEKEI-QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 390 VNGRLAELGLHLKEEKCQWSkERAGLLQSVEAEKDKILKLSAEILRLEKaVQEERTQNQVFKTELAREKDSSLVQLSESK 469
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
330 340
....*....|....*....|..
gi 14149742 470 RELTELRSALRVLQKEKEQLQE 491
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILE 1007
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-485 |
4.03e-15 |
|
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: 79.34 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKlqlegqvtELRSRVQELERALATARQEHTElmEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQ--------ALLKEKREYEGYELLKEKEALE--RQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTK-EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEV 387
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 388 AEVNGRLAELglhlkeekcqwskeRAGLLQSVEAEKDKILKLSA---EILRLEKAVQEERTQNQVFKTELAREKDsslvQ 464
Cdd:TIGR02169 423 ADLNAAIAGI--------------EAKINELEEEKEDKALEIKKqewKLEQLAADLSKYEQELYDLKEEYDRVEK----E 484
|
330 340
....*....|....*....|.
gi 14149742 465 LSESKRELTELRSALRVLQKE 485
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-455 |
9.15e-15 |
|
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: 78.56 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 160 RNDLMQLKLQLEG-QVTELRSRVQELERALATARQEHTELMEQykgISRSHGEITEERDI---LSRQQGDHVARILELED 235
Cdd:TIGR02168 219 KAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEvseLEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 236 DIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE-------NHHLNLDLKEAKSWQE 308
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaassQQKATLLGEELASAAAARDRTIAELHRSRLEVA 388
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE-----RLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149742 389 EVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELA 455
Cdd:TIGR02168 451 ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-506 |
1.40e-14 |
|
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: 77.79 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 150 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATAR-------QEHTELMEQYKGISRSHGEITEERDILSRQ 222
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 223 QGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKE 302
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 303 AKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHR 382
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 383 SRLEVAEVNGRLAELGLHlkeekcqwskeraglLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSL 462
Cdd:TIGR02168 913 LRRELEELREKLAQLELR---------------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 14149742 463 ---------VQLsESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:TIGR02168 978 enkikelgpVNL-AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
654-682 |
4.46e-14 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 66.37 E-value: 4.46e-14
10 20
....*....|....*....|....*....
gi 14149742 654 KECPICKERFPAESDKDALEDHMDGHFFF 682
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHFFF 29
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-527 |
5.90e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITE---ERDILSRQQGD 225
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 226 HVARILELEDDIQTISEkvltkEVELDRLRDtvKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKS 305
Cdd:PRK02224 284 LRERLEELEEERDDLLA-----EAGLDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 306 WQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAaaaRDRTIAELHRSRL 385
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE---RDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 386 EVAEVNGRLAELGLHLKEEKC---QWSKERAGLLQSVEAEKDKILKLSAEILRLEkaVQEERTQNQVFKTELAREKDSSL 462
Cdd:PRK02224 434 TLRTARERVEEAEALLEAGKCpecGQPVEGSPHVETIEEDRERVEELEAELEDLE--EEVEEVEERLERAEDLVEAEDRI 511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 463 VQLSESKRELTELRSalrvlqkEKEQLQEEKQELLEYMRKLEARLEKVADEKwnEDATTEDEEAA 527
Cdd:PRK02224 512 ERLEERREDLEELIA-------ERRETIEEKRERAEELRERAAELEAEAEEK--REAAAEAEEEA 567
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-526 |
2.15e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEgqvtELRSRVQELERALATARQEHTEL--MEQYKGISRSHGEITEERDILSRQQG-- 224
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEel 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 225 -DHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQ-EKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKe 302
Cdd:COG4717 152 eERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELE- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 303 akswQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLG-------EELASAAAARDR 375
Cdd:COG4717 231 ----QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 376 TIAELHRSRLEVAEVNGRLAELGL-----------------HLKEEKCQWSKERAGL-LQSVEAEKDKILKLS------- 430
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLppdlspeellelldrieELQELLREAEELEEELqLEELEQEIAALLAEAgvedeee 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 431 -AEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKREltELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:COG4717 387 lRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410
....*....|....*..
gi 14149742 510 VADEKWNEDATTEDEEA 526
Cdd:COG4717 465 LEEDGELAELLQELEEL 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-542 |
5.13e-13 |
|
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: 72.78 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 244 VLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQ 323
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 324 MKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRsrlEVAEVNGRLAELGLHLKE 403
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 404 EKCQ---WSKERAGLLQSVEAEKDKILKLSAEILRLEKAV---QEERTQNQVFKTELAREKDSSLVQLSESKRELTELRS 477
Cdd:TIGR02168 829 LERRiaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 478 ALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDSEDE 542
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-504 |
5.52e-13 |
|
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: 72.79 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRshgEITEERDilsrQQGDHVA 228
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ---EIENVKS----ELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLR-DTVKALTREQEK----LLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEA 303
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEevsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 304 KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGaQELAASSQQKATLLGEELASAAAARDRTIAELHRS 383
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 384 RLEVAEvnGRLAELGLHLKEEkcqwsKERAGLLQSVEAEKDKILKLSAEILRLE----KAVQEertqnqvFKTELAREKD 459
Cdd:TIGR02169 925 KLEALE--EELSEIEDPKGED-----EEIPEEELSLEDVQAELQRVEEEIRALEpvnmLAIQE-------YEEVLKRLDE 990
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 14149742 460 sslvqlseskreltelrsalrvLQKEKEQLQEEKQELLEYMRKLE 504
Cdd:TIGR02169 991 ----------------------LKEKRAKLEEERKAILERIEEYE 1013
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-513 |
7.50e-13 |
|
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: 70.56 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 276 QADKEQSEAELQVAQQEnhhlnldLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkeqlrgaQELAASS 355
Cdd:COG4942 19 ADAAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---------QELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 356 QQKATLlGEELASAAAARDRTIAELhRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV-EAEKDKILKLSA--- 431
Cdd:COG4942 83 AELAEL-EKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRAdla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 432 EILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 511
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 14149742 512 DE 513
Cdd:COG4942 241 ER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-398 |
1.73e-12 |
|
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: 70.86 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKswqe 308
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR---- 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 eqsAQAQRLKDKVAQMKDTLGQAQQRVAElepLKEQLRGAQELAAssqqkatllgEELASAAAARDRTIAELHRsrlEVA 388
Cdd:TIGR02168 915 ---RELEELREKLAQLELRLEGLEVRIDN---LQERLSEEYSLTL----------EEAEALENKIEDDEEEARR---RLK 975
|
250
....*....|
gi 14149742 389 EVNGRLAELG 398
Cdd:TIGR02168 976 RLENKIKELG 985
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-527 |
1.82e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLK------- 301
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavl 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 302 ---EAKSWQEEQSAQAQRLKDKVAqmkDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIA 378
Cdd:COG1196 530 igvEAAYEAALEAALAAALQNIVV---EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 379 EL--HRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR 456
Cdd:COG1196 607 DLreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 457 EKDSSLVQLSESKRELTELRSALRV---------LQKEKEQLQEEKQELLEYMRKLEARLEKVADEKwNEDATTEDEEAA 527
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEaeeerleeeLEEEALEEQLEAEREELLEELLEEEELLEEEAL-EELPEPPDLEEL 765
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-513 |
9.70e-12 |
|
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: 68.56 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSwQE 308
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA-QA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQR-LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAA---ARDR-----TIAE 379
Cdd:TIGR02169 500 RASEERVRgGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAielLKRRkagraTFLP 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 380 LHRSRLEVAEVnGRLAELG-----LHLKEEKCQWSK------ERAGLLQSVEAEKD-----KILKLSAEIL--------- 434
Cdd:TIGR02169 580 LNKMRDERRDL-SILSEDGvigfaVDLVEFDPKYEPafkyvfGDTLVVEDIEAARRlmgkyRMVTLEGELFeksgamtgg 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 435 -------RLEKAVQEERTQN-QVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:TIGR02169 659 sraprggILFSRSEPAELQRlRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
....*..
gi 14149742 507 LEKVADE 513
Cdd:TIGR02169 739 LEELEED 745
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-513 |
1.31e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 150 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQEL--ERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDhv 227
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 arILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:TIGR04523 344 --ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaaSSQQKATLLGEELASAAAARDRTIAELHRSRLEV 387
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 388 AEvngrlaelglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR-----EKDSSL 462
Cdd:TIGR04523 499 KK-----------LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekEIDEKN 567
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 14149742 463 VQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-375 |
7.67e-11 |
|
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: 64.40 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 224
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 225 DHVARILELEDDIQTISEKVLTKEV-------ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnhhLN 297
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149742 298 LDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLrgaQELAASSQQKATLLGEELASAAAARDR 375
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-514 |
1.15e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 169 QLEGQVTELRSRVQELERALATAR--------------QEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELE 234
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAReavedrreeieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 235 DDIQTISEKVltkeVELDRLRDTVKALTREQEKLLGQLKEVQADKEQ---------SEAELQVAQQENHHLNL-DLKEAK 304
Cdd:PRK02224 433 ATLRTARERV----EEAEALLEAGKCPECGQPVEGSPHVETIEEDRErveeleaelEDLEEEVEEVEERLERAeDLVEAE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 305 SWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAElepLKEQlrgAQELAASSQQKAtllgeelASAAAARDRtiAELHRSr 384
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEE---LRER---AAELEAEAEEKR-------EAAAEAEEE--AEEARE- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 385 lEVAEVNGRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKLSAEILRLekavQEERTQnqvfKTELAREKDSSLVQ 464
Cdd:PRK02224 573 -EVAELNSKLAEL------------KERIESLERIRTLLAAIADAEDEIERL----REKREA----LAELNDERRERLAE 631
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 14149742 465 LSESKRELTELRSALRVlqkekEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:PRK02224 632 KRERKRELEAEFDEARI-----EEAREDKERAEEYLEQVEEKLDELREER 676
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
170-497 |
1.82e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 64.07 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 170 LEGQVTELRSRVQELERALATARQEHTELMEQYKGISrshGEITEERDILSRQQgdhvARILELEDDIQTISEKVLTKEV 249
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA---GEIRDLKDMLDVKE----RKINVLQKKIENLQEQLRDKDK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 ELDRLRDTVK-----------ALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAK-------------- 304
Cdd:pfam10174 416 QLAGLKERVKslqtdssntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKekvsalqpelteke 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 305 ----SWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQ-------------QKATLLGEELA 367
Cdd:pfam10174 496 ssliDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeindrirlleQEVARYKEESG 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 368 SAAAARDRTIAELHRSRLEVAEVNGRLAEL--------------GLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEI 433
Cdd:pfam10174 576 KAQAEVERLLGILREVENEKNDKDKKIAELesltlrqmkeqnkkVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 434 LRLEKAVQEERTQNQVFKTELareKDSSLVQ-LSESKRELTELRSALRvlqKEKEQLQEEKQELL 497
Cdd:pfam10174 656 QLEELMGALEKTRQELDATKA---RLSSTQQsLAEKDGHLTNLRAERR---KQLEEILEMKQEAL 714
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-518 |
2.11e-10 |
|
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: 64.37 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQ-----LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRshgEITEERDILSRQQ 223
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 224 GDHVARILEL-----------EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:pfam15921 320 SDLESTVSQLrselreakrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 293 NHHL-------NLDLKEAKSWQEEQSAQAQRLKDKVAQMK-DTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLG- 363
Cdd:pfam15921 400 NKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRk 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 364 --EELASAA---AARDRTIAELHRSRLE----VAEVNGRLAEL--GLHLKEEKCQWSKERAGLLQSVE----------AE 422
Cdd:pfam15921 480 vvEELTAKKmtlESSERTVSDLTASLQEkeraIEATNAEITKLrsRVDLKLQELQHLKNEGDHLRNVQtecealklqmAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 423 KDKILK-LSAEILRLEKAV-QEERTQN--QVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLE 498
Cdd:pfam15921 560 KDKVIEiLRQQIENMTQLVgQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
410 420
....*....|....*....|
gi 14149742 499 YMRKleaRLEKVADEKWNED 518
Cdd:pfam15921 640 AGSE---RLRAVKDIKQERD 656
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
654-680 |
2.16e-10 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 55.73 E-value: 2.16e-10
10 20
....*....|....*....|....*..
gi 14149742 654 KECPICKERFPAESDKDALEDHMDGHF 680
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-490 |
3.71e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEkvltkevELDRLRDTVKAL--TREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLdlkeaksWQEE 309
Cdd:COG4913 222 DTFEAADALVE-------HFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAALRL-------WFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 310 QsaQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAE 389
Cdd:COG4913 288 R--RLELLEAELEELRAELARLEAELERLEARLDALR--EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 390 VNGRLAELGLHLKEEkcqwskeragllqsveaekdkilklsaeilrlEKAVQEERTQNQVFKTELAREKDSSLVQLSESK 469
Cdd:COG4913 364 LEALLAALGLPLPAS--------------------------------AEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
250 260
....*....|....*....|.
