|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-595 |
6.85e-180 |
|
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: 520.99 E-value: 6.85e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 122 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEGQVTELRS 179
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 180 RVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVK 259
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 260 altreqeKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE 339
Cdd:pfam07888 161 -------KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 340 PLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV 419
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 420 EAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEY 499
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 500 MRKLEARLEKVADEKWNEDAATDEEAAaglscPAALTDSEDESPEDMRLPP----YGLCEHR-----DPGSSPAGPREAS 570
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERP-----DSPLSDSEDENPEALQPPRplghYSLCEQGqpdslLLATPPPSPRDPE 468
|
490 500
....*....|....*....|....*
gi 1622845278 571 PLVVISQPAPISPHlsgpaEDSSSD 595
Cdd:pfam07888 469 STVVISQPAPLSSP-----HQSSSD 488
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-118 |
8.95e-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: 141.23 E-value: 8.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 15 VNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWssVPESTTDGSPIHTSVQFQASYLPKPG 94
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 1622845278 95 AQLYQFRYVNRQGRVCGQSPPFQF 118
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-492 |
1.29e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 174 VTELRSRVQELERALATAR--QEHAELMEQYKGISRSHgeiteERDILSRQQGDHVARILELEDDIQTISEKVLTKEVEL 251
Cdd:COG1196 195 LGELERQLEPLERQAEKAEryRELKEELKELEAELLLL-----KLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQA 331
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKE 411
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 412 RAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQE 491
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA----ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
.
gi 1622845278 492 E 492
Cdd:COG1196 506 F 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-443 |
3.12e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 145 KATVLQNQLDESQQErndLMQLKLQ-LEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQ 223
Cdd:COG1196 214 RYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 224 GDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEA 303
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 304 KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRS 383
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 384 RLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEE 443
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-491 |
7.74e-18 |
|
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: 88.20 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 167 KLQLEGQVTELRSRVQELERALATARQEHA-------ELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQT 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 240 ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA----------DKEQSEAELQVAQQENRRLNLDLQEAKSWQEE 309
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 310 QSAQAQRlKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAE 389
Cdd:TIGR02169 829 EYLEKEI-QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 390 VNGRLAELGLHLKEEKCQWSkERAGLLQSVEAEKDKILKLSAEILRLEKaVQEERTQNQVFKTELAREKDSSLVQLSESK 469
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
330 340
....*....|....*....|..
gi 1622845278 470 RELTELRSALRVLQKEKEQLQE 491
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILE 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-513 |
1.03e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQE 308
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQ---LRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRL 385
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 386 EVAEVNGRLAElglHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQL 465
Cdd:COG1196 554 EDDEVAAAAIE---YLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622845278 466 SESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-506 |
7.33e-17 |
|
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: 85.11 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 155 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELE 234
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 235 DDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAkswQEEQSAQA 314
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL---RERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 315 QRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRL 394
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 395 AELGLHLKEekCQWSKERAGL-LQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSL---------VQ 464
Cdd:TIGR02168 911 SELRRELEE--LREKLAQLELrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLenkikelgpVN 988
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622845278 465 LsESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:TIGR02168 989 L-AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-496 |
1.13e-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: 81.27 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKlqlegqvtELRSRVQELERALATARQEHAElmEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQ--------ALLKEKREYEGYELLKEKEALE--RQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTK-EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQ 307
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 308 EEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEV 387
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 388 AEVNGRLAELglhlkeekcqwskeRAGLLQSVEAEKDKILKLSAEILRLEKAVQeertqnqvfktelarekdsslvQLSE 467
Cdd:TIGR02169 423 ADLNAAIAGI--------------EAKINELEEEKEDKALEIKKQEWKLEQLAA----------------------DLSK 466
|
330 340
....*....|....*....|....*....
gi 1622845278 468 SKRELTELRSALRVLQKEKEQLQEEKQEL 496
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-455 |
1.95e-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: 80.49 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 160 RNDLMQLKLQLEG-QVTELRSRVQELERALATARQEHAELMEQykgISRSHGEITEERDI---LSRQQGDHVARILELED 235
Cdd:TIGR02168 219 KAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEvseLEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 236 DIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE-------NRRLNLDLQEAKSWQE 308
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaassQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE-----RLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845278 389 EVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELA 455
Cdd:TIGR02168 451 ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-511 |
2.56e-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: 80.10 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 251 LDRLRDTVKALTREQEKLLGQ------LKEVQADKEQSEAELQVA---QQENRRLNLDLQEAKSWQEEQSAQAQ------ 315
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQaekaerYKELKAELRELELALLVLrleELREELEELQEELKEAEEELEELTAElqelee 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 316 ---RLKDKVAQMKDTLGQAQQR----VAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:TIGR02168 268 kleELRLEVSELEEEIEELQKElyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 EVNGRLAELGLHLKEEKCQW-----------------SKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELeelesrleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 452 TELAR-EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 511
Cdd:TIGR02168 428 KKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-514 |
1.00e-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: 78.17 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 218 ILSRQQ--GDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRR 295
Cdd:TIGR02168 672 ILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 296 LNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaqELAASSQQKATLLGEELASAATARDR 375
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 376 TIAELHRSRLEVAEVNGRLAELGLHLKEekcqWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELa 455
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIES----LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL- 903
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 456 REKDSslvQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR02168 904 RELES---KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
653-681 |
4.20e-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: 4.20e-14
10 20
....*....|....*....|....*....
gi 1622845278 653 KECPICKERFPAESDKDALEDHMDGHFFF 681
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHFFF 29
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-513 |
3.08e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.88 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEgqvtELRSRVQELERALATARQEHAEL--MEQYKGISRSHGEITEERDILSRQQG-- 224
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEel 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 225 -DHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQ-EKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQe 302
Cdd:COG4717 152 eERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELE- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 303 akswQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLG-------EELASAATARDR 375
Cdd:COG4717 231 ----QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 376 TIAELHRSRLEVAEVNGRLAELGL-----------------HLKEEKCQWSKERAGL-LQSVEAEKDKILKLS------- 430
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLppdlspeellelldrieELQELLREAEELEEELqLEELEQEIAALLAEAgvedeee 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 431 -AEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKREltELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:COG4717 387 lRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
....