gi 14149742 470 RELTELRSALRVLQKEKEQLQ 490
Cdd:COG4913 412 AALRDLRRELRELEAEIASLE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-526 |
5.59e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTEL---MEQYKGISRSHGEITEERDILSRQQGd 225
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLellLSNLKKKIQKNKSLESQISELKKQNN- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 226 hvarilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQ-----SEAELQVAQQENHHLNLDL 300
Cdd:TIGR04523 229 ------QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkiKELEKQLNQLKSEISDLNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 301 KEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaQELAASSQQKATlLGEELASAAAARDRTIAEL 380
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK--KELTNSESENSE-KQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 381 HRSRLEVAEVNGRLAELGLHLKEEKcQWSKERAGLLQSVEAEKDKILK----LSAEILRLEKAVQEERTQNQVFKT---E 453
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEKELLEKeierLKETIIKNNSEIKDLTNQDSVKELiikN 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14149742 454 LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEarlEKVADEKWNEDATTEDEEA 526
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE---EKVKDLTKKISSLKEKIEK 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-503 |
7.31e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQ-------------YKGISRSHGEITEERDI 218
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 219 LSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTR--EQEKLLGQLKEVQADKEQSEAELqvAQQENHHL 296
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRL--TGLTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 297 NLDLKEAKSWQEEQSAQAQRLKDKVAQMKdtlgqaqQRVAELEPLKEQLRGAqelaassQQKATLLGEELASAAAAR--D 374
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELK-------KEIKELKKAIEELKKA-------KGKCPVCGRELTEEHRKEllE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 375 RTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVfkTEL 454
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL--KEK 533
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 14149742 455 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-456 |
1.04e-09 |
|
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: 60.93 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLg 329
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 330 QAQQRVAELEPLkeqlrgaqeLAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWS 409
Cdd:COG4942 114 YRLGRQPPLALL---------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14149742 410 KERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR 456
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-513 |
1.11e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 162 DLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITE-ERDILSRQQgdhvaRILELEDDIQTI 240
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElEKELESLEG-----SKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 241 SEKVLTKEVELDRLRDTVKALT------REQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAkswqEEQSAQA 314
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 315 QRLKDKVAQMKDTLGQAQQRVAELE---PLKEQLRG-AQELAASSQQKatlLGEELASAAAARDRTIAELHRSRLEVAEV 390
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEeakAKKEELERlKKRLTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 391 NGRLAELGLHLKEEKCQWSK-----------ERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTqnqvfKTELAREKD 459
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKE 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 460 SSLVQLSESKRELTELRSALRVLQKEK-EQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-546 |
1.47e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 158 QERNDLMQLKLQLEGQV-TELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEerdILSRQQGDHvARILELEDD 236
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHEERR-EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 237 IQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQR 316
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 317 LKDkvaqmkdtlgqaqqrvaELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:PRK02224 340 HNE-----------------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 397 LGLHLKEEkcqwSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKT-ELARE-KDSSLVQLSESKRE-LT 473
Cdd:PRK02224 403 APVDLGNA----EDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpECGQPvEGSPHVETIEEDRErVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 474 ELRSALRVLQKEKEQLqEEKQELLEYMRKLEARLEKVADEKWN--------EDATTEDEEAAVGLSCPAALTDSEDESPE 545
Cdd:PRK02224 479 ELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKR 557
|
.
gi 14149742 546 D 546
Cdd:PRK02224 558 E 558
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-524 |
1.62e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 158 QERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDI 237
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 238 QTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQenhhlnldLKEAKSWQEeqsaQAQRL 317
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA--------LLEAGKCPE----CGQPV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 318 KDkvAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHRSRLEVAEVNGRLAEl 397
Cdd:PRK02224 462 EG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA----EDLVEAEDRIERLEERREDLEELIAERRETIEE- 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 398 glhlKEEKCQWSKERAGLLQSVEAEKDkilklsAEILRLEKAVQEERTQNQVFKTELAREKDS--SLVQLSESKRELTEL 475
Cdd:PRK02224 535 ----KRERAEELRERAAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADA 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 14149742 476 RSALRVLQKEKEQLQEEKQELLEYM-------RKLEARLEKVADEKWNEDATTEDE 524
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLaekrerkRELEAEFDEARIEEAREDKERAEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-528 |
4.49e-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: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 251 LDRLRDTVKALTREQEKLlgqlkEVQADKEQSEAELQvAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQ 330
Cdd:TIGR02168 188 LDRLEDILNELERQLKSL-----ERQAEKAERYKELK-AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 331 AQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEekcqwsk 410
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE------- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 411 eragLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTelarekdsslvQLSESKRELTELRSALRVLQKEKEQLQ 490
Cdd:TIGR02168 335 ----LAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270
....*....|....*....|....*....|....*...
gi 14149742 491 EEKQELLEYMRKLEARLEKVADEkwNEDATTEDEEAAV 528
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQE--IEELLKKLEEAEL 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-397 |
5.76e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 197 ELMEQYKGISRSHGEITEERdilsrQQGDHVARILELEDDIQTISEKVLtkevELDRLRDTVKALTREQEKLLGQLKEVQ 276
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAR-----EQIELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 277 ADKEQSEAELQVAQQENHHLNLDLKEA---KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE--------PLKEQL 345
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDeleAQIRGNGGDRLEQLEREIERLERELEERERRRARLEallaalglPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14149742 346 RGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAEL 397
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-372 |
5.79e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 144 PKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQykgISRSHGEITEERDILsrqq 223
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 224 GDHVARILELEDDIQTISEKVLTKEVE--LDRLrDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLK 301
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSdfLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149742 302 EAKSWQEEQSAQAQRLkdkVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAA 372
Cdd:COG3883 168 AAKAELEAQQAEQEAL---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-517 |
6.83e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 124 MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYK 203
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 204 G--ISRSHGEIteeRDILSRqqgdhVARILELEDDIQ---TISEKVLTKEVELDRLRDTVKALTREQEKLLG-QLKEVQA 277
Cdd:PRK03918 451 KelLEEYTAEL---KRIEKE-----LKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEK 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 278 DKEQSE---AELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAE-LEPLKEQLrgaQELAA 353
Cdd:PRK03918 523 KAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERL---KELEP 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 354 SSQQKATLLG--EELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagllqsVEAEKDKILKLSA 431
Cdd:PRK03918 600 FYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEYLELSR 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 432 EILRLEKAVQEERTQNQvfktelarEKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLE----ARL 507
Cdd:PRK03918 674 ELAGLRAELEELEKRRE--------EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKeralSKV 745
|
410
....*....|
gi 14149742 508 EKVADEKWNE 517
Cdd:PRK03918 746 GEIASEIFEE 755
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
151-509 |
9.06e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 151 NQLDESQQERNDLMQLKLQLEGQVTELRSR-VQELERALATARQEHTELMEQYKgisrshgEITEERDILSRQQGDHVAR 229
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEIS-------KITARIGELKKEIKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 230 ILELED----------DIQTISEKVLTKE--VELDRLRDTVKALTREQEKLLGQLKEVQ-ADKEQSE--AELQVAQQ--- 291
Cdd:PRK03918 428 IEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEkVLKKESEliKLKELAEQlke 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 292 -ENHHLNLDLKEAkswqEEQSAQAQRLKDKVAQMKdtlgqaqqrvAELEPLKEQLRGAQELaassQQKATLLGEELASAa 370
Cdd:PRK03918 508 lEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLK----------GEIKSLKKELEKLEEL----KKKLAELEKKLDEL- 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 371 aarDRTIAELHRSRLE-----VAEVNGRLAELG------LHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKA 439
Cdd:PRK03918 569 ---EEELAELLKELEElgfesVEELEERLKELEpfyneyLELKDAE----KELEREEKELKKLEEELDKAFEELAETEKR 641
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 440 VQEERTQNQVFKTELAREKdsslvqLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:PRK03918 642 LEELRKELEELEKKYSEEE------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-507 |
1.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDIlsrQQGDHV 227
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL---KEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 ARILeleddiqTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA-DKEQSEAELQVAQQENHHLNLDLKEAKSW 306
Cdd:COG4717 252 LLIA-------AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLArEKASLGKEAEELQALPALEELEEEELEEL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 307 QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaqeLAASSQQKATLLGE----------ELASAAAARDRT 376
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALLAEagvedeeelrAALEQAEEYQEL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 377 IAELHRSRLEVAEVNGRLAELGLHLKEEkcQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVfkTELAR 456
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQ 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 14149742 457 EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQ-ELLEYMRKLEARL 507
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-525 |
1.32e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 150 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELmeqykgisRSHGEITE-ERDILSRQQGDHVA 228
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------LAEAGLDDaDAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQE 308
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEP----LKEQLRGAQELAASSqqKATLLGEELASAAAArdRTIAElhrSR 384
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEAtlrtARERVEEAEALLEAG--KCPECGQPVEGSPHV--ETIEE---DR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 385 LEVAEVNGRLAELglhlkeekcqwskeragllqsveaeKDKILKLSAEILRLEKAVQEERtqnqvfKTELAREKDSSLVQ 464
Cdd:PRK02224 475 ERVEELEAELEDL-------------------------EEEVEEVEERLERAEDLVEAED------RIERLEERREDLEE 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149742 465 LSESKRE-LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE--KWNEDATTEDEE 525
Cdd:PRK02224 524 LIAERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaELNSKLAELKER 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
152-512 |
1.55e-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: 58.06 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEGQVTELRS---RVQELERALATARQ-----EHTELMEQY-KGISRSHGEITE---ERDIL 219
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAqeaVLEETQERINRARKaaplaAHIKAVTQIeQQAQRIHTELQSkmrSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 220 SRQQGDHVARILELEDdiQTISEKVLTKEVELDRLRDTVKALTRE----QEKLLGQLKEVQADKEQSEAELQVAQQENHH 295
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEE--QRRLLQTLHSQEIHIRDAHEVATSIREiscqQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 296 LNLDLKEAKSWQEEQSAQAQRL----KDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEElaSAAA 371
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK--EQIH 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 372 ARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149742 452 TELAREKDSSLV---QLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVAD 512
Cdd:TIGR00618 563 EQMQEIQQSFSIltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
152-525 |
1.99e-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: 57.67 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDhVARIL 231
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEK--VLTKEVE-LDRLRDTVKALTREQEKLLGQLkevQADKEQSEAELQVAQQENHHLNLDLKEAKSWQE 308
Cdd:TIGR00618 383 TLQQQKTTLTQKlqSLCKELDiLQREQATIDTRTSAFRDLQGQL---AHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDtLGQAQQRVAELEPLKEQLrgAQELAassQQKATLLGEELASAAAARDRTIAELHRSRLE-- 386
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLAR--LLELQ---EEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrg 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 387 ----------VAEVNGRLAELGLHLKEEKCQWSKERagllQSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAR 456
Cdd:TIGR00618 534 eqtyaqletsEEDVYHQLTSERKQRASLKEQMQEIQ----QSFSILTQCDNRSKEDIPNLQNITVRLQDLTE----KLSE 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 457 EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNedATTEDEE 525
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL--SIRVLPK 672
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
228-548 |
2.08e-08 |
|
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: 57.93 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 ARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEvqadkeqseAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN---------ARLDLRRLFDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSAQAQRLKDKVAQMKDTLGQAQqrvAELEPLKEQLRgaqELAASSQQKATLLGEELASAAAARDRTIAELHRSRlev 387
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQ---AWLEEQKEQKR---EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGA--- 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 388 aevngrlaelglhlKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAV-------QEERTQNQVFKTELAREKDS 460
Cdd:pfam12128 746 --------------KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrQEVLRYFDWYQETWLQRRPR 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 461 SLVQLSESKRELTELRSALRVLQK---------EKEQLQEEKQ--ELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVG 529
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklrraklEMERKASEKQqvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGER 891
|
330
....*....|....*....
gi 14149742 530 LSCPAALTDSEDESPEDMR 548
Cdd:pfam12128 892 LAQLEDLKLKRDYLSESVK 910
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-526 |
2.61e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 245 LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEaELQVAQQENhhlnlDLKEAKSWQEEQSAQAQRLKDKVAQM 324
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAK-----KADEAKKAEEAKKADEAKKAEEKKKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 325 KDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHRSRLEVAEVNGRlaelglhlKEE 404
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAK--------KAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 405 KCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTELRSALRVLQK 484
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE-------EDKKKAEEAKKAEEDEKK 1689
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 14149742 485 EKEQLQEEKQEL--LEYMRKLEARLEKVADE--KWNEDATTEDEEA 526
Cdd:PTZ00121 1690 AAEALKKEAEEAkkAEELKKKEAEEKKKAEElkKAEEENKIKAEEA 1735
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-514 |
3.77e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 224
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 225 DHVARILELEDDIQTISEKVLTKEVELDRLR---DTVKALTRE--QEKLLGQLKEVQADKEQSEAELQVA-----QQENH 294
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLagLRGLAGAVAVLIGVEAAYEAALEAAlaaalQNIVV 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 295 HLNLDLKEAKSWQEEQSAQA-------QRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELA 367
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRatflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 368 SAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQN 447
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 448 QVFKTELAR-------------------------------EKDSSLVQLSESKRELTELRSALRVL-------------- 482
Cdd:COG1196 714 EERLEEELEeealeeqleaereelleelleeeelleeealEELPEPPDLEELERELERLEREIEALgpvnllaieeyeel 793
|
410 420 430
....*....|....*....|....*....|..
gi 14149742 483 QKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG1196 794 EERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-378 |
6.23e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 147 TVLQNQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEH--TELMEQYKGISRSHGEITEERDILSRQQ 223
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 224 GDHVARILELEDDIQTISEKV--LTKEVELDRLRDTVKALTREQEKLLGQLKE-----VQADKEQSEAELQVAQqenhhl 296
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvIALRAQIAALRAQLQQ------ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 297 nldlkEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRT 376
Cdd:COG3206 310 -----EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
..
gi 14149742 377 IA 378
Cdd:COG3206 385 VG 386
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-292 |
7.38e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDI--LSRQQGDH 226
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149742 227 VARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-492 |
1.21e-07 |
|
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: 55.03 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALataRQEHTELmeqykgisrshgeITEERDILSRQQg 224
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL---EEKQNEI-------------EKLKKENQSYKQ- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 225 dhvaRILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAK 304
Cdd:TIGR04523 385 ----EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 305 SWQEEQSAQAQRLKDKVAQMKDTLGQAQQ----RVAELEPLKEQLRG-AQELAASSQQKATLLG--EELASAAAARDRTI 377
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKelksKEKELKKLNEEKKElEEKVKDLTKKISSLKEkiEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 378 AELHRSRLEVAEVNGR--LAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEertqnqvfKTELA 455
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE--------KEKKI 612
|
330 340 350
....*....|....*....|....*....|....*..
gi 14149742 456 REKDSslvQLSESKRELTELRSALRVLQKEKEQLQEE 492
Cdd:TIGR04523 613 SSLEK---ELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-528 |
1.31e-07 |
|
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: 55.12 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELM-------EQYKGISRSH------------ 209
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLedsntqiEQLRKMMLSHegvlqeirsilv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 210 ------GEITEERDILS----RQQGDHVARIL-ELEDDIQTISEKVLTKEVELdrlrDTVKALTREQEKLLGQLKEVQAD 278
Cdd:pfam15921 195 dfeeasGKKIYEHDSMStmhfRSLGSAISKILrELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQHQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 279 KEQSEAELQVAqqenhhlNLDLKEAKSWQEEQSAQAQrLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaqelaassqqk 358
Cdd:pfam15921 271 QLISEHEVEIT-------GLTEKASSARSQANSIQSQ-LEIIQEQARNQNSMYMRQLSDLESTVSQLR------------ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 359 atllgEELASAAAARDRTIAELHRsrlEVAEVNGRLAElglhLKEEKCQWSKERAGLlqsveaeKDKILKLSAEILRLEK 438
Cdd:pfam15921 331 -----SELREAKRMYEDKIEELEK---QLVLANSELTE----ARTERDQFSQESGNL-------DDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 439 AVQEERTQNqvfKTELAREKDSSLV------QLSESKRELTELRSALRVLQKE-KEQLQEE------KQELLEYMRKLEA 505
Cdd:pfam15921 392 ELSLEKEQN---KRLWDRDTGNSITidhlrrELDDRNMEVQRLEALLKAMKSEcQGQMERQmaaiqgKNESLEKVSSLTA 468
|
410 420 430
....*....|....*....|....*....|
gi 14149742 506 RLE-------KVADEKWNEDATTEDEEAAV 528
Cdd:pfam15921 469 QLEstkemlrKVVEELTAKKMTLESSERTV 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-494 |
1.45e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDlkeakswqeeqsAQAQRLKDKVAQMKDTLGQA 331
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 332 QQRVAELEPLKEQLRgaQELAASSQqkatllgeelASAAAARDRTIAELhrsRLEVAEVNGRLAELGLHLKEE-----KC 406
Cdd:COG3206 232 RAELAEAEARLAALR--AQLGSGPD----------ALPELLQSPVIQQL---RAQLAELEAELAELSARYTPNhpdviAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 407 QwsKERAGLLQSVEAEKDKIL-KLSAEILRLEKAVQEERTQNQVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKE 485
Cdd:COG3206 297 R--AQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELE-AELRRLEREVEVARELYESLLQR 373
|
....*....
gi 14149742 486 KEQLQEEKQ 494
Cdd:COG3206 374 LEEARLAEA 382
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
656-679 |
1.51e-07 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 47.57 E-value: 1.51e-07
10 20
....*....|....*....|....
gi 14149742 656 CPICKERFPAESDKDALEDHMDGH 679
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
199-520 |
1.92e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 199 MEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQAD 278
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 279 KEQ-SEAELQVAQQENH--HLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVA-----------------EL 338
Cdd:PRK03918 237 KEEiEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeeyldelreiekRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 339 EPLKEQLRGAQELAASSQQKATLLgEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQS 418
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 419 VEAEK----DKILKLSAEILRLEKAVQEERTQNQ----------VFKTELAREKDSSLV-----QLSESKRELTELRSAL 479
Cdd:PRK03918 396 LEKAKeeieEEISKITARIGELKKEIKELKKAIEelkkakgkcpVCGRELTEEHRKELLeeytaELKRIEKELKEIEEKE 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 14149742 480 RVLQKEKEQLQEE---------KQELLEYMRKLEARLEKVADEKWNEDAT 520
Cdd:PRK03918 476 RKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-372 |
2.43e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGI------------------- 205
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 206 SRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKvltkEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAE 285
Cdd:COG3883 111 SESFSDFLDRLSALSKIADADADLLEELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 286 LQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEE 365
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
....*..
gi 14149742 366 LASAAAA 372
Cdd:COG3883 267 AAAGAAG 273
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
173-506 |
2.53e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 173 QVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILS----------RQQGD---HVARILELEDDIQT 239
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtalRQQEKierYQADLEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 240 ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA--DKEQSEA--------ELQVAQQENHHLNLDLKEAKSWQEE 309
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQalDVQQTRAiqyqqavqALERAKQLCGLPDLTADNAEDWLEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 310 QSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLR---GAQELAASSQQKATLLGE-----ELASAAAARDRTIAELH 381
Cdd:PRK04863 447 FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiaGEVSRSEAWDVARELLRRlreqrHLAEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 382 RSRLEVAEVNGRLAELGLH----------LKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFk 451
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRlgknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW- 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149742 452 telaREKDSSLVQLSE-------SKRELTELRSAL----RVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:PRK04863 606 ----LAAQDALARLREqsgeefeDSQDVTEYMQQLlereRELTVERDELAARKQALDEEIERLSQP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-520 |
3.84e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 185 ERALATARQEHTELMEQYKGISRSHGEITEERDILsRQQGDHVARILEL---EDDIQTISEKVLTKEVELDRLR---DTV 258
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdEIDVASAEREIAELEAELERLDassDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 259 KALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEE-QSAQAQRLKDKVAQMKDTLGQAQQRVAE 337
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 338 LEPLKEQLRGAQELAASSQQKATLL----GEELASAAAARDRTIAELHrsrlEVAEVNGRLAELGLHLKEEKcqWskerA 413
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLP----EYLALLDRLEEDGLPEYEER--F----K 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 414 GLLQsvEAEKDKILKLSAEILRLEKAVQEERTQ-NQvfktELAREK---------DSSLVQLSESKRELTELRSALRVLQ 483
Cdd:COG4913 838 ELLN--ENSIEFVADLLSKLRRAIREIKERIDPlND----SLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGAS 911
|
330 340 350
....*....|....*....|....*....|....*..
gi 14149742 484 KEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDAT 520
Cdd:COG4913 912 LFDEELSEARFAALKRLIERLRSEEEESDRRWRARVL 948
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
228-400 |
4.26e-07 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 52.43 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 ARILELEDDIQTISEKVLTKEVELDRLRdtvkALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQAELDRLQ----ALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSAQAQRL---KDKVAQMKDTLGQAQQRVAELEPLKEQLrgAQELAAssQQKATLLGEELASAAAARDRTIAELHRSR 384
Cdd:pfam00529 134 PIGGISRESLvtaGALVAQAQANLLATVAQLDQIYVQITQS--AAENQA--EVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
170
....*....|....*..
gi 14149742 385 LEV-AEVNGRLAELGLH 400
Cdd:pfam00529 210 TEIrAPVDGTVAFLSVT 226
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-528 |
4.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQgdHVA 228
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAE---LQVAQQENHHLNLDLKEAKS 305
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKALLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 306 WQEEQSAQAQRLKDKV-------AQMKDTLGQAQQRVAeLEPLKEQLRGAQELAASSQQKATLLGEELASAAA--ARDRT 376
Cdd:TIGR02168 514 NQSGLSGILGVLSELIsvdegyeAAIEAALGGRLQAVV-VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEiqGNDRE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 377 IAELHRSRLEVAE------------VNGRLAEL--------GLHL-KEEKCQW-------------------SKERAGLL 416
Cdd:TIGR02168 593 ILKNIEGFLGVAKdlvkfdpklrkaLSYLLGGVlvvddldnALELaKKLRPGYrivtldgdlvrpggvitggSAKTNSSI 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 417 QSVEAEKD----KILKLSAEILRLEKAVQEERTQNQVFKTELA---REKDSSLVQLSESKRELTELRSALRVLQKEKEQL 489
Cdd:TIGR02168 673 LERRREIEeleeKIEELEEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
410 420 430
....*....|....*....|....*....|....*....
gi 14149742 490 QEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 528
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-523 |
5.64e-07 |
|
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: 53.10 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELEralatarqehtelmeqyKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE-----------------QQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISekvlTKEVELDRLRDTVKALTREQEKLLGQLKEVQAD--------------KEQSEAEL-----QVA 289
Cdd:TIGR04523 108 INSEIKNDKEQKN----KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyndlkkqKEELENELnllekEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 290 QQEN------------HHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQrvaELEPLKEQLRGAQelaassQQ 357
Cdd:TIGR04523 184 NIQKnidkiknkllklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQ------TQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 358 KATLLGEElasaaaarDRTIAELHRSRLEVAEVNGRLAELG----------LHLKEEKCQ-WSKERAGLLQSVEAEKD-- 424
Cdd:TIGR04523 255 LNQLKDEQ--------NKIKKQLSEKQKELEQNNKKIKELEkqlnqlkseiSDLNNQKEQdWNKELKSELKNQEKKLEei 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 425 ---------KILKLSAEILRLEKAVQEERTQNQVFKTELA----------REKDSSLVQLSESKRELTELRSALRVLQKE 485
Cdd:TIGR04523 327 qnqisqnnkIISQLNEQISQLKKELTNSESENSEKQRELEekqneieklkKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430
....*....|....*....|....*....|....*...
gi 14149742 486 KEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTED 523
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-514 |
7.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 317 LKDKVAQMKDTLGQAQQR-----VAELEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHRSRLEVAEVN 391
Cdd:COG4717 47 LLERLEKEADELFKPQGRkpelnLKELKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 392 GRLAELGLHLKEEKCQwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRE 471
Cdd:COG4717 123 KLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14149742 472 LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
152-514 |
1.00e-06 |
|
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: 52.15 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEGQVTELRSRV-QELERALA--TARQEHTELMEQYKG------ISRSHGEitEERDILSRQ 222
Cdd:pfam12128 277 RQEERQETSAELNQLLRTLDDQWKEKRDELnGELSAADAavAKDRSELEALEDQHGafldadIETAAAD--QEQLPSWQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 223 QGDHVARILE-LEDDIQTISEKvlTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE-NHHLNLDL 300
Cdd:pfam12128 355 ELENLEERLKaLTGKHQDVTAK--YNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 301 KEAKSWQEEQSAQAQRLKDKVAQM---KDTLGQAQQRVAELEPLKEqlrgAQELAASSQQKATLlgeELASAAAARDRTI 377
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERARE----EQEAANAEVERLQS---ELRQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 378 AELHRSRLEVAEVNGRLAELGL-----------HLKEEKCQWSKERAGLLQS------------VEAEKDKILKL----- 429
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELqlfpqagtllhFLRKEAPDWEQSIGKVISPellhrtdldpevWDGSVGGELNLygvkl 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 430 ------------SAEILRLEKAVQEERTQNQvfkTELAREKDSSLVQLS----ESKRELTELRSA-------LRVLQKEK 486
Cdd:pfam12128 586 dlkridvpewaaSEEELRERLDKAEEALQSA---REKQAAAEEQLVQANgeleKASREETFARTAlknarldLRRLFDEK 662
|
410 420
....*....|....*....|....*....
gi 14149742 487 EQLQEEKQELL-EYMRKLEARLEKVADEK 514
Cdd:pfam12128 663 QSEKDKKNKALaERKDSANERLNSLEAQL 691
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
258-512 |
1.01e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 258 VKALTREQEKLLGQLKEVQADKEQSE--AELQVAQQENHHLNLDLKEAkswqEEQSAQAQRLKDkvaQMKDTLGQAQQRV 335
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERY----EEQREQARETRD---EADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 336 AELEPLKEQLRGAQELAASSQQKATLLGEELASA-------AAARDRTIAELHRSRLEVAEVNGRLAElgLHLKEEKCQW 408
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLrerleelEEERDDLLAEAGLDDADAEAVEARREE--LEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 409 SKERAGLlqSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKE--- 485
Cdd:PRK02224 329 RLEECRV--AAQAHNEEAESLREDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERfgd 402
|
250 260 270
....*....|....*....|....*....|....*...