gi 1622845278 510 VADE 513
Cdd:COG4717 465 LEED 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-513 |
3.82e-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: 71.72 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 276 QADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASS 355
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 356 QQKATLLGEELASaatardrtiaelhrsRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV-EAEKDKILKLSA--- 431
Cdd:COG4942 96 RAELEAQKEELAE---------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRAdla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 432 EILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 511
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 1622845278 512 DE 513
Cdd:COG4942 241 ER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-433 |
4.24e-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: 73.17 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 157 QQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDD 236
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 237 IQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQ--- 313
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElre 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 314 -----------AQRLKDKVAQMKDTLGQAQQRVAEL-EPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELH 381
Cdd:TIGR02168 906 leskrselrreLEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG 985
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845278 382 RSRL----EVAEVNGRLAELglhlkeekcqwSKERAGLLQSVEAEKDKILKLSAEI 433
Cdd:TIGR02168 986 PVNLaaieEYEELKERYDFL-----------TAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-514 |
4.79e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 169 QLEGQVTELRSRVQELERALATAR--------------QEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELE 234
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAReavedrreeieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 235 DDIQTISEKVltkeVELDRLRDTVKALTREQE----KLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEeQ 310
Cdd:PRK02224 433 ATLRTARERV----EEAEALLEAGKCPECGQPvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-A 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 311 SAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRG-AQELAASSQQKAtllgeelASAATARDRtiAELHRSrlEVAE 389
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRErAAELEAEAEEKR-------EAAAEAEEE--AEEARE--EVAE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 390 VNGRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKLSAEILRLekavQEERTQnqvfKTELAREKDSSLVQLSESK 469
Cdd:PRK02224 577 LNSKLAEL------------KERIESLERIRTLLAAIADAEDEIERL----REKREA----LAELNDERRERLAEKRERK 636
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622845278 470 RELTELRSALRVlqkekEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:PRK02224 637 RELEAEFDEARI-----EEAREDKERAEEYLEQVEEKLDELREER 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-513 |
7.57e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKS--- 305
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArll 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 306 ------WQEEQSAQAQRLKDKVAQMKD----------------------TLGQAQQRVAE--------LEPLKEQLRGAQ 349
Cdd:COG1196 495 llleaeADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaaLAAALQNIVVEddevaaaaIEYLKAAKAGRA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 350 ELAASSQQKATLLGEELASAATARDRTI-----AELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKD 424
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 425 KILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRV---------LQKEKEQLQEEKQE 495
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEaeeerleeeLEEEALEEQLEAER 734
|
410
....*....|....*...
gi 1622845278 496 LLEYMRKLEARLEKVADE 513
Cdd:COG1196 735 EELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-509 |
1.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQ-----QENRRLNLDLQEA 303
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllAGLRGLAGAVAVL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 304 KSWQEEQ-----------------------SAQAQRLKDKVA-----------------QMKDTLGQAQQRVAELEPLKE 343
Cdd:COG1196 530 IGVEAAYeaaleaalaaalqnivveddevaAAAIEYLKAAKAgratflpldkiraraalAAALARGAIGAAVDLVASDLR 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 344 QLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEkcqwSKERAGLLQSVEAEK 423
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL----LAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 424 DKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
....*.
gi 1622845278 504 EARLEK 509
Cdd:COG1196 766 ERELER 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-345 |
2.40e-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: 70.48 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAEL--MEQYKGISRSHGEITEERDILSRQQG-- 224
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEArl 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 225 DHVARILE--------LEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRL 296
Cdd:TIGR02169 815 REIEQKLNrltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622845278 297 NLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQL 345
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-513 |
2.90e-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: 70.10 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 181 VQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQgDHVARILELEDDIQTISEKVLTKEVEldrlrdtvkA 260
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEGYELLKEKE---------A 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 261 LTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDL-QEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVA--- 336
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAeke 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 337 -ELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEekcqWSKERAGL 415
Cdd:TIGR02169 315 rELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 416 LQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvQLSESKRELTELRSALRVLQKEKEQLQEEKQE 495
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA----KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330
....*....|....*...
gi 1622845278 496 LLEYMRKLEARLEKVADE 513
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKE 484
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-513 |
3.17e-12 |
|
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: 70.05 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 150 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERalatarQEHAELMEQYKGISRShgeITEERDILSRQQGDHVAR 229
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNKELKSELKN---QEKKLEEIQNQISQNNKI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 230 ILELEDDIQTISEKV-------LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQE 302
Cdd:TIGR04523 337 ISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 303 AKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaaSSQQKATLLGEELASAATARDRTIAELHR 382
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 383 SRLEVAEvngrlaelglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR-----E 457
Cdd:TIGR04523 494 KEKELKK-----------LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekE 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845278 458 KDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-513 |
2.09e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSwQE 308
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA-QA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQR-LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAatardRTIAELHRSRLev 387
Cdd:TIGR02169 500 RASEERVRgGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAK-----EAIELLKRRKA-- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 388 aevnGRLAELGLH-----------LKEEKC------------------QWSKERAGLLQSVEAEKD-----KILKLSAEI 433
Cdd:TIGR02169 573 ----GRATFLPLNkmrderrdlsiLSEDGVigfavdlvefdpkyepafKYVFGDTLVVEDIEAARRlmgkyRMVTLEGEL 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 434 L----------------RLEKAVQEERTQN-QVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQEL 496
Cdd:TIGR02169 649 FeksgamtggsraprggILFSRSEPAELQRlRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
410
....*....|....*..
gi 1622845278 497 LEYMRKLEARLEKVADE 513
Cdd:TIGR02169 729 EQEEEKLKERLEELEED 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-375 |
2.70e-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: 65.94 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQG 224
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 225 DHVARILELEDDIQTISEKVLTKEV-------ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnrrLN 297
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845278 298 LDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLrgaQELAASSQQKATLLGEELASAATARDR 375
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-513 |
3.10e-11 |
|
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: 67.07 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQ-----LEGQVTELRSRVQELERALATARQEHAELMEQYKGISRshgEITEERDILSRQQ 223
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 224 GDHVARILEL-----------EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:pfam15921 320 SDLESTVSQLrselreakrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 293 NRRL---------------------NLDLQ--EA--KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRG 347
Cdd:pfam15921 400 NKRLwdrdtgnsitidhlrrelddrNMEVQrlEAllKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 348 -AQELAA------SSQQKATLLGEELASAATARDRTIAELHRSRlevAEVNGRLAELGlHLK--EEKCQWSKERAGLLQS 418
Cdd:pfam15921 480 vVEELTAkkmtleSSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQ-HLKneGDHLRNVQTECEALKL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 419 VEAEKDKILK-LSAEILRLEKAV-QEERTQN--QVFKTELAREKDSSLVQLSESK-------RELTELRSALRVLQKEKE 487
Cdd:pfam15921 556 QMAEKDKVIEiLRQQIENMTQLVgQHGRTAGamQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKV 635
|
410 420
....*....|....*....|....*.