gi 14149742 486 -----------KEQLQEEKQELLEYMRKLEARLEKVAD 512
Cdd:PRK02224 403 apvdlgnaedfLEELREERDELREREAELEATLRTARE 440
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
149-513 |
1.15e-06 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 52.00 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELerALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQtisekvltkevELDRLRDTVKALTREQEKLLGQLKEVQAD-KEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:COG4192 117 AVADLRNLLQ-----------QLDSLLTQRIALRRRLQELLEQINWLHQDfNSELTPLLQEASWQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSA--QAQRLKDKVAQMKDTLGQ-AQQR-VAELEPLKEQLrgaQELAASSQQKATLLGEelASAAAARDRTIAELhrs 383
Cdd:COG4192 186 NLQNElqLLLRLLAIENQIVSLLREvAAARdQADVDNLFDRL---QYLKDELDRNLQALKN--YPSTITLRQLIDEL--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 384 rLEVAEVNGRLAEL---GLHLKEEkcqwskeraglLQSVEAEKDKILKLSAEilRLEKAVQEERTQNQVFKTELAREKDS 460
Cdd:COG4192 258 -LAIGSGEGGLPSLrrdELAAQAT-----------LEALAEENNSILEQLRT--QISGLVGNSREQLVALNQETAQLVQQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 461 S------------------------------LVQLSES-----------------KRELTELRSALRV-LQKEKEQLQEE 492
Cdd:COG4192 324 SgilllaiallslllavlinyfyvrrrlvkrLNALSDAmaaiaagdldvpipvdgNDEIGRIARLLRVfRDQAIEKTQEL 403
|
410 420
....*....|....*....|.
gi 14149742 493 KQELLEYMRkLEARLEKVADE 513
Cdd:COG4192 404 ETEIEERKR-IEKNLRQTQDE 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-292 |
1.16e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGIS-RSHGEITEERDILSRQQGDHVARI 230
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14149742 231 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
165-525 |
1.47e-06 |
|
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: 51.90 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 165 QLKLQLEGQVTELRSRVQELERALATARQEhteLMEQYKGISRshgeiTEERDILSRQQGDHV--ARILELEDDIQTISE 242
Cdd:pfam02463 668 LSELTKELLEIQELQEKAESELAKEEILRR---QLEIKKKEQR-----EKEELKKLKLEAEELlaDRVQEAQDKINEELK 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 243 KVLTK--EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHH-LNLDLKEAKSWQEEQSAQAQRLKd 319
Cdd:pfam02463 740 LLKQKidEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEkLKAQEEELRALEEELKEEAELLE- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 320 kvAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAA------AARDRTIAELHRSRLEVAEVNGR 393
Cdd:pfam02463 819 --EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEllqellLKEEELEEQKLKDELESKEEKEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 394 LAELGLHLKEEKCQWSKERAGLLQSVEAEKDKIL-KLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKREL 472
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAEILlKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 473 TELRSALRVLQK-------EKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEE 525
Cdd:pfam02463 977 LMAIEEFEEKEErynkdelEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKV 1036
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-517 |
3.53e-06 |
|
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: 50.35 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQvAQQENHHLNLDLKEAKSWQEEQS 311
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 312 AQAQRLKDKVAQMKDTLGQAQQR---VAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVA 388
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 389 -----EVNGRLAELGLHLKEEKCQWSKERAGLLQSVE-----AEKDKILKLSAEILRLEKAVQEERTQNQ--------VF 450
Cdd:TIGR00618 350 lhsqeIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttlTQKLQSLCKELDILQREQATIDTRTSAFrdlqgqlaHA 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 451 KTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQEL--LEYMRKLEARLEKVADEKWNE 517
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtKEQIHLQETRKKAVVLARLLE 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-498 |
4.15e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 206 SRSHGEITEERDILSRQQ--GDHVARILELEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEVQADKEQSE 283
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEE-------ELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 284 AELQVAQQENHHLNLdlkeakswqEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLG 363
Cdd:COG4913 659 DEIDVASAEREIAEL---------EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 364 EELASAAAARDRTIAELHRSRLEvaevnGRLAELGLhlkeekcqwSKERAGLLQSVEAEKDkilKLSAEILRLEKAVQEE 443
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLE-----ERFAAALG---------DAVERELRENLEERID---ALRARLNRAEEELERA 792
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 14149742 444 RTQ-NQVFKTELArEKDSSLVQLSESKRELTELR-SAL-RVLQKEKEQLQEEKQELLE 498
Cdd:COG4913 793 MRAfNREWPAETA-DLDADLESLPEYLALLDRLEeDGLpEYEERFKELLNENSIEFVA 849
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-508 |
6.84e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEiTEERDILSRQQGDHVA 228
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE-AEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RilELEDDIQTISEKVLTKEVELDRLRdtvkALTREQEKLLGQLKEVQADKEQSEAELQVAQQ---------ENHHLNLD 299
Cdd:pfam01576 468 S--QLQDTQELLQEETRQKLNLSTRLR----QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlsdmkkklEEDAGTLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 300 LKEA--KSWQEEQSAQAQRLKDKVAQMkDTLGQAQQRV-AELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRT 376
Cdd:pfam01576 542 ALEEgkKRLQRELEALTQQLEEKAAAY-DKLEKTKNRLqQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARY 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 377 IAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSK-ERAGLLQSVEAE-----KDKILKLSAEILR----LEKAVQEERTQ 446
Cdd:pfam01576 621 AEERDRAEAEAREKETRALSLARALEEALEAKEElERTNKQLRAEMEdlvssKDDVGKNVHELERskraLEQQVEEMKTQ 700
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 447 NQVFKTELAREKDSSL---VQLSESKRELTelrsalRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:pfam01576 701 LEELEDELQATEDAKLrleVNMQALKAQFE------RDLQARDEQGEEKRRQLVKQVRELEAELE 759
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-506 |
7.52e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 147 TVLQNQLD-------ESQQERNDLMQLKLQLEGQVTELRSRVQELERalaTARQEHTELMEQYKGISRSHGEITEERDIL 219
Cdd:pfam01576 43 NALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEE---RSQQLQNEKKKMQQHIQDLEEQLDEEEAAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 220 SRQQGDHV---ARILELEDDIQTISEK--VLTKEVEL--DRLRDTVKALTREQEKlLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:pfam01576 120 QKLQLEKVtteAKIKKLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEK-AKSLSKLKNKHEAMISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 293 NHHLNLDLKEAKSWQEEQSAQAQ-RLKDKVAQMKDTLGQAQQRVAELEPLkeQLRGAQELAASSQQKATL---------L 362
Cdd:pfam01576 199 EEKGRQELEKAKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAA--LARLEEETAQKNNALKKIreleaqiseL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 363 GEELASAAAARDRtiAELHRSRLEvaevngrlaelglhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQE 442
Cdd:pfam01576 277 QEDLESERAARNK--AEKQRRDLG----------------EELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEE 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149742 443 ERTQNQVFKTELAREKDSSLVQLSEskrELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:pfam01576 339 ETRSHEAQLQEMRQKHTQALEELTE---QLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-289 |
1.06e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.83 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 147 TVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALA----TARQEHTELMEQYKGISRSHGEITEE------- 215
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAElerlqee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 216 ----RDILSRQQGDHVARILELEDDIQTISEKVLTK------EVELD-RLRD----------TVKALTREQEKLLGQLK- 273
Cdd:pfam09787 123 lrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqssssQSELEnRLHQltetliqkqtMLEALSTEKNSLVLQLEr 202
|
170
....*....|....*..
gi 14149742 274 -EVQADKEQSEAELQVA 289
Cdd:pfam09787 203 mEQQIKELQGEGSNGTS 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-526 |
1.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 171 EGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHgEITEERDILSRQQGDHVARILELE--DDIQTISEKVLTKE 248
Cdd:PTZ00121 1132 EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR-KAEDAKKAEAARKAEEVRKAEELRkaEDARKAEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 249 VeldrlRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAK-----SWQEEQSAQAQRLKDKVAQ 323
Cdd:PTZ00121 1211 E-----RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfaRRQAAIKAEEARKADELKK 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 324 MK-----DTLGQAQQ--RVAELEPLKEQLRGAQEL---AASSQQKATLLGE--ELASAAAARDRTIAELHRSRLEVAEVN 391
Cdd:PTZ00121 1286 AEekkkaDEAKKAEEkkKADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 392 GRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRE 471
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 472 LTELRSalrvlQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 526
Cdd:PTZ00121 1446 ADEAKK-----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
219-508 |
1.21e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 219 LSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKE-------VQADKEQSEAELQVAQQ 291
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElneqlqaAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 292 ENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkeqlrgaQELAASSQQKATLLGEELASAAA 371
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE---------EQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 372 ARDRTIAELhrsrleVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:COG4372 180 EAEQALDEL------LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 14149742 452 TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-492 |
1.74e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 171 EGQVTELRSRVQELERALATARQEHTELMEQYKgisrshgEITEERDILSRqqgdHVARILELEDDiqTISEKVLTKEVE 250
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSALNR----LLPRLNLLADE--TLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 251 LDRLRDTvKALTREQEKLLGQLkevqadkEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDkVAQMKDTLG- 329
Cdd:PRK04863 903 LDEAEEA-KRFVQQHGNALAQL-------EPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTE-VVQRRAHFSy 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 330 -QAQQRVAELEPLKEQLRGAQELAassQQKATLLGEELASAAA-ARDRT------IAELHRSRLEVAEVNGRLAELGLHL 401
Cdd:PRK04863 974 eDAAEMLAKNSDLNEKLRQRLEQA---EQERTRAREQLRQAQAqLAQYNqvlaslKSSYDAKRQMLQELKQELQDLGVPA 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 402 KEEkcqwSKERAGLLQSveaekdkilklsaeilRLEKAVQEERTQnqvfktelareKDSSLVQLSESKRELTELRSALRV 481
Cdd:PRK04863 1051 DSG----AEERARARRD----------------ELHARLSANRSR-----------RNQLEKQLTFCEAEMDNLTKKLRK 1099
|
330
....*....|.
gi 14149742 482 LQKEKEQLQEE 492
Cdd:PRK04863 1100 LERDYHEMREQ 1110
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
158-525 |
2.07e-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: 47.79 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 158 QERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGIS-RSHGEITEERDILSRQQGD-HVARILEleD 235
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlKLEEEIQENKDLIKENNATrHLCNLLK--E 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 236 DIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENH----HLNLDLKEAKSWQEEQ- 310
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHekiqHLEEEYKKEINDKEKQv 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 311 SAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEV 390
Cdd:pfam05483 243 SLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 391 NGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSaEILRLEKA-VQEERTQNQVFKTELaREKDSSLVQLSESK 469
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQrLEKNEDQLKIITMEL-QKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 470 R----ELTELRSAL----------RVLQKEKEQLQEEKQELLEYmrkLEARLEKVADEKWNEDATTEDEE 525
Cdd:pfam05483 401 NnkevELEELKKILaedeklldekKQFEKIAEELKGKEQELIFL---LQAREKEIHDLEIQLTAIKTSEE 467
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-518 |
3.00e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 245 LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNL-DLKEAKSWQEEQSAQAQRLKDKVAQ 323
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 324 MKdtlgQAQQRVAELEPLK-EQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEV--AEVNGRLAELGLh 400
Cdd:PTZ00121 1607 MK----AEEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkAEEDKKKAEEAK- 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 401 lKEEKCQWSKERAGLLQSVEAEK-DKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTELRsal 479
Cdd:PTZ00121 1682 -KAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE-------EDKKKAEEAK--- 1750
|
250 260 270
....*....|....*....|....*....|....*....