gi 1622845278 488 QLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQERDQLLNE 661
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-513 |
3.82e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 162 DLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITE-ERDILSRQQgdhvaRILELEDDIQTI 240
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElEKELESLEG-----SKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 241 SEKVLTKEVELDRLRDTVKALT--REQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLK 318
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 319 DKVAQMKDTLGQAQQRVAELE---PLKEQLRG-AQELAASSQQKatlLGEELASAATARDRTIAELHRSRLEVAEVNGRL 394
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEeakAKKEELERlKKRLTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 395 AELGLHLKEEKCQWSK-----------ERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTqnqvfKTELAREKDSSLV 463
Cdd:PRK03918 422 KELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELI 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 464 QLSESKRELTELRSALRVLQKEK-EQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-514 |
4.46e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAEL---MEQYKGISRSHGEITEERDILSRQQGd 225
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLellLSNLKKKIQKNKSLESQISELKKQNN- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 226 hvarilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQ-----SEAELQVAQQENRRLNLDL 300
Cdd:TIGR04523 229 ------QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkiKELEKQLNQLKSEISDLNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 301 QEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaQELAASSQQKATlLGEELASAATARDRTIAEL 380
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK--KELTNSESENSE-KQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 381 HRSRLEVAEVNGRLAELGLHLKEEKcQWSKERAGLLQSVEAEKDKILK----LSAEILRLEKAVQEERTQNQVFKT---E 453
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEKELLEKeierLKETIIKNNSEIKDLTNQDSVKELiikN 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 454 LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
653-679 |
1.94e-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: 1.94e-10
10 20
....*....|....*....|....*..
gi 1622845278 653 KECPICKERFPAESDKDALEDHMDGHF 679
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-396 |
2.11e-10 |
|
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: 63.24 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 179 SRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRdtv 258
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 259 KALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAEL 338
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845278 339 EPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-503 |
2.94e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQ-------------YKGISRSHGEITEERDI 218
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 219 LSRQQGDHVARILELEDDIQTISEkvltKEVELDRLRDTVKALTREQEKLLGQLKEVQaDKEQSEAELQvaQQENRRLNL 298
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELE--RLKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 299 DLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAqelaassQQKATLLGEELASAATAR--DRT 376
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-------KGKCPVCGRELTEEHRKEllEEY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 377 IAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVfkTELAR 456
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL--KEKLI 535
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622845278 457 EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-372 |
3.25e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 144 PKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQykgISRSHGEITEERDILsrqq 223
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 224 GDHVARILELEDDIQTISEKVLTKEVE--LDRLrDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQ 301
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSdfLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 302 EAKSWQEEQSAQAQRLkdkVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATA 372
Cdd:COG3883 168 AAKAELEAQQAEQEAL---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
149-361 |
3.35e-10 |
|
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: 62.47 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQykgISRSHGEITEERDILSRQ------ 222
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 223 --QGDHVARILELEDDIQTISEKVLTKEVeLDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDL 300
Cdd:COG4942 116 lgRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 301 QEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATL 361
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-508 |
3.64e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 158 QERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDI 237
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 238 QTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEqseaELQVAQQENRRLnldLQEAKSWQEEQSaqaqrL 317
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR----TARERVEEAEAL---LEAGKCPECGQP-----V 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 318 KDkvAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKAtllgEELASAATARDRTIAELHRSRLEVAEVNGRLAEl 397
Cdd:PRK02224 462 EG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA----EDLVEAEDRIERLEERREDLEELIAERRETIEE- 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 398 glhlKEEKCQWSKERAGLLQSVEAEKDkilklsAEILRLEKAVQEERTQNQVFKTELAREKDS--SLVQLSESKRELTEL 475
Cdd:PRK02224 535 ----KRERAEELRERAAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADA 604
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622845278 476 RSALRVLQKEKEQLQEEKQELLEYM-------RKLEARLE 508
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLaekrerkRELEAEFD 644
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
170-497 |
4.48e-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: 62.92 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 170 LEGQVTELRSRVQELERALATARQEHAELMEQYKGISrshGEITEERDILSRQQgdhvARILELEDDIQTISEKVLTKEV 249
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA---GEIRDLKDMLDVKE----RKINVLQKKIENLQEQLRDKDK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVK-----------ALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAK-------------- 304
Cdd:pfam10174 416 QLAGLKERVKslqtdssntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKekvsalqpelteke 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 305 ----SWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQ-------------QKATLLGEELA 367
Cdd:pfam10174 496 ssliDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeindrirlleQEVARYKEESG 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 368 SAATARDRTIAELHRSRLEVAEVNGRLAEL--------------GLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEI 433
Cdd:pfam10174 576 KAQAEVERLLGILREVENEKNDKDKKIAELesltlrqmkeqnkkVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845278 434 LRLEKAVQEERTQNQVFKTELareKDSSLVQ-LSESKRELTELRSALRvlqKEKEQLQEEKQELL 497
Cdd:pfam10174 656 QLEELMGALEKTRQELDATKA---RLSSTQQsLAEKDGHLTNLRAERR---KQLEEILEMKQEAL 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-397 |
4.86e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 197 ELMEQYKGISRSHGEITEERdilsrQQGDHVARILELEDDIQTISEKVLtkevELDRLRDTVKA---------LTREQEK 267
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAR-----EQIELLEPIRELAERYAAARERLA----ELEYLRAALRLwfaqrrlelLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 268 LLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQ-SAQAQRLKDKVAQMKDTLGQAQQRVAELE-PLKEQL 345
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGlPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622845278 346 RGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAEL 397
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-456 |
5.31e-10 |
|
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: 61.70 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLg 329
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 330 QAQQRVAELEPLkeqlrgaqeLAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWS 409
Cdd:COG4942 114 YRLGRQPPLALL---------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622845278 410 KERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR 456
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-490 |
6.34e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEkvltkevELDRLRDTVKAL--TREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLdlqeaksWQEE 309
Cdd:COG4913 222 DTFEAADALVE-------HFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAALRL-------WFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 310 QsaQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAE 389
Cdd:COG4913 288 R--RLELLEAELEELRAELARLEAELERLEARLDALR--EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 390 VNGRLAELGLHLKEEkcqwskeragllqsveaekdkilklsaeilrlEKAVQEERTQNQVFKTELAREKDSSLVQLSESK 469
Cdd:COG4913 364 LEALLAALGLPLPAS--------------------------------AEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
250 260
....*....|....*....|.