gi 14149742 480 rVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNED 518
Cdd:PTZ00121 1751 -KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
241-513 |
3.02e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 241 SEKVLTKEVELdrlRDTVKALTREQEKLL---GQLKEVQADKEQSEAELQVAqqeNHHLNLDLkeakswqeeqsaQAQRL 317
Cdd:COG3096 284 SERALELRREL---FGARRQLAEEQYRLVemaRELEELSARESDLEQDYQAA---SDHLNLVQ------------TALRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 318 KDKVAQMKDTLGQAQQRVAE----LEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHR---------SR 384
Cdd:COG3096 346 QEKIERYQEDLEELTERLEEqeevVEEAAEQLAEAEARLEAAEEEV----DSLKSQLADYQQALDVQQTraiqyqqavQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 385 LEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLS-------AEILRLEKAVQEERTQNQVFKT----- 452
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAdaarrqfEKAYELVCKIAGEVERSQAWQTarell 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149742 453 ELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQE----------EKQELLEYMRKLEARLEKVADE 513
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcqrigqqldAAEELEELLAELEAQLEELEEQ 572
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-525 |
3.15e-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: 47.48 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 162 DLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHgeiteERDILSR-QQGDHVARIL--------- 231
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF-----ERDLQARdEQGEEKRRQLvkqvrelea 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTK---EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQseaelqvaqqenhhLNLDLKEAKSWQE 308
Cdd:pfam01576 757 ELEDERKQRAQAVAAKkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD--------------LQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQlrgaqelaasSQQKATLLGEELASAAAARDRTIAElhRSRLEva 388
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ----------AQQERDELADEIASGASGKSALQDE--KRRLE-- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 389 evnGRLAELGLHLKEEKCqwskeragllqSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfKTELAREKDSSlvQLSES 468
Cdd:pfam01576 889 ---ARIAQLEEELEEEQS-----------NTELLNDRLRKSTLQVEQLTTELAAERSTSQ--KSESARQQLER--QNKEL 950
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 469 KRELTELRSALRVLQKE------------KEQLQEEKQElleymRKLEARLEKVADEKWNEDATTEDEE 525
Cdd:pfam01576 951 KAKLQEMEGTVKSKFKSsiaaleakiaqlEEQLEQESRE-----RQAANKLVRRTEKKLKEVLLQVEDE 1014
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-528 |
3.52e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 375 RTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTEL 454
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELE----DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 455 -----AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 528
Cdd:COG1579 83 gnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
158-492 |
3.72e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.21 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 158 QERNDLMQLKLQLEGQVTELRSR----VQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQqgdhvariLEL 233
Cdd:pfam15964 307 KERDDLMSALVSVRSSLAEAQQRessaYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKE--------LAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 234 EDDIQTISEKVLTKEVELDR--LRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQS 311
Cdd:pfam15964 379 QQEKRAQEKEALRKEMKKEReeLGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 312 AQAQRLKDKVAQ-----MKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLE 386
Cdd:pfam15964 459 NQTKMKKDEAEKehreyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLE 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKA----VQEERTQNQVFKTELAREKDSSL 462
Cdd:pfam15964 539 KESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTfiakLKEECCTLAKKLEEITQKSRSEV 618
|
330 340 350
....*....|....*....|....*....|
gi 14149742 463 VQLSESKRELTElrsALRVLQKEKEQLQEE 492
Cdd:pfam15964 619 EQLSQEKEYLQD---RLEKLQKRNEELEEQ 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-527 |
4.14e-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: 47.09 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTiSEKVLTKEVELDRLRDTVKALTREQ-EKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:pfam01576 188 MISDLEERLKK-EEKGRQELEKAKRKLEGESTDLQEQiAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 EEQSAQAQRLKDKVAQMKDTLGQAQQRV----AELEPLKEQLR-------GAQELAASSQQKATLLGEELASAAAARDRT 376
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRrdlgEELEALKTELEdtldttaAQQELRSKREQEVTELKKALEEETRSHEAQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 377 IAELHR----------SRLEVAEVN-GRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLE-KAVQEER 444
Cdd:pfam01576 347 LQEMRQkhtqaleeltEQLEQAKRNkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQaRLSESER 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 445 TQNQ----VFKTELAREKDSSLVQLSESK--RELTELRSALRVLQKEKEQLQEEKQELLeymrKLEARLEKVADEKWNED 518
Cdd:pfam01576 427 QRAElaekLSKLQSELESVSSLLNEAEGKniKLSKDVSSLESQLQDTQELLQEETRQKL----NLSTRLRQLEDERNSLQ 502
|
....*....
gi 14149742 519 ATTEDEEAA 527
Cdd:pfam01576 503 EQLEEEEEA 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-345 |
4.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 151 NQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILsrqqgdhvar 229
Cdd:PRK02224 522 EELIAERRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL---------- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 230 ileleDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENhhLNLDLKEAKSWQEE 309
Cdd:PRK02224 592 -----ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE--AREDKERAEEYLEQ 664
|
170 180 190
....*....|....*....|....*....|....*.
gi 14149742 310 QSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQL 345
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-288 |
4.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQ----------------VTELRSRVQELERALATARQEHTE-------LMEQYKG- 204
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQlgsgpdalpellqspvIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAAl 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 205 -------ISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKvltkEVELDRLRDTVKALTREQEKLLGQLKEVQA 277
Cdd:COG3206 304 raqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
170
....*....|.
gi 14149742 278 DKEQSEAELQV 288
Cdd:COG3206 380 AEALTVGNVRV 390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-524 |
4.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 176 ELRsRVQELERALATARQEHTELMEQYKGISRSHgEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLR 255
Cdd:PTZ00121 1192 ELR-KAEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 256 DTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLK---EAKSWQEEQSAQAQRLKDKVAQMKDtlgQAQ 332
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadEAKKKAEEAKKKADAAKKKAEEAKK---AAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 333 QRVAELEPLKEQLRGAQELAASSQQKATllgEELASAAAARDRtiAELHRSRLEV---AEVNGRLAElglHLKEEKCQWS 409
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKE---EAKKKADAAKKK--AEEKKKADEAkkkAEEDKKKAD---ELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 410 KERAGLLQSVEAEKDKILKLSAEILR----LEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKE 485
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 14149742 486 KEQLQ--EEKQELLEYMRKLEARleKVADE-KWNEDATTEDE 524
Cdd:PTZ00121 1499 ADEAKkaAEAKKKADEAKKAEEA--KKADEaKKAEEAKKADE 1538
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-514 |
4.80e-05 |
|
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: 46.66 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 155 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQ----EHTELMEQYKGISRSHGEITEERDILSRQqgdhVARI 230
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldrESDRNQELQKRIRLLEKREAEAEEALREQ----AELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 231 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQ 310
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 311 SAQAQRLKDKVAQMKD----------------TLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARD 374
Cdd:pfam05557 159 EKQQSSLAEAEQRIKElefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 375 RtiaeLHRSRLEVAEVNGRLAELGLHLKEekcqWSKeragLLQSVEAEKDKILKLSAEILRLEkavQEERTqnqvfkteL 454
Cdd:pfam05557 239 R----EEKYREEAATLELEKEKLEQELQS----WVK----LAQDTGLNLRSPEDLSRRIEQLQ---QREIV--------L 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 455 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKER 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
250-542 |
4.99e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 ELDRLRDTVKALTREQE---KLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQ---------RL 317
Cdd:COG4717 72 ELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 318 KDKVAQMKDTLGQAQQRVAELEPLKEQL-RGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 397 L--GLHLKEEKCQWSKER-----AGLLQSVEAEKDKILKLSAEILRLEKAVQE----ERTQNQVFKTELAREKDSSLVQL 465
Cdd:COG4717 232 LenELEAAALEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149742 466 SESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVadEKWNEDATTEDEEAAVGLSCPAALTDSEDE 542
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-507 |
5.25e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQwsKE 411
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 412 RAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTELRSALRVLQKEKEQLQE 491
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|....*.
gi 14149742 492 EKQELLEymrKLEARL 507
Cdd:COG1579 164 EREELAA---KIPPEL 176
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-444 |
5.33e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQE 308
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVA 388
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 14149742 389 EVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEER 444
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
309-596 |
9.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELhRSRLEVA 388
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 389 EVNGRLAELGLHLKEekcqwSKERAGLLQSVEAeKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSES 468
Cdd:COG3883 96 YRSGGSVSYLDVLLG-----SESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 469 KRELTELRSALRVLQKE-KEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDSEDESPEDM 547
Cdd:COG3883 170 KAELEAQQAEQEALLAQlSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 14149742 548 RLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSD 596
Cdd:COG3883 250 GAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGA 298
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
250-397 |
1.04e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKswqeeqsAQAQRLKDKVAQMKDT-- 327
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 328 -------LGQAQQRVAELE----PLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRsrlEVAEVNGRLAE 396
Cdd:COG1579 91 yealqkeIESLKRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAEREE 167
|
.
gi 14149742 397 L 397
Cdd:COG1579 168 L 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
232-526 |
1.09e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQAdkeqseaELQVAQQENHHLNLDLKEAKSWQEEQS 311
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 312 AQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaasSQQKATLLGEElasaaaarDRTIAElhrsrlevaevn 391
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEW----RQQTEVLSPEE--------EKELVE------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 392 gRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfKTELAREKDSSLVQLSESKRE 471
Cdd:COG1340 141 -KIKEL------------EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK----IKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14149742 472 LTELRSALRVLQKEKEQLQEE-----------KQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 526
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKadelheeiielQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-548 |
1.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEER--DILSRQ 222
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkaDEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 223 QGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKAltREQEKLLGQLKEVQADKEQSEAELQVAQQENhhlnldLKE 302
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------ADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 303 AKSWQEEQSAQAQRLKDKVAQMK--DTLGQAQQRVAELEPLK---EQLRGAQELAASSQQK-----ATLLGEELASAAAA 372
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAkkaeeAKKKAEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 373 RDRtiAELHRSRLEV---AEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKA--VQEERTQN 447
Cdd:PTZ00121 1476 KKK--AEEAKKADEAkkkAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKKADEAKKAEEAKKADEAkkAEEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 448 QVFKTE---LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDE 524
Cdd:PTZ00121 1550 ELKKAEelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
410 420
....*....|....*....|....
gi 14149742 525 EAAVGLSCPAALTDSEDESPEDMR 548
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
226-508 |
1.15e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 226 HVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLgqlkevqadkeqseAELQVAQQENHHLnldlkeakS 305
Cdd:PRK10246 193 HKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLL--------------TAQQQQQQSLNWL--------T 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 306 WQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLK--EQLRGA----QELAAS---SQQKATLLGEELASAAAARDRT 376
Cdd:PRK10246 251 RLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHweriQEQSAAlahTRQQIEEVNTRLQSTMALRARI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 377 IAELHRSRLEVAEVNGRLAELgLHLKEEKCQWSKERAG---LLQSVEAEKDKILKLSAeilRLEKAVQEERTQNQVFKTE 453
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTW-LAEHDRFRQWNNELAGwraQFSQQTSDREQLRQWQQ---QLTHAEQKLNALPAITLTL 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 14149742 454 LAREKDSSLVQLSES---KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:PRK10246 407 TADEVAAALAQHAEQrplRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
276-388 |
1.24e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.72 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 276 QADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAAS- 354
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIg 136
|
90 100 110
....*....|....*....|....*....|....*.
gi 14149742 355 --SQQKATLLGEELASAAAARDRTIAELHRSRLEVA 388
Cdd:pfam00529 137 giSRESLVTAGALVAQAQANLLATVAQLDQIYVQIT 172
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-529 |
1.39e-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: 45.34 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHT-ELMEQYKGISRSHGEITEERDI----- 218
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKEREQQLQTKeqihl 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 219 -LSRQQGDHVARILELEDDIQTISEKVLTKEVE-------------LDRLRDTVKALTREQEKLLGQL----KEVQADKE 280
Cdd:TIGR00618 484 qETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLtserKQRASLKE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 281 QSEAELQ----VAQQEN-----------------HHLNLDLKEAKSWQEEQSAQAQRLKDKVA--QMKDTLGQAQQRVAE 337
Cdd:TIGR00618 564 QMQEIQQsfsiLTQCDNrskedipnlqnitvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELAL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 338 LEPLKEQL-------RGAQELAASSQQKATLLGEELASAAAARDRtIAELHRSRLEVAEVNGRLAELGLHLKE---EKCQ 407
Cdd:TIGR00618 644 KLTALHALqltltqeRVREHALSIRVLPKELLASRQLALQKMQSE-KEQLTYWKEMLAQCQTLLRELETHIEEydrEFNE 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 408 WSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE 487
Cdd:TIGR00618 723 IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK 802
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 14149742 488 QLQEE-KQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVG 529
Cdd:TIGR00618 803 TLEAEiGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
213-527 |
1.50e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 213 TEERDILSRQQGDHVARILELEDDIQTI---SEKVLTKEVELDRlRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVA 289
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEklgENAESSKRLNENA-NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 290 QQEnhhLNLDLKEAKSwqeEQSAQAQRLKDKVAQMKDTLgqaQQRVAELEPLKEQLRGAQELAASSqqkatllgEELASA 369
Cdd:COG5185 320 AAE---AEQELEESKR---ETETGIQNLTAEIEQGQESL---TENLEAIKEEIENIVGEVELSKSS--------EELDSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 370 AAARDRTIAELHRSRLEVAEVNGRLAE-----LGLHLKEEKcQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEER 444
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGYAQEILAtledtLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 445 TQNQVfktelarekdsslvqlSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK---VADEKWNEDATT 521
Cdd:COG5185 462 QSRLE----------------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERqleGVRSKLDQVAES 525
|
....*.
gi 14149742 522 EDEEAA 527
Cdd:COG5185 526 LKDFMR 531
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
242-506 |
1.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 242 EKVLTKEVELDRLRdtvkaltREQEKLLGQLKEVQADKEQSEAELQvaQQENhhLNLDLKEAKSWQEEQSAQAQRLKDKV 321
Cdd:PRK03918 148 EKVVRQILGLDDYE-------NAYKNLGEVIKEIKRRIERLEKFIK--RTEN--IEELIKEKEKELEEVLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 322 AQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGE---ELASAAAARDRTIAELHRSRLEVAEVNG------ 392
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEkaeeyi 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 393 RLAELGLHLKEEKCQWSKERAGL---LQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKT-----ELAREKDSSLVQ 464
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLeeeINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhelyEEAKAKKEELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 14149742 465 LSESKRELT--ELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:PRK03918 377 LKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
149-511 |
1.69e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQ---GD 225
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQsslAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 226 HVARILELEDDIQT-ISEKVLTK------------EVELDRLRDTVKALTR--------------------EQEKLLGQL 272
Cdd:pfam05557 168 AEQRIKELEFEIQSqEQDSEIVKnskselaripelEKELERLREHNKHLNEnienklllkeevedlkrkleREEKYREEA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 273 KEVQADKEQSEAELQ--VAQQENHHLNLDLKEAKSWQ------------EEQSAQAQRLKDKVAQMKDTLGQAQQRVAEL 338
Cdd:pfam05557 248 ATLELEKEKLEQELQswVKLAQDTGLNLRSPEDLSRRieqlqqreivlkEENSSLTSSARQLEKARRELEQELAQYLKKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 339 EPLKEQLRGAQELAASSQQKATLLGEE----------------LASAAAARDRTIAELH-------------RSRLEVAE 389
Cdd:pfam05557 328 EDLNKKLKRHKALVRRLQRRVLLLTKErdgyrailesydkeltMSNYSPQLLERIEEAEdmtqkmqahneemEAQLSVAE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 390 VNGRLAELGLHLKEEKCQWSKERAGLL-QSVEAEKDKILKLSAEILRLEkaVQEERTQNQVFKTELARE--------KDS 460
Cdd:pfam05557 408 EELGGYKQQAQTLERELQALRQQESLAdPSYSKEEVDSLRRKLETLELE--RQRLREQKNELEMELERRclqgdydpKKT 485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 14149742 461 SLVQLSESKRELtelrsALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 511
Cdd:pfam05557 486 KVLHLSMNPAAE-----AYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-496 |
1.71e-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: 44.96 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 103 VNRQGQVCGQSPPFQFREPRPMDElVTLEEADGGSDILLVVPKATVLQNQLDESQQerndLMQLKLQLEGQVTELRSRVQ 182
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCG-SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ----LETSEEDVYHQLTSERKQRA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 183 ELERALATARQEHTELMEQYKGISRSHGEITEERDILsRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALT 262
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 263 REQEKLLgqlkevqADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSA--QAQRLKDKVAQMKDTLGQAQQRVAELEP 340
Cdd:TIGR00618 639 QELALKL-------TALHALQLTLTQERVREHALSIRVLPKELLASRQLAlqKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 341 -LKEQLRGAQELA-ASSQQKATLLGEELASA-----------AAARDRTIAELHRSRLEVAEVNgRLAELGlHLKEEKCQ 407
Cdd:TIGR00618 712 hIEEYDREFNEIEnASSSLGSDLAAREDALNqslkelmhqarTVLKARTEAHFNNNEEVTAALQ-TGAELS-HLAAEIQF 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 408 WSKERA---GLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNqvFKTELaREKDSSLVQLSESKRELTELRSALRVLQK 484
Cdd:TIGR00618 790 FNRLREedtHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ--FLSRL-EEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
410
....*....|..
gi 14149742 485 EKEQLQEEKQEL 496
Cdd:TIGR00618 867 EQAKIIQLSDKL 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
141-593 |
1.79e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 141 LVVPKATvLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELEralatarQEHTELMEQYKGISRSHGEITEERDILs 220
Cdd:pfam15921 588 MQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-------LEKVKLVNAGSERLRAVKDIKQERDQL- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 221 rqqgdhVARILELEDDIQTISEKVltkEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLnldL 300
Cdd:pfam15921 659 ------LNEVKTSRNELNSLSEDY---EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA---M 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 301 KEAKSWQEEQSAQAqrlkdkvaqmkdtlGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAEL 380
Cdd:pfam15921 727 KVAMGMQKQITAKR--------------GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 381 HRSRLEVAEVNGRLAELGLHLKEEKCQWSkERAGLLQSVEAEKDKiLKL-----------------SAEILRLEKAVQEE 443
Cdd:pfam15921 793 EVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQEQESVR-LKLqhtldvkelqgpgytsnSSMKPRLLQPASFT 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 444 RTQNQVFKTE-----LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNED 518
Cdd:pfam15921 871 RTHSNVPSSQstasfLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESS 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 519 ATTEDEEAAVGLSCPAALTDSEDESPEDMRLPPyglCERGDPGSSPAGPREASPLVVIS---------QPAPISPHLSGP 589
Cdd:pfam15921 951 LRSDICHSSSNSLQTEGSKSSETCSREPVLLHA---GELEDPSSCFTFPSTASPSVKNSasrsfhsspKKSPVHSLLTSS 1027
|
....
gi 14149742 590 AEDS 593
Cdd:pfam15921 1028 AEGS 1031
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-492 |
1.93e-04 |
|
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: 44.94 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 171 EGQVTELRSRVQELERALATARQEHTELMEQYKgisrshgEITEERDILSRQQG--------DHVARILELEDDIQTISE 242
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKLLPqanlladeTLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 243 K---VLTKEVELDRLRDTVKALTREQEkllgQLKEVQADKEQSEAELQVAQQENHHLN--LDLKEAKSWQEEQSAQAQRl 317
Cdd:COG3096 908 AqafIQQHGKALAQLEPLVAVLQSDPE----QFEQLQADYLQAKEQQRRLKQQIFALSevVQRRPHFSYEDAVGLLGEN- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 318 KDKVAQMKDTLGQAQQrvaELEPLKEQLRGAQELAASSQQKATllgeELASAAAARDRTIAELHRsrlevaevngRLAEL 397
Cdd:COG3096 983 SDLNEKLRARLEQAEE---ARREAREQLRQAQAQYSQYNQVLA----SLKSSRDAKQQTLQELEQ----------ELEEL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 398 GLHLKEEkcqwSKERAgllqsvEAEKDKIlklsaeilrlekavQEERTQNQVFKTELarEKdsslvQLSESKRELTELRS 477
Cdd:COG3096 1046 GVQADAE----AEERA------RIRRDEL--------------HEELSQNRSRRSQL--EK-----QLTRCEAEMDSLQK 1094
|
330
....*....|....*
gi 14149742 478 ALRVLQKEKEQLQEE 492
Cdd:COG3096 1095 RLRKAERDYKQEREQ 1109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
231-526 |
1.94e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 231 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnhhlnldLKEAKSWQEEQ 310
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 311 SAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRS----RLE 386
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQleslQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLS 466
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14149742 467 ESKRELTELRSALRVLQKEKE--QLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 526
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAilVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-448 |
2.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 234 EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQ 313
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 314 AQR--------------------------LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELA 367
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 368 SAAAARDRTIAELhrsRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQN 447
Cdd:COG3883 175 AQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
.
gi 14149742 448 Q 448
Cdd:COG3883 252 A 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
180-527 |
2.22e-04 |
|
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: 44.78 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 180 RVQELERALATARQEHTELMEqykgISRSHGEITEERDILSRQQgdhvaRILELEDDiQTISEKvltkevelDRLRDTVK 259
Cdd:pfam01576 620 YAEERDRAEAEAREKETRALS----LARALEEALEAKEELERTN-----KQLRAEME-DLVSSK--------DDVGKNVH 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 260 ALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSwQEEQSAQAqrlKDKVAQMKDTlgQAQQRVAELE 339
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKA-QFERDLQA---RDEQGEEKRR--QLVKQVRELE 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 340 PLKEQLRGAQELAASSQQKATLLGEELAS----AAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEkcqwskeragL 415
Cdd:pfam01576 756 AELEDERKQRAQAVAAKKKLELDLKELEAqidaANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI----------L 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 416 LQSVEAEKdKILKLSAEILRLEK---AVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEE 492
Cdd:pfam01576 826 AQSKESEK-KLKNLEAELLQLQEdlaASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN 904
|
330 340 350
....*....|....*....|....*....|....*
gi 14149742 493 KQELLEYMRKLEARLEKVADEKWNEDATTEDEEAA 527
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA 939
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
151-502 |
2.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 151 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDilsrqqgdhvari 230
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRD------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 231 lELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLL---GQLKEVQADKEQSEAELQVAqqenhhlNLDLKEAKswq 307
Cdd:COG1340 68 -ELNEKVKELKEERDELNEKLNELREELDELRKELAELNkagGSIDKLRKEIERLEWRQQTE-------VLSPEEEK--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 308 eeqsaqaqRLKDKVAQMKdtlgqaqqrvAELEPLKEQLRGAQELaassqqkatllgeelasaaaarDRTIAELHRSRLEV 387
Cdd:COG1340 137 --------ELVEKIKELE----------KELEKAKKALEKNEKL----------------------KELRAELKELRKEA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 388 AEVNGRLAELGlhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfktelareKDSSLVQLSE 467
Cdd:COG1340 177 EEIHKKIKELA----EEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE-----------IIELQKELRE 241
|
330 340 350
....*....|....*....|....*....|....*..
gi 14149742 468 SKRELTELRSALRVLQKEKEQ--LQEEKQELLEYMRK 502
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKK 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-507 |
2.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 145 KATVLQ---NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILsr 221
Cdd:PRK01156 330 KLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 222 qqgdhVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQ------------------LKEVQADKEQSE 283
Cdd:PRK01156 408 -----KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgeeksnhiINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 284 AELQVAQQENHHLNLDLKEAKSWQEE-QSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELaaSSQQKATLL 362
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI--KNRYKSLKL 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 363 G------EELASAAAARDRTIAELHRSRLEvaEVNGRL--AELGLH--------LKEEKCQWSKERAGLLQSVEAEKDKI 426
Cdd:PRK01156 561 EdldskrTSWLNALAVISLIDIETNRSRSN--EIKKQLndLESRLQeieigfpdDKSYIDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 427 LKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEIT-SRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
.
gi 14149742 507 L 507
Cdd:PRK01156 718 I 718
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
241-397 |
2.59e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 241 SEKVLTKEVELDRLRDTVKALTReqekLLG----QLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQR 316
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELAD----LLSlerqGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 317 LKDKVAQMKDTLGQAQQRVAEL----EPLKEQLRGAQEL-------AASSQQKATLLGEELASAAAARdrtIAELHRSRl 385
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLnqqiAALRRQLAALEAAldasekrDRESQAKIADLGRRLNVALAQR---VQELNRYR- 196
|
170
....*....|..
gi 14149742 386 evAEVNGRLAEL 397
Cdd:PRK09039 197 --SEFFGRLREI 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-495 |
2.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 248 EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAkswQEEQSAQAQRLKDKVAQMKDT 327
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 328 LGQAQQRVAELEPLkEQLRGAQELAassqqkatllgeELASAAAARDRtIAELHRSRLEvaevngrlaelglHLKEEKcq 407
Cdd:COG3883 92 ARALYRSGGSVSYL-DVLLGSESFS------------DFLDRLSALSK-IADADADLLE-------------ELKADK-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 408 wsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE 487
Cdd:COG3883 143 --AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
....*...
gi 14149742 488 QLQEEKQE 495
Cdd:COG3883 221 AAAAAAAA 228
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
176-399 |
3.12e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 176 ELRSRVQELERALATARQEHTELMEQYKGISR---SHGE---ITEERDILSrqqgdHVARILEledDIQTISEkvLTKEV 249
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEeeeLEEERRRLS-----NAEKLRE---ALQEALE--ALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 E---LDRLRDTVKALtREQEKLLGQLKEVQADKEQSEAELQVAQQE-NHHL-NLDLKEAK-SWQEEQSAQAQRLKDK--- 320
Cdd:COG0497 239 EggaLDLLGQALRAL-ERLAEYDPSLAELAERLESALIELEEAASElRRYLdSLEFDPERlEEVEERLALLRRLARKygv 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 321 -VAQMKDTLGQAQQRVAELEplkeqlRGAQELAAssqqkatlLGEELASAAAARDRTIAELHRSRLEVA-----EVNGRL 394
Cdd:COG0497 318 tVEELLAYAEELRAELAELE------NSDERLEE--------LEAELAEAEAELLEAAEKLSAARKKAAkklekAVTAEL 383
|
....*
gi 14149742 395 AELGL 399
Cdd:COG0497 384 ADLGM 388
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
232-513 |
3.47e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEK-------------------------LLGQLKEVQADKEQSEAEL 286
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKekleleeeyllyldylklneeridlLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 287 QVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVA----ELEPLKEQLRGAQELAASSQQKATLL 362
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVddeeKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 363 GEELASAAAAR--DRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILR-LEKA 439
Cdd:pfam02463 341 EKELKELEIKReaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqLEDL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149742 440 VQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQ---LQEEKQELLEYMRKLEARLEKVADE 513
Cdd:pfam02463 421 LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKsedLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
271-507 |
3.57e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 271 QLKEVQADKEQSEAELQVAQQENHHLNLDLKEakswQEEQSAQAQRlkdKVAQMKDTLGQAQQRVAELEPLKEQLRGAQe 350
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK----QEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQQ- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 351 laaSSQQKatLLGEELAsaAAARdrtiaelhrsrlevaevNGRLAELGLHLKEEKCQWSkERA----GLLQsvEAEKDKI 426
Cdd:PRK11637 120 ---AAQER--LLAAQLD--AAFR-----------------QGEHTGLQLILSGEESQRG-ERIlayfGYLN--QARQETI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 427 --LKLSAEILRLEKAVQEE-RTQNQVFKTELAREKDSSLVQLSESKRELTELRSAlrvLQKEKEQLQEekqelleyMRKL 503
Cdd:PRK11637 173 aeLKQTREELAAQKAELEEkQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESS---LQKDQQQLSE--------LRAN 241
|
....