gi 1622845278 470 RELTELRSALRVLQKEKEQLQ 490
Cdd:COG4913 412 AALRDLRRELRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-513 |
9.11e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 124 MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYK 203
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 204 G--ISRSHGEIteeRDILSRqqgdhVARILELEDDIQ---TISEKVLTKEVELDRLRDTVKALTREQEKLLG-QLKEVQA 277
Cdd:PRK03918 451 KelLEEYTAEL---KRIEKE-----LKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEK 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 278 DKEQSE---AELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAE-LEPLKEQLRGAQEL-- 351
Cdd:PRK03918 523 KAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFyn 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 352 ----AASSQQKATLLGEELASAATardrtiaELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagllqsVEAEKDKIL 427
Cdd:PRK03918 603 eyleLKDAEKELEREEKELKKLEE-------ELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEYL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 428 KLSAEILRLEKAVQEERTQNQvfktelarEKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLE--- 504
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRRE--------EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKera 741
|
410
....*....|
gi 1622845278 505 -ARLEKVADE 513
Cdd:PRK03918 742 lSKVGEIASE 751
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
152-512 |
1.71e-09 |
|
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: 61.14 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNDLMQLKLQLEGQVTELRS---RVQELERALATARQ-----EHAELMEQY-KGISRSHGEITE---ERDIL 219
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAqeaVLEETQERINRARKaaplaAHIKAVTQIeQQAQRIHTELQSkmrSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 220 SRQQGDHVARILELEDdiQTISEKVLTKEVELDRLRDTVKALTRE----QEKLLGQLKEVQADKEQSEAELQVAQQENRR 295
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEE--QRRLLQTLHSQEIHIRDAHEVATSIREiscqQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 296 LNLDLQEAKSWQEEQSAQAQRL----KDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEElaSAAT 371
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK--EQIH 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 372 ARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 452 TELAREKDSSLV---QLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVAD 512
Cdd:TIGR00618 563 EQMQEIQQSFSIltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-480 |
2.78e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 206 SRSHGEITEERDILSRQQ--GDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKL--LGQLKEVQADKEQ 281
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 282 SEAELQVAQQENRRL---NLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQK 358
Cdd:COG4913 666 AEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 359 AT------LLGEELASAATARDRTIAELHRSRLEvAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEA--EKDKIL-KL 429
Cdd:COG4913 746 ELralleeRFAAALGDAVERELRENLEERIDALR-ARLNRAEEELERAMRAFNREWPAETADLDADLESlpEYLALLdRL 824
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622845278 430 SAEIL--RLEKAVQEERTQNQVFKTELAREKDSSlvqLSESKRELTELRSALR 480
Cdd:COG4913 825 EEDGLpeYEERFKELLNENSIEFVADLLSKLRRA---IREIKERIDPLNDSLK 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-507 |
2.83e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDIlsrQQGDHV 227
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL---KEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILeleddiqTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA-DKEQSEAELQVAQQENRRLNLDLQEAKSW 306
Cdd:COG4717 252 LLIA-------AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLArEKASLGKEAEELQALPALEELEEEELEEL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 307 QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRgaqeLAASSQQKATLLGE----------ELASAATARDRT 376
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALLAEagvedeeelrAALEQAEEYQEL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 377 IAELHRSRLEVAEVNGRLAELGLHLKEEkcQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVfkTELAR 456
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQ 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622845278 457 EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQ-ELLEYMRKLEARL 507
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
151-509 |
7.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 151 NQLDESQQERNDLMQLKLQLEGQVTELRSR-VQELERALATARQEHAELMEQYKgisrshgEITEERDILSRQQGDHVAR 229
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEIS-------KITARIGELKKEIKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 230 ILELED----------DIQTISEKVLTKE--VELDRLRDTVKALTREQEKLLGQLKEVQ-ADKEQSE--AELQVAQQ--- 291
Cdd:PRK03918 428 IEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEkVLKKESEliKLKELAEQlke 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 292 -ENRRLNLDLQEAkswqEEQSAQAQRLKDKVAQMKdtlgqaqqrvAELEPLKEQLRGAQELaassQQKATLLGEELASAa 370
Cdd:PRK03918 508 lEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLK----------GEIKSLKKELEKLEEL----KKKLAELEKKLDEL- 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 371 tarDRTIAELHRSRLE-----VAEVNGRLAELG------LHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKA 439
Cdd:PRK03918 569 ---EEELAELLKELEElgfesVEELEERLKELEpfyneyLELKDAE----KELEREEKELKKLEEELDKAFEELAETEKR 641
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 440 VQEERTQNQVFKTELAREKdsslvqLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:PRK03918 642 LEELRKELEELEKKYSEEE------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-513 |
1.13e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 245 LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEaELQVAQQENRRlnldlQEAKSWQEEQSAQAQRLKDKVAQM 324
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKA-----DEAKKAEEAKKADEAKKAEEKKKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 325 KDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKAtllgEELASAATARDRTIAELHRSRLEVAEVNGRlaelglhlKEE 404
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAK--------KAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 405 KCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTELRSALRVLQK 484
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE-------EDKKKAEEAKKAEEDEKK 1689
|
250 260 270
....*....|....*....|....*....|.
gi 1622845278 485 EKEQLQEEKQEL--LEYMRKLEARLEKVADE 513
Cdd:PTZ00121 1690 AAEALKKEAEEAkkAEELKKKEAEEKKKAEE 1720
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
152-515 |
1.26e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDhVARIL 231
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEK--VLTKEVE-LDRLRDTVKALTREQEKLLGQL----KEVQADKEQ-------SEAELQVAQQENRRLN 297
Cdd:TIGR00618 383 TLQQQKTTLTQKlqSLCKELDiLQREQATIDTRTSAFRDLQGQLahakKQQELQQRYaelcaaaITCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 298 lDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE-PLKEQLRgaqelaaSSQQKATLLGEelASAATAR-DR 375
Cdd:TIGR00618 463 -ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcPLCGSCI-------HPNPARQDIDN--PGPLTRRmQR 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 376 TIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagllQSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfktELA 455
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ----QSFSILTQCDNRSKEDIPNLQNITVRLQDLTE----KLS 604
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 456 REKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKW 515
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-513 |
1.29e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 150 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELmeqykgisRSHGEITE-ERDILSRQQGDHVA 228
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------LAEAGLDDaDAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQE 308
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEP----LKEQLRGAQELAASSqqKATLLGEELASAATArdRTIAElhrSR 384
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEAtlrtARERVEEAEALLEAG--KCPECGQPVEGSPHV--ETIEE---DR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 385 LEVAEVNGRLAELglhlkeekcqwskeragllqsveaeKDKILKLSAEILRLEKAVQEERtqnqvfKTELAREKDSSLVQ 464
Cdd:PRK02224 475 ERVEELEAELEDL-------------------------EEEVEEVEERLERAEDLVEAED------RIERLEERREDLEE 523
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622845278 465 LSESKRE-LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK02224 524 LIAERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-380 |
1.38e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 185 ERALATARQEHAELMEQYKGISRSHGEITEERDILsRQQGDHVARILEL---EDDIQTISEKVLTKEVELDRLRDTVKAL 261
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 262 TREQEkllgQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQmkdtlgqaqqrvaELEPL 341
Cdd:COG4913 688 AALEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-------------ELRAL 750
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622845278 342 KEQLRGAQELAASSQQKATLLGEELASAATARDRTIAEL 380
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-292 |
2.30e-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: 55.32 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDI--LSRQQGDH 226
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845278 227 VARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
125-502 |
4.84e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 125 DELVTLEEADGGSDIllvvpkatvlqnQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQ--EHAELMEQY 202
Cdd:PRK02224 391 EEIEELRERFGDAPV------------DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPECG 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 203 KGISRS-HGEITEERDilsrqqgdhvARILELEDDIQTISEKVLTKEVELDRLRDTVKAlTREQEKLLGQLKEVQADKEQ 281
Cdd:PRK02224 459 QPVEGSpHVETIEEDR----------ERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 282 SEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAAssqqKATL 361
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA----AIAD 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 362 LGEELASAATARDrTIAELHRSRLE-VAEVNGRLAELGLHLKE---EKCQWSKERA--------GLLQSVEAEKDKILKl 429
Cdd:PRK02224 604 AEDEIERLREKRE-ALAELNDERRErLAEKRERKRELEAEFDEariEEAREDKERAeeyleqveEKLDELREERDDLQA- 681
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845278 430 saEILRLEKAVQEertqnqvfktelarekdssLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRK 502
Cdd:PRK02224 682 --EIGAVENELEE-------------------LEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
199-510 |
6.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 199 MEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQAD 278
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 279 KE---QSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRV---AELEPLKEQLRGAQELA 352
Cdd:PRK03918 237 KEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 353 ASSQQKATLLGEELASAATARDRT------IAELHRsRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLlqSVEAEKDKI 426
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLeelkkkLKELEK-RLEELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 427 LKLSAEILRLEKAVQEERTQNQVFKTELAREKDsSLVQLSESK-------RELTELRSA--LRVLQKEKEQLQEEKQELL 497
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKK-AIEELKKAKgkcpvcgRELTEEHRKelLEEYTAELKRIEKELKEIE 472
|
330
....*....|...