gi 14149742 504 EARL 507
Cdd:PRK11637 242 ESRL 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-278 |
3.93e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEgqvtELRSRVQELERALATARQEHTELMEQYKGISRshgEITEERDILSR-QQGDHV 227
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEE---ELDELQDRLEAaEDLARL 745
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 14149742 228 ARILELEDDIQTISEKVLTKEVElDRLRDTVKALTREQEKLLGQLKEVQAD 278
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-347 |
4.72e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 230 ILELEDDIQTISEKVLTKEVEL-----DRLRDTVKALTREqeklLGQLKEVQADKEQ-SEAELQVAQQENHHLNLDLKEA 303
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELlnsikPKLRDRKDALEEE----LRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIK 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 14149742 304 KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRG 347
Cdd:smart00787 224 VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
246-524 |
5.14e-04 |
|
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: 43.40 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 246 TKEVELDRLRDTVKALTREQEKLLGQLKEVqadkEQsEAELQVAQQENHHLNLD---------------LKEAKSWQEEQ 310
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEM----EQ-KLQLHLLAKEDHHKQLNeiekyyatitgqfglVKENHGKLEQN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 311 SAQAQRLKDKVAqmkdTLGQAQQrvAELEPLKEQLRG-AQELAASSQQKATLLGEELASaAAARDRTIAELH-RSRLEVa 388
Cdd:pfam15818 164 VQEAIQLNKRLS----ALNKKQE--SEICSLKKELKKvTSDLIKSKVTCQYKMGEENIN-LTIKEQKFQELQeRLNMEL- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 389 EVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEIlRLEKAVQEERTQNQVFKTELAREKdsslvqLSES 468
Cdd:pfam15818 236 ELNKKINEEITHIQEEK----QDIIISFQHMQQLLQQQTQANTEM-EAELKALKENNQTLERDNELQREK------VKEN 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14149742 469 KRELTELRS----ALRVLQKEKEQLQEEKQEL---LEYMRKLEARLEKVADEKWNEDATTEDE 524
Cdd:pfam15818 305 EEKFLNLQNehekALGTWKKHVEELNGEINEIkneLSSLKETHIKLQEHYNKLCNQKKFEEDK 367
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
162-309 |
5.48e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 162 DLMQLKLQLEGQVTELRSR--------------VQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQqgdhV 227
Cdd:smart00787 113 LLMDKQFQLVKTFARLEAKkmwyewrmklleglKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEE----L 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 ARILELEDDIQTIsekvltKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ 307
Cdd:smart00787 189 RQLKQLEDELEDC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
..
gi 14149742 308 EE 309
Cdd:smart00787 263 EQ 264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-355 |
5.58e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 215 ERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTRE-------QEKLLGQLKEVQADKEQS--EAE 285
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEieevearIKKYEEQLGNVRNNKEYEalQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149742 286 LQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQR----VAELEPLKEQLRGAQELAASS 355
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLAELEAELEELEAEREELAAK 171
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
149-515 |
7.82e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.75 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQE-------RNDLMQLKLQLEGQVTELRSRVQELERALATARQehtelmeqykgisrshgeITEERDILsR 221
Cdd:pfam05622 64 LQKQLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNEELTSLAEEAQA------------------LKDEMDIL-R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 222 QQGDHVARileLEDDIQTISEKVltkeVELDRLRDTVKAL----------TREQEKllgQLKEVQADKEQSEAELQVAQQ 291
Cdd:pfam05622 125 ESSDKVKK---LEATVETYKKKL----EDLGDLRRQVKLLeernaeymqrTLQLEE---ELKKANALRGQLETYKRQVQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 292 ENHHLNLDLKEAKSWQ------EEQSAQAQRLKDKVAQMKDTL---------GQAQQRvaeleplkeQLRGAQELAASSQ 356
Cdd:pfam05622 195 LHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDTLretneelrcAQLQQA---------ELSQADALLSPSS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 357 QKATLLGEELASaAAARDRTIAELHRSRL----EVAEVNGRLAELGLHLkeEKCQWSKERagLLQSVEAEKDKILKLSAE 432
Cdd:pfam05622 266 DPGDNLAAEIMP-AEIREKLIRLQHENKMlrlgQEGSYRERLTELQQLL--EDANRRKNE--LETQNRLANQRILELQQQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 433 ILRLEKAVQEERTQNQVFKTeLAREKDSSLVQLSESKRELTELRSALRVLQ-KEKEQLQEEKQELLEYMRKLEARLeKVA 511
Cdd:pfam05622 341 VEELQKALQEQGSKAEDSSL-LKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKDEDM-KAM 418
|
....
gi 14149742 512 DEKW 515
Cdd:pfam05622 419 EERY 422
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
149-293 |
8.58e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTEL---MEQYKGIS---RSHGE-------ITEE 215
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskIEQFQKVIkmyEKGGVcptctqqISEG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 216 RDILS--RQQGDHVARILELEDDIQtisEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEN 293
Cdd:PHA02562 298 PDRITkiKDKLKELQHSLEKLDTAI---DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-505 |
9.22e-04 |
|
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: 42.63 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 117 QFREPRPMDELVTLEEADGG--------SDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERAL 188
Cdd:COG3096 305 QYRLVEMARELEELSARESDleqdyqaaSDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 189 ATARQEHTELMEQ-----------------YKGISRSHGE---ITEERDILSRQQGDHVArilELEDDIQTISEKVLTKE 248
Cdd:COG3096 385 EAAEEEVDSLKSQladyqqaldvqqtraiqYQQAVQALEKaraLCGLPDLTPENAEDYLA---AFRAKEQQATEEVLELE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 249 velDRLRDTvKALTREQEKLLGQLKEVQADKEQSEAeLQVAQQEnhhlnldLKEAKswqeEQSAQAQRlkdkVAQMKDTL 328
Cdd:COG3096 462 ---QKLSVA-DAARRQFEKAYELVCKIAGEVERSQA-WQTAREL-------LRRYR----SQQALAQR----LQQLRAQL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 329 GQAQQRVaeleplkEQLRGAQELAASSQQKAtllGEELASAAAardrtiAELHRSRLEVaevngRLAELGLHLKEEkcqw 408
Cdd:COG3096 522 AELEQRL-------RQQQNAERLLEEFCQRI---GQQLDAAEE------LEELLAELEA-----QLEELEEQAAEA---- 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 409 SKERAGLLQSVEAEKDKILKLSAEILRLEKAvQEERTQnqvfkteLAREKDSSLvqlsESKRELTELRSAL----RVLQK 484
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAA-QDALER-------LREQSGEAL----ADSQEVTAAMQQLlereREATV 644
|
410 420
....*....|....*....|.
gi 14149742 485 EKEQLQEEKQELLEYMRKLEA 505
Cdd:COG3096 645 ERDELAARKQALESQIERLSQ 665
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
155-259 |
1.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 155 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGI-SRSHGEITEERDILSRQqgdhvARILEL 233
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREISRLD-----REIERL 477
|
90 100
....*....|....*....|....*.
gi 14149742 234 EDDIQTISEKVLTKEVELDRLRDTVK 259
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKELWK 503
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
271-405 |
1.03e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 271 QLKEVqadKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQA-QQRVAELEP-LKEQLRGA 348
Cdd:pfam07111 521 QLSEV---AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAlQEKVAEVETrLREQLSDT 597
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149742 349 QEL---AASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNG-RLAELGLHLKEEK 405
Cdd:pfam07111 598 KRRlneARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGqRLARRVQELERDK 658
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-495 |
1.04e-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: 42.40 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 149 LQNQLDESQQERNDLMQLKLQ----LEGQVTELRS-------RVQELERALATARQEHTELMEQYKGISRSHGEITEE-- 215
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKeihdLEIQLTAIKTseehylkEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEas 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 216 ----------RDILS--RQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSE 283
Cdd:pfam05483 510 dmtlelkkhqEDIINckKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 284 AELQVA------QQENHHLNLD--LKEAKSWQEEQSAQAQRL---KDKVAQMKDTLGQAQQRVAELeplkeqlrgaqela 352
Cdd:pfam05483 590 KILENKcnnlkkQIENKNKNIEelHQENKALKKKGSAENKQLnayEIKVNKLELELASAKQKFEEI-------------- 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 353 ASSQQKatllgeELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLhlkeeKCQWS-KERAGLLQSVEAEKDKILKLSA 431
Cdd:pfam05483 656 IDNYQK------EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK-----RCQHKiAEMVALMEKHKHQYDKIIEERD 724
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14149742 432 EILRLEKAVQEERTQNQVfktelarekdSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQE 495
Cdd:pfam05483 725 SELGLYKNKEQEQSSAKA----------ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
174-514 |
1.17e-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: 42.34 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 174 VTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDhvarILELEDDIQTIsEKVLTKEVELDR 253
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENE----LDPLKNRLKEI-EHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 254 LRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQ-----EEQSAQAQRLKDKVAQMKDTL 328
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDcqrelEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 329 GQAQQRVaelEPLKEQLRGAQELAASSQQKATLLGEElasAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQW 408
Cdd:TIGR00606 350 GRLQLQA---DRHQEHIRARDSLIQSLATRLELDGFE---RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 409 SKERAGLLQSVEAEKDKILKLSAEIlrLEKAVQEERT-----QNQVFKTELAREKDSSLVQlSESKRELTELRSALRVLQ 483
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEI--LEKKQEELKFvikelQQLEGSSDRILELDQELRK-AERELSKAEKNSLTETLK 500
|
330 340 350
....*....|....*....|....*....|.
gi 14149742 484 KEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-469 |
1.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 171 EGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVE 250
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 251 LDRLRDTVKAlTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLK-----------EAKSWQEEQSAQAQRLKD 319
Cdd:PTZ00121 1618 AKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkkkaeEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 320 KvAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEElasaaaarDRTIAElhRSRLEVAEVNgRLAELGL 399
Cdd:PTZ00121 1697 E-AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE--------DKKKAE--EAKKDEEEKK-KIAHLKK 1764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 400 HLKEEKCQWSKERAGLLQSVEAEKDKILKLSAE-----ILRLEKAVQEERTQN--------QVFKTELAREKDSSLVQLS 466
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdIFDNFANIIEGGKEGnlvindskEMEDSAIKEVADSKNMQLE 1844
|
...
gi 14149742 467 ESK 469
Cdd:PTZ00121 1845 EAD 1847
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
250-372 |
1.54e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.76 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLG 329
Cdd:COG5283 22 RVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSSLEQTNRQLE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 14149742 330 QAQQRVAELEPLKEQLRGA-QELAASSQQKATLLGeeLASAAAA 372
Cdd:COG5283 102 RQQQRLARLGARQDRLKAArARLQRLAGAGAAAAA--IGAALAA 143
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
261-402 |
2.05e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 261 LTREQEKLLGQLKEVQADKEQSEAELQVAQQenhhLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEP 340
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14149742 341 L-------------KEQLRGAQE--LAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLK 402
Cdd:pfam00529 132 LapiggisreslvtAGALVAQAQanLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
167-498 |
2.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 167 KLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLT 246
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 247 KEVELDRLRDTVKALTREQEKLLGQLKEVQAdkeqseaELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKD 326
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 327 TLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKC 406
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 407 QWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEK 486
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|..
gi 14149742 487 EQLQEEKQELLE 498
Cdd:COG4372 325 AKKLELALAILL 336
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
151-345 |
2.41e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 151 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGdhvari 230
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 231 lelEDDIQtisEKVLTKEVELDRLRDTVKALTRE----QEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSW 306
Cdd:pfam15905 147 ---EDGTQ---KKMSSLSMELMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14149742 307 QEEQ----------SAQAQRLKDKVAQMKDTLGQAQQrvaELEPLKEQL 345
Cdd:pfam15905 221 TEKLleyitelscvSEQVEKYKLDIAQLEELLKEKND---EIESLKQSL 266
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
120-385 |
2.56e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 120 EPRPMDELVTLEEADggSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELm 199
Cdd:PRK10929 94 EPRSVPPNMSTDALE--QEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPL- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 200 eqykgisrshgeitEERDILSRQ--QGDHVARILELEddiqtISEKVLTKEVELDRLRDTVKALTREQ-EKLLGQLKEVQ 276
Cdd:PRK10929 171 --------------AQAQLTALQaeSAALKALVDELE-----LAQLSANNRQELARLRSELAKKRSQQlDAYLQALRNQL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 277 ADKEQSEAEL------QVAQQ---------ENHHLNLDLKEAkswqeeQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPL 341
Cdd:PRK10929 232 NSQRQREAERalesteLLAEQsgdlpksivAQFKINRELSQA------LNQQAQRMDLIASQQRQAASQTLQVRQALNTL 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 14149742 342 KEQlrgAQELAASsqqkaTLLGEELaSAAAAR----------DRTIAELHRSRL 385
Cdd:PRK10929 306 REQ---SQWLGVS-----NALGEAL-RAQVARlpempkpqqlDTEMAQLRVQRL 350
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
252-372 |
2.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.62 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnhhlnldLKEAKSwqEEQSAQAQRLKDKVAQmkdtlgQA 331
Cdd:PRK12472 207 DEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKA-------LAAAKT--DEAKARAEERQQKAAQ------QA 271
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 14149742 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAA 372
Cdd:PRK12472 272 AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKA 312
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
137-513 |
3.42e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 137 SDILLVVPKATVLQNQLDESQQERNDLMQLklqLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSH---GEIT 213
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKKEKRRDEMLGL---APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQEtllGTIM 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 214 EERDILSRQQGDhVARILELEDDIQTISEKVLTKEVELDR--LRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQ 291
Cdd:TIGR00606 779 PEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 292 ENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQ-LRGAQELAASSQQKATLLGEELASAA 370
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdSPLETFLEKDQQEKEELISSKETSNK 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 371 AARDrtiaELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEkdkilkLSAEILRLEKAVQEERTQNQVF 450
Cdd:TIGR00606 938 KAQD----KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ------LEECEKHQEKINEDMRLMRQDI 1007
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 451 KTELARE---KDsslvQLSESKR--ELTELRSALRVLQKEKEQLQ--EEKQElleyMRKLEARLEKVADE 513
Cdd:TIGR00606 1008 DTQKIQErwlQD----NLTLRKRenELKEVEEELKQHLKEMGQMQvlQMKQE----HQKLEENIDLIKRN 1069
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
152-386 |
3.72e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNDLMQLKLQLEgqvtelRSRVQELERaLATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARIL 231
Cdd:pfam17380 354 RQEERKRELERIRQEEIAME------ISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKE--VELDRLRDTVKALTREQEKLLGQ---LKEVQADKEQSEAELQVAQQENHH-LNLDLKEAKS 305
Cdd:pfam17380 427 AEQEEARQREVRRLEEEraREMERVRLEEQERQQQVERLRQQeeeRKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 306 WQEEQSAQAQRLKDKVAQMKDTLGQAQQ-RVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARD--RTIAELHR 382
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREmmRQIVESEK 586
|
....