gi 1622845278 498 EYMRKLEARLEKV 510
Cdd:PRK03918 473 EKERKLRKELREL 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-339 |
6.66e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRsrVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDH-V 227
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILELEDDIQtisekvlTKEVELDRLRdtvkaltREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLnldLQEAKSWQ 307
Cdd:COG4913 338 DRLEQLEREIE-------RLERELEERE-------RRRARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEEL 400
|
170 180 190
....*....|....*....|....*....|..
gi 1622845278 308 EEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE 339
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-378 |
6.94e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 145 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRS---HGEITEERDIL-- 219
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrSGGSVSYLDVLlg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 220 SRQQGDHVARIleleDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLD 299
Cdd:COG3883 111 SESFSDFLDRL----SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 300 LQEakswqEEQSAQAQRlkdkvAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIA 378
Cdd:COG3883 187 LSA-----EEAAAEAQL-----AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
178-498 |
7.25e-08 |
|
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: 55.07 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 178 RSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDT 257
Cdd:pfam19220 47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 258 VKALTREQEKLLGQLKEVQADKEQSEAELQ--------------VAQQENRRLNLDLqeakswqEEQSAQAQRLKDKVAQ 323
Cdd:pfam19220 127 LAAETEQNRALEEENKALREEAQAAEKALQraegelatarerlaLLEQENRRLQALS-------EEQAAELAELTRRLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 324 MKDTLGQAQQRVAELE-PLKEQLRGAQELAASSQQKATLLGEELAS------AATAR----DRTIAELhRSRLEVAEVNG 392
Cdd:pfam19220 200 LETQLDATRARLRALEgQLAAEQAERERAEAQLEEAVEAHRAERASlrmkleALTARaaatEQLLAEA-RNQLRDRDEAI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 393 RLAELGlhLKEEkcqwSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELArEKDSSLVQLSESKREL 472
Cdd:pfam19220 279 RAAERR--LKEA----SIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALA-AKDAALERAEERIASL 351
|
330 340
....*....|....*....|....*..
gi 1622845278 473 TE-LRSALRVLQKEKEQLQEEKQELLE 498
Cdd:pfam19220 352 SDrIAELTKRFEVERAALEQANRRLKE 378
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
228-400 |
9.00e-08 |
|
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: 54.35 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILELEDDIQTISEKVLTKEVELDRLRdtvkALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQ 307
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQAELDRLQ----ALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 308 EEQSAQAQRL---KDKVAQMKDTLGQAQQRVAELEPLKEQLrgAQELAAssQQKATLLGEELASAATARDRTIAELHRSR 384
Cdd:pfam00529 134 PIGGISRESLvtaGALVAQAQANLLATVAQLDQIYVQITQS--AAENQA--EVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
170
....*....|....*..
gi 1622845278 385 LEV-AEVNGRLAELGLH 400
Cdd:pfam00529 210 TEIrAPVDGTVAFLSVT 226
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
238-516 |
1.20e-07 |
|
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: 55.23 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 238 QTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRL 317
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 318 KDKvaQMKDTLGQAQQRVAELEPLKEQLRG-AQELAASSQQKATLLGEELASAATARDRTIAELHRSRlevaevngrlae 396
Cdd:pfam12128 680 ANE--RLNSLEAQLKQLDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGA------------ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 397 lglhlKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAV-------QEERTQNQVFKTELAREKDSSLVQLSESK 469
Cdd:pfam12128 746 -----KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrQEVLRYFDWYQETWLQRRPRLATQLSNIE 820
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 470 RELTELRSALRVLQK---------EKEQLQEEKQ--ELLEYMRKLEARLEKVAD--EKWN 516
Cdd:pfam12128 821 RAISELQQQLARLIAdtklrraklEMERKASEKQqvRLSENLRGLRCEMSKLATlkEDAN 880
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
655-678 |
1.48e-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: 1.48e-07
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-353 |
2.23e-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: 54.29 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAElmeqykgisrshgeiteerdiLSRQQGDHVA 228
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ---------------------LELQIASLNN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTIsekvltkEVELDRLRDTVKALTREQEKLlgQLKEVQADKEQSEAELQVAQQENRRlnldLQEAKSWQE 308
Cdd:TIGR02168 401 EIERLEARLERL-------EDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELER----LEEALEELR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622845278 309 EQSAQAQRlkdKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAA 353
Cdd:TIGR02168 468 EELEEAEQ---ALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
237-513 |
2.24e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 237 IQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQR 316
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 317 LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRS--RLEVAEVNGRL 394
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQElqALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 395 AELGLHLKEEK-CQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELT 473
Cdd:COG4372 186 DELLKEANRNAeKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622845278 474 ELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
149-513 |
2.31e-07 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 53.92 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELerALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQtisekvltkevELDRLRDTVKALTREQEKLLGQLKEVQAD-KEQSEAELQVA--QQENRRLNLDLQEAKS 305
Cdd:COG4192 117 AVADLRNLLQ-----------QLDSLLTQRIALRRRLQELLEQINWLHQDfNSELTPLLQEAswQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 306 WQEEQSAQAQRLKDKVAQMKDTLGQ-AQQR-VAELEPLKEQLrgaQELAASSQQKATLLgEELASAATARdRTIAELhrs 383
Cdd:COG4192 186 NLQNELQLLLRLLAIENQIVSLLREvAAARdQADVDNLFDRL---QYLKDELDRNLQAL-KNYPSTITLR-QLIDEL--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 384 rLEVAEVNGRLAEL---GLHLKEEkcqwskeraglLQSVEAEKDKILKLSAEilRLEKAVQEERTQNQVFKTELAREKDS 460
Cdd:COG4192 258 -LAIGSGEGGLPSLrrdELAAQAT-----------LEALAEENNSILEQLRT--QISGLVGNSREQLVALNQETAQLVQQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 461 S------------------------------LVQLSES-----------------KRELTELRSALRV-LQKEKEQLQEE 492
Cdd:COG4192 324 SgilllaiallslllavlinyfyvrrrlvkrLNALSDAmaaiaagdldvpipvdgNDEIGRIARLLRVfRDQAIEKTQEL 403
|
410 420
....*....|....*....|.
gi 1622845278 493 KQELLEYMRkLEARLEKVADE 513
Cdd:COG4192 404 ETEIEERKR-IEKNLRQTQDE 423
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-494 |
2.33e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDlqeakswqeeqsAQAQRLKDKVAQMKDTLGQA 331
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 332 QQRVAELEPLKEQLRgaQELAASSQQKATLLGeelasaatarDRTIAELhrsRLEVAEVNGRLAELGLHLKEE-----KC 406
Cdd:COG3206 232 RAELAEAEARLAALR--AQLGSGPDALPELLQ----------SPVIQQL---RAQLAELEAELAELSARYTPNhpdviAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 407 QwsKERAGLLQSVEAEKDKIL-KLSAEILRLEKAVQEERTQNQVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKE 485
Cdd:COG3206 297 R--AQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELE-AELRRLEREVEVARELYESLLQR 373
|
....*....
gi 1622845278 486 KEQLQEEKQ 494
Cdd:COG3206 374 LEEARLAEA 382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-495 |
2.86e-07 |
|
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: 54.28 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQS 311
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 312 AQAQRLKDKVAQMKDtlgqAQQRVAELEPLKEQLRGAQELAAssQQKATLLGEELasaatarDRTIAELHRSRLEVAEVN 391
Cdd:TIGR00606 772 TLLGTIMPEEESAKV----CLTDVTIMERFQMELKDVERKIA--QQAAKLQGSDL-------DRTVQQVNQEKQEKQHEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 GRLAELGlhlkEEKCQWSKERAGLLQSVeaeKDKILKLSAEILRLEKAVQeERTQNQVFKTELAREKDSSLVQLSESKRE 471
Cdd:TIGR00606 839 DTVVSKI----ELNRKLIQDQQEQIQHL---KSKTNELKSEKLQIGTNLQ-RRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
250 260
....*....|....*....|....
gi 1622845278 472 LTELRSALRVLQKEKEQLQEEKQE 495
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKET 934
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-362 |
3.35e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLK--LQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRshgEITEERDILSRQQGDH 226
Cdd:COG3206 187 LRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA---QLGSGPDALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 227 VarileleddIQTISEKVLTKEVELDRLRDT-------VKALTREQEKLLGQLK-EVQADKEQSEAELQVAQQENRRLNL 298
Cdd:COG3206 264 V---------IQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 299 DLQEakswQEEQSAQAQRLKDKVAQMKDTLGQAQQRvaeLEPLKEQLRGAQELAASSQQKATLL 362
Cdd:COG3206 335 QLAQ----LEARLAELPELEAELRRLEREVEVAREL---YESLLQRLEEARLAEALTVGNVRVI 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-512 |
3.57e-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: 53.58 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELM-------EQYKGISRSH------------ 209
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLedsntqiEQLRKMMLSHegvlqeirsilv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 210 ------GEITEERDILS----RQQGDHVARIL-ELEDDIQTISEKVLTKEVELdrlrDTVKALTREQEKLLGQLKEVQAD 278
Cdd:pfam15921 195 dfeeasGKKIYEHDSMStmhfRSLGSAISKILrELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQHQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 279 KEQSEAELQVAQQENRRLNLDLQeAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEP-LKEQLRGAQELAASSQQ 357
Cdd:pfam15921 271 QLISEHEVEITGLTEKASSARSQ-ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSeLREAKRMYEDKIEELEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 358 KATLLGEELASAATARDRTIAELHR--SRLE--VAEVNGRLAELGLHLKEEKCQWSKERAGLLqSVEAEKDKILKLSAEI 433
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNldDQLQklLADLHKREKELSLEKEQNKRLWDRDTGNSI-TIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 434 LRLEKAVqeertqnQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVAD 512
Cdd:pfam15921 429 QRLEALL-------KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
159-505 |
3.80e-07 |
|
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: 53.80 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 159 ERNDLMQLKLQLEGQVTELRsrvqeleRALATARQEHAELMEQYKGISRSHGEITEERDILS----------RQQ---GD 225
Cdd:COG3096 279 ERRELSERALELRRELFGAR-------RQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlnlvqtalRQQekiER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 226 HVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA--DKEQSEAeLQVAQ-----QENRRL-- 296
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQalDVQQTRA-IQYQQavqalEKARALcg 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 297 --NLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE---PLKEQLRGAQELAASSQQKATLLGE-----EL 366
Cdd:COG3096 431 lpDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEkayELVCKIAGEVERSQAWQTARELLRRyrsqqAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 367 ASAATARDRTIAELHRSRLEVAEVNGRLAELGLH----------LKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRL 436
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRigqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 437 EKAVQEERTQNQVFktelaREKDSSLVQLSE-------SKRELTELRSAL----RVLQKEKEQLQEEKQELLEYMRKLEA 505
Cdd:COG3096 591 RARIKELAARAPAW-----LAAQDALERLREqsgealaDSQEVTAAMQQLlereREATVERDELAARKQALESQIERLSQ 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
258-512 |
4.00e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 258 VKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLnlDLQEAKSWQEEQSAQAQRLKDkvaQMKDTLGQAQQRVAE 337
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELA--ELDEEIERYEEQREQARETRD---EADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 338 LEPLKEQLRGAQELAASSQQKATLLGEELASA-------ATARDRTIAELHRSRLEVAEVNGRLAElgLHLKEEKCQWSK 410
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLrerleelEEERDDLLAEAGLDDADAEAVEARREE--LEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 411 ERAGLlqSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKE----- 485
Cdd:PRK02224 331 EECRV--AAQAHNEEAESLREDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERfgdap 404
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622845278 486 ---------KEQLQEEKQELLEYMRKLEARLEKVAD 512
Cdd:PRK02224 405 vdlgnaedfLEELREERDELREREAELEATLRTARE 440
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-514 |
4.37e-07 |
|
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: 53.30 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 130 LEEADGGSDILLVVPKATVLQNQLD-------ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQY 202
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 203 KG-ISRSHGEITEERDILSRQQGDH----------VARILELEDDIQTISEKVltkEVELDRLRDTVKALTREQEKLLGQ 271
Cdd:pfam12128 307 NGeLSAADAAVAKDRSELEALEDQHgafldadietAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 272 LKEVQADKEQSEAELQVAQQENRRLNL-----DLQEAKS-WQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAEL---EPLK 342
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAKIREARDRQLavaedDLQALESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 343 EQLRGAQEL---AASSQQKATL----LGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGL-----------HLKEE 404
Cdd:pfam12128 464 LQLENFDERierAREEQEAANAeverLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqagtllhFLRKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 405 KCQWSKERAGLLQS------------VEAEKDKILKL-----------------SAEILRLEKAVQEERTQNQvfkTELA 455