gi 14149742 383 SRLE 386
Cdd:pfam17380 587 ARAE 590
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
216-443 |
4.41e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 216 RDILsrqqgDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQAdkeqseaelqvaqqenhh 295
Cdd:COG0497 144 RELL-----DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA------------------ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 296 LNLDLKEAKSWQEEQS--AQAQRLKDKVAQMK-----------DTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLL 362
Cdd:COG0497 201 AALQPGEEEELEEERRrlSNAEKLREALQEALealsggeggalDLLGQALRALERLAEYDPSLAELAERLESALIELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 363 GEELASAAAArdrtiAELHRSRLEvaEVNGRLAELgLHLK-------EEKCQWSKERAGLLQSVEAEKDKILKLSAEILR 435
Cdd:COG0497 281 ASELRRYLDS-----LEFDPERLE--EVEERLALL-RRLArkygvtvEELLAYAEELRAELAELENSDERLEELEAELAE 352
|
....*...
gi 14149742 436 LEKAVQEE 443
Cdd:COG0497 353 AEAELLEA 360
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-525 |
4.45e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLkeakswqeeqs 311
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI----------- 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 312 aqaQRLKDKVAQMKDTLGqaqqrvaeleplkeqlrgaqelaassqqkaTLLGEELASAAAARDRTIAElhRSRLEVAEVN 391
Cdd:TIGR00606 761 ---QRLKNDIEEQETLLG------------------------------TIMPEEESAKVCLTDVTIME--RFQMELKDVE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 392 GRLAELGLHLKEEKCQWSKERagLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTelarekdsslvQLSESKRE 471
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS-----------KTNELKSE 872
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 472 LTELRSALRVLQKEKEQLQEEKQELLEYMRKL-EARLEKVADEKWNEDATTEDEE 525
Cdd:TIGR00606 873 KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIkDAKEQDSPLETFLEKDQQEKEE 927
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-509 |
4.52e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 154 DESQQERNDLMQL----KLQLEGQVTELRSRVQELEralatarQEHTELMEQYKGISRSHGEITEERDILsrqqgdhVAR 229
Cdd:pfam01576 4 EEEMQAKEEELQKvkerQQKAESELKELEKKHQQLC-------EEKNALQEQLQAETELCAEAEEMRARL-------AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 230 ILELEDDIQTIsekvltkEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKS---W 306
Cdd:pfam01576 70 KQELEEILHEL-------ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdilL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 307 QEEQSAQAQR----LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHR 382
Cdd:pfam01576 143 LEDQNSKLSKerklLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 383 srlEVAEVNGRLAELGLHL--KEEKCQWSKERAG--LLQSVEAEKdKILKLSAEILRLEKAVQEERTQN----------- 447
Cdd:pfam01576 223 ---QIAELQAQIAELRAQLakKEEELQAALARLEeeTAQKNNALK-KIRELEAQISELQEDLESERAARnkaekqrrdlg 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14149742 448 ---QVFKTELAREKDSSLVQL---SESKRELTELRSALRVLQKEKE-QLQE----------EKQELLEYMRKLEARLEK 509
Cdd:pfam01576 299 eelEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRSHEaQLQEmrqkhtqaleELTEQLEQAKRNKANLEK 377
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
247-366 |
4.74e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 247 KEVELDRLRDTVKALTrEQEKllgQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQaqrLKDKVAQMKD 326
Cdd:pfam02841 185 KEAVEEAILQTDQALT-AKEK---AIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ---LIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 14149742 327 TLGQAQQRVAELEpLKEQLRgaqELAASSQQKATLLGEEL 366
Cdd:pfam02841 258 QLLAEQERMLEHK-LQEQEE---LLKEGFKTEAESLQKEI 293
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
460-514 |
4.81e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 4.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 460 SSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4026 125 QNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEN 179
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
401-505 |
4.83e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 401 LKEEKCQwskeraglLQSVEAEKDKILK-LSAEILRLEKAVQEERTQNQVFKTELAR-EKDsslvqlsesKRELTELRSA 478
Cdd:pfam13851 31 LKEEIAE--------LKKKEERNEKLMSeIQQENKRLTEPLQKAQEEVEELRKQLENyEKD---------KQSLKNLKAR 93
|
90 100
....*....|....*....|....*..
gi 14149742 479 LRVLQKEKEQLQEEKQELLEYMRKLEA 505
Cdd:pfam13851 94 LKVLEKELKDLKWEHEVLEQRFEKVER 120
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
420-510 |
5.57e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.07 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 420 EAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAREKDSSLVQLSESKRELTELRSALR----VLQKEKEQLQEEKQE 495
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLE----DLERELALLQAKERQLEKKLKTLEQKLKnekeELQRLKNALQQIKTQ 130
|
90
....*....|....*
gi 14149742 496 LLEYMRKLEARLEKV 510
Cdd:pfam11559 131 FAHEVKKRDREIEKL 145
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
301-513 |
5.58e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 301 KEAKSWQEEQSAQAQRLKDKVAQMKDT-----------LGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASA 369
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTyherkqvlekeLKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 370 AAARDRTIA-ELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGlLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQ 448
Cdd:TIGR00618 270 EELRAQEAVlEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE-LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14149742 449 VFKTE---LAREKDSSLVQLSESKRElTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR00618 349 TLHSQeihIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
373-504 |
5.79e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 373 RDRTIAELHrsrlevaevngrlaELGL-HLKEEKCQWSKERAGLLQSveaekdKILKLSAEILRLEKAVQEERTqnqVFK 451
Cdd:PRK05771 18 KDEVLEALH--------------ELGVvHIEDLKEELSNERLRKLRS------LLTKLSEALDKLRSYLPKLNP---LRE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 14149742 452 TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLE 504
Cdd:PRK05771 75 EKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE 127
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
185-504 |
6.62e-03 |
|
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: 39.94 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 185 ERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVAriLELEDDiqtisekvltKEVELDRLRDTVKALTRE 264
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLA--VAFAPD----------PEAELAALRQRRSELERE 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 265 QEKLLGQLKEVQADKEQSEAELQVAQQENHHLNL----DLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAEL-- 338
Cdd:COG3096 852 LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladeTLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLqs 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 339 -----EPLKEQLRGAQELAASSQQKATLLGE----------ELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKE 403
Cdd:COG3096 932 dpeqfEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 404 EKC-QWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEErtqnqvfKTELAREKDSSLVQlseskrELTELRSALRVL 482
Cdd:COG3096 1012 AQYsQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAE-------AEERARIRRDELHE------ELSQNRSRRSQL 1078
|
330 340
....*....|....*....|..
gi 14149742 483 QKEKEQLQEEKQELLEYMRKLE 504
Cdd:COG3096 1079 EKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
228-496 |
6.72e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 228 ARILELEDDIQTISEKVLTKEVELDRLRDTVKALTReqekLLGQLKEV--QADkeqSEAELQVAQQENHHLNLDLKEAKS 305
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSR----FIGSHLAVafEAD---PEAELRQLNRRRVELERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 306 WQEEQSAQAQRLKDKVAQMKDTLGQA--------QQRVAELEplkEQLRGAQELAASSQQKATLLG--EELASAAAARDR 375
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIR---EQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPE 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 376 TIAELHRSRLE--------------VAEVNGRLAELGLHlkeekcqwskERAGLLqsvEAEKDKILKLSAeilRLEKAVQ 441
Cdd:PRK04863 936 QFEQLKQDYQQaqqtqrdakqqafaLTEVVQRRAHFSYE----------DAAEML---AKNSDLNEKLRQ---RLEQAEQ 999
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 14149742 442 EERTQnqvfkTELAREKDSslvQLSESKRELTELRSALRVLQkekEQLQEEKQEL 496
Cdd:PRK04863 1000 ERTRA-----REQLRQAQA---QLAQYNQVLASLKSSYDAKR---QMLQELKQEL 1043
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
130-503 |
7.83e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 39.57 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 130 LEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSH 209
Cdd:COG4995 98 LAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 210 GEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVA 289
Cdd:COG4995 178 ALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAAL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 290 QQENHHLNLDLKEAksWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASA 369
Cdd:COG4995 258 LALAAALLLLAALA--ALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLAL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 370 AAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQV 449
Cdd:COG4995 336 LLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAA 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 14149742 450 FKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:COG4995 416 LALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRL 469
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
324-508 |
7.85e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.28 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 324 MKDTLGQAQQRVAELEPLKEQL--------RGAQELAASSQQKA---TLLGEELASAAAARDrtiaELHRSRLEVAEVNG 392
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFsqliepieAILRELPQAKSRLLeleALLAQERAAYGKLRR----ELAGLTRRLSAAEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 393 RLAELGLHLKEEkcqwskerAGLLQSVEAEKDKI----LKLSAEILRLEKAVQEERTQNQVFKTELAR---EKDSSLVQL 465
Cdd:pfam19220 84 ELEELVARLAKL--------EAALREAEAAKEELrielRDKTAQAEALERQLAAETEQNRALEEENKAlreEAQAAEKAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14149742 466 SESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:pfam19220 156 QRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA 198
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
171-339 |
7.88e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 171 EGQV------TELRSRVQELERALATARQEHTELmeqykgisrshgeiteerdilsRQQGDHVARILELEDDIQTISEKV 244
Cdd:COG1566 69 KGQVlarldpTDLQAALAQAEAQLAAAEAQLARL----------------------EAELGAEAEIAAAEAQLAAAQAQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 245 LTKEVELDRLRDTVK--ALTREQekllgqLKEVQADKEQSEAELQVAQQenhhlNLDLKEAKSWQEEQSAQAQRlkdKVA 322
Cdd:COG1566 127 DLAQRELERYQALYKkgAVSQQE------LDEARAALDAAQAQLEAAQA-----QLAQAQAGLREEEELAAAQA---QVA 192
|
170
....*....|....*..
gi 14149742 323 QMKDTLGQAQQRVAELE 339
Cdd:COG1566 193 QAEAALAQAELNLARTT 209
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
280-373 |
8.05e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 280 EQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgAQELAASSQQKA 359
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ-EKAAETSQERKQ 216
|
90
....*....|....
gi 14149742 360 TLlgEELASAAAAR 373
Cdd:PRK11448 217 KR--KEITDQAAKR 228
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
373-511 |
8.19e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 373 RDRTIAELHRSrLEVAEVNGRLAELGLHLKEEKCQWSKERAGllQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKT 452
Cdd:COG2433 365 RDEVKARVIRG-LSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149742 453 ELAR-EKDSSLVQLSESK-----RELTELRSALRVLQKEKEQLQEEKQEL------LEYMRKLEARLEKVA 511
Cdd:COG2433 442 RIERlERELSEARSEERReirkdREISRLDREIERLERELEEERERIEELkrklerLKELWKLEHSGELVP 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-513 |
8.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 151 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRshgEITEERDILSRQQGDHVARI 230
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE---ALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 231 LELEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEvQADKEQSE----AEL-QVAQQE------------N 293
Cdd:COG4913 415 RDLRRELRELEA-------EIASLERRKSNIPARLLALRDALAE-ALGLDEAElpfvGELiEVRPEEerwrgaiervlgG 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 294 HHLNL-----DLKEAKSW----QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE----P----LKEQLRG--------- 347
Cdd:COG4913 487 FALTLlvppeHYAAALRWvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDfkphPfrawLEAELGRrfdyvcvds 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 348 AQELA---------------ASSQQKAT--------LLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEE 404
Cdd:COG4913 567 PEELRrhpraitragqvkgnGTRHEKDDrrrirsryVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 405 KCQWSKeragLLQSVEAEKDkILKLSAEILRLEKAVQEERTQNQVFKtELARekdsslvQLSESKRELTELRSALRVLQK 484
Cdd:COG4913 647 REALQR----LAEYSWDEID-VASAEREIAELEAELERLDASSDDLA-ALEE-------QLEELEAELEELEEELDELKG 713
|
410 420
....*....|....*....|....*....
gi 14149742 485 EKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
152-457 |
9.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 152 QLDESQQERNdlmqlklQLEGQVTELRSRVQELERALATARQEHTELMEQYKgisrshgEITEERDILSRQQGDHVARIL 231
Cdd:COG4372 39 ELDKLQEELE-------QLREELEQAREELEQLEEELEQARSELEQLEEELE-------ELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAEL-----QVAQQENHHLNLDLKEAKSW 306
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqeELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14149742 307 QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLE 386
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14149742 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELARE 457
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| |