Cdd:pfam12128 544 APDWEQSIGKVISPellhrtdldpevWDGSVGGELNLygvkldlkridvpewaaSEEELRERLDKAEEALQSA---REKQ 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 456 REKDSSLVQLS----ESKRELTELRSA-------LRVLQKEKEQLQEEKQELL-EYMRKLEARLEKVADEK 514
Cdd:pfam12128 621 AAAEEQLVQANgeleKASREETFARTAlknarldLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQL 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-513 |
9.39e-07 |
|
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: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGIS-RSHGEITEERDILSRQQGDHVARI 230
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 231 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQ---------VAQQENRRLNLDlq 301
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelreleaeIASLERRKSNIP-- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 302 eakswqeeqsAQAQRLKDkvaQMKDTLGQAQQR---VAEL---EPLKEQLRGAQELAASSqQKATLL------------- 362
Cdd:COG4913 440 ----------ARLLALRD---ALAEALGLDEAElpfVGELievRPEEERWRGAIERVLGG-FALTLLvppehyaaalrwv 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 363 ----------------GEELASAATARDRTIAElhrsRLEVAE------VNGRLAELGLHLK----EE--KCQWSKERAG 414
Cdd:COG4913 506 nrlhlrgrlvyervrtGLPDPERPRLDPDSLAG----KLDFKPhpfrawLEAELGRRFDYVCvdspEElrRHPRAITRAG 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 415 LLQSVEA--EKD-----------------KILKLSAEILRLEKAVQEERTQNQVFKTELA-------------------- 455
Cdd:COG4913 582 QVKGNGTrhEKDdrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDalqerrealqrlaeyswdei 661
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845278 456 ---------REKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG4913 662 dvasaereiAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-514 |
9.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 317 LKDKVAQMKDTLGQAQQR-----VAELEPLKEQLRGAQELAASSQQKAtllgEELASAATARDRTIAELHRSRLEVAEVN 391
Cdd:COG4717 47 LLERLEKEADELFKPQGRkpelnLKELKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 GRLAELGLHLKEEKCQwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRE 471
Cdd:COG4717 123 KLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622845278 472 LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-514 |
1.05e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQgdHVA 228
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAE---LQVAQQENRRLNLDLQEAKS 305
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKALLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 306 WQEEQSAQAQRLKDKV-------AQMKDTLGQAQQRVAeLEPLKEQLRGAQELAASSQQKATLLGEELASAA--TARDRT 376
Cdd:TIGR02168 514 NQSGLSGILGVLSELIsvdegyeAAIEAALGGRLQAVV-VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTeiQGNDRE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 377 IAELHRSRLEVAE------------VNGRLAEL--------GLHL-KEEKCQW-------------------SKERAGLL 416
Cdd:TIGR02168 593 ILKNIEGFLGVAKdlvkfdpklrkaLSYLLGGVlvvddldnALELaKKLRPGYrivtldgdlvrpggvitggSAKTNSSI 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 417 QSVEAEKD----KILKLSAEILRLEKAVQEERTQNQVFKTELA---REKDSSLVQLSESKRELTELRSALRVLQKEKEQL 489
Cdd:TIGR02168 673 LERRREIEeleeKIEELEEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
410 420
....*....|....*....|....*
gi 1622845278 490 QEEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEEL 777
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-557 |
1.09e-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: 52.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQvAQQENRRLNLDLQEAKSWQEEQS 311
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 312 AQAQRLKDKVAQMKDTLGQAQQR---VAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 -----EVNGRLAELGLHLKEEKCQWSKERAGLLQSVE-----AEKDKILKLSAEILRLEKAVQEERTQNQ--------VF 450
Cdd:TIGR00618 350 lhsqeIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttlTQKLQSLCKELDILQREQATIDTRTSAFrdlqgqlaHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 451 KTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQEL--LEYMRKLEARLEKVADEKWNEDAATDEEAAAG 528
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340
....*....|....*....|....*....
gi 1622845278 529 LSCPAALTDSEDESPEDMRLPPYGLCEHR 557
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
219-508 |
1.22e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 219 LSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKE-------VQADKEQSEAELQVAQQ 291
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElneqlqaAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 292 ENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkeqlrgaQELAASSQQKATLLGEELASAAT 371
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE---------EQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 372 ARDRTIAELhrsrleVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:COG4372 180 EAEQALDEL------LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845278 452 TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
170-347 |
1.39e-06 |
|
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: 51.88 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 170 LEGQVTELRSRVQELERALAtaRQEHAElmEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEV 249
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLR--QQQNAE--RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQenrrlnldLQEAKSWQEEQSAQAQRLKDKVAQMKDTLG 329
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE--------VTAAMQQLLEREREATVERDELAARKQALE 657
|
170 180
....*....|....*....|....*.
gi 1622845278 330 QAQQRVA--------ELEPLKEQLRG 347
Cdd:COG3096 658 SQIERLSqpggaedpRLLALAERLGG 683
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
148-511 |
1.44e-06 |
|
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: 51.67 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 148 VLQNQLDESQQERNDLMQLKLQLEGQVTELRS---RVQELERALATARQEHAELMEqykgiSRSHGEITEERDILSRQQG 224
Cdd:pfam05557 136 ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKN-----SKSELARIPELEKELERLR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 225 DHVARILELEDDIQTISEKVLTKEVELDRL---RDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQ 301
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEVEDLKRKLEREekyREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 302 EAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEE---------------- 365
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKErdgyrailesydkelt 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 366 LASAATARDRTIAELH-------------RSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLL-QSVEAEKDKILKLSA 431
Cdd:pfam05557 371 MSNYSPQLLERIEEAEdmtqkmqahneemEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdPSYSKEEVDSLRRKL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 432 EILRLEkaVQEERTQNQVFKTELARE--------KDSSLVQLSESKRELtelrsALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:pfam05557 451 ETLELE--RQRLREQKNELEMELERRclqgdydpKKTKVLHLSMNPAAE-----AYQQRKNQLEKLQAEIERLKRLLKKL 523
|
....*...
gi 1622845278 504 EARLEKVA 511
Cdd:pfam05557 524 EDDLEQVL 531
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-508 |
3.42e-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: 50.56 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEiTEERDILSRQQGDHVA 228
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE-AEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RilELEDDIQTISEKVLTKEVELDRLRdtvkALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQE------ 302
Cdd:pfam01576 468 S--QLQDTQELLQEETRQKLNLSTRLR----QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagtle 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 303 -----AKSWQEEQSAQAQRLKDKVAQMkDTLGQAQQRV-AELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRT 376
Cdd:pfam01576 542 aleegKKRLQRELEALTQQLEEKAAAY-DKLEKTKNRLqQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARY 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 377 IAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSK-ERAGLLQSVEAE-----KDKILKLSAEILR----LEKAVQEERTQ 446
Cdd:pfam01576 621 AEERDRAEAEAREKETRALSLARALEEALEAKEElERTNKQLRAEMEdlvssKDDVGKNVHELERskraLEQQVEEMKTQ 700
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845278 447 NQVFKTELAREKDSSL---VQLSESKRELTelrsalRVLQKEKEQLQEEKQELLEYMRKLEARLE 508
Cdd:pfam01576 701 LEELEDELQATEDAKLrleVNMQALKAQFE------RDLQARDEQGEEKRRQLVKQVRELEAELE 759
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
165-514 |
3.45e-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: 50.74 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 165 QLKLQLEGQVTELRSRVQELERALATARQEhaeLMEQYKGISRshgeiTEERDILSRQQGDHV--ARILELEDDIQTISE 242
Cdd:pfam02463 668 LSELTKELLEIQELQEKAESELAKEEILRR---QLEIKKKEQR-----EKEELKKLKLEAEELlaDRVQEAQDKINEELK 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 243 KVLTK--EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENR----RLNLDLQEAKSWQEEQSAQAQR 316
Cdd:pfam02463 740 LLKQKidEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeklkAQEEELRALEEELKEEAELLEE 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 317 LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 397 LGLHLKEEKCQWSKERAGLLQSVEAEKDKIL-KLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTEL 475
Cdd:pfam02463 900 KELEEESQKLNLLEEKENEIEERIKEEAEILlKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622845278 476 RSALRVLQK-------EKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:pfam02463 980 IEEFEEKEErynkdelEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-514 |
3.47e-06 |
|
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: 50.51 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 155 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQ----EHAELMEQYKGISRSHGEITEERDILSRQqgdhVARI 230
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldrESDRNQELQKRIRLLEKREAEAEEALREQ----AELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 231 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQ 310
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 311 SAQAQRLKDKVAQMKD----------------TLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARD 374
Cdd:pfam05557 159 EKQQSSLAEAEQRIKElefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 375 RtiaeLHRSRLEVAEVNGRLAELGLHLKEekcqWSKeragLLQSVEAEKDKILKLSAEILRLEkavQEERTqnqvfkteL 454
Cdd:pfam05557 239 R----EEKYREEAATLELEKEKLEQELQS----WVK----LAQDTGLNLRSPEDLSRRIEQLQ---QREIV--------L 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 455 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKER 355
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-514 |
4.18e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 230 ILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEE 309
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 310 Q---SAQAQRLKDKVAQMKDTLGQAQQrvaELEPLKEQLRGAQelaassQQKATLLGEElasaatarDRTIAELHRSRLE 386
Cdd:TIGR04523 213 NkslESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQ------TQLNQLKDEQ--------NKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 387 VAEVNGRLAELglhlkeekcqwskeragllqsveaeKDKILKLSAEILRLEKavQEERTQNQVFKTELA---REKDSSLV 463
Cdd:TIGR04523 276 LEQNNKKIKEL-------------------------EKQLNQLKSEISDLNN--QKEQDWNKELKSELKnqeKKLEEIQN 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 464 QLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
173-506 |
4.48e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 173 QVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILS----------RQQGD---HVARILELEDDIQT 239
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtalRQQEKierYQADLEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 240 ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA--DKEQSEA--------ELQVAQQENRRLNLDLQEAKSWQEE 309
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQalDVQQTRAiqyqqavqALERAKQLCGLPDLTADNAEDWLEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 310 QSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLR---GAQELAASSQQKATLLGE-----ELASAATARDRTIAELH 381
Cdd:PRK04863 447 FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiaGEVSRSEAWDVARELLRRlreqrHLAEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 382 RSRLEVAEVNGRLAELGLH----------LKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFk 451
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRlgknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW- 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845278 452 telaREKDSSLVQLSE-------SKRELTELRSAL----RVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:PRK04863 606 ----LAAQDALARLREqsgeefeDSQDVTEYMQQLlereRELTVERDELAARKQALDEEIERLSQP 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-382 |
4.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 151 NQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILsrqqgdhvar 229
Cdd:PRK02224 522 EELIAERRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL---------- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 230 ileleDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLnlDLQEAKSWQEE 309
Cdd:PRK02224 592 -----ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE--DKERAEEYLEQ 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 310 QSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLrgaQELAASSQQKATLLGE--ELASA-----ATARDRTIAELHR 382
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRERR---EALENRVEALEALYDEaeELESMygdlrAELRQRNVETLER 741
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-506 |
5.02e-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: 50.17 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 147 TVLQNQLD-------ESQQERNDLMQLKLQLEGQVTELRSRVQELERalaTARQEHAELMEQYKGISRSHGEITEERDIL 219
Cdd:pfam01576 43 NALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEE---RSQQLQNEKKKMQQHIQDLEEQLDEEEAAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 220 SRQQGDHV---ARILELEDDIQTISEK--VLTKEVEL--DRLRDTVKALTREQEKlLGQLKEVQADKEQSEAELQVAQQE 292
Cdd:pfam01576 120 QKLQLEKVtteAKIKKLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEK-AKSLSKLKNKHEAMISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 293 NRRLNLDLQEAKSWQEEQSAQAQ-RLKDKVAQMKDTLGQAQQRVAELEPLkeQLRGAQELAASSQQKATL---------L 362
Cdd:pfam01576 199 EEKGRQELEKAKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAA--LARLEEETAQKNNALKKIreleaqiseL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 363 GEELASAATARDRtiAELHRSRLEvaevngrlaelglhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQE 442
Cdd:pfam01576 277 QEDLESERAARNK--AEKQRRDLG----------------EELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEE 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 443 ERTQNQVFKTELAREKDSSLVQLSEskrELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:pfam01576 339 ETRSHEAQLQEMRQKHTQALEELTE---QLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-492 |
5.49e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 171 EGQVTELRSRVQELERALATARQEHAELMEQYKgisrshgEITEERDILSRqqgdHVARILELEDDiqTISEKVLTKEVE 250
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSALNR----LLPRLNLLADE--TLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 251 LDRLRDTvKALTREQEKLLGQLkevqadkEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDkVAQMKDTLG- 329
Cdd:PRK04863 903 LDEAEEA-KRFVQQHGNALAQL-------EPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTE-VVQRRAHFSy 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 330 -QAQQRVAELEPLKEQLRGAQELAassQQKATLLGEEL-ASAATARDRT------IAELHRSRLEVAEVNGRLAELGLHL 401
Cdd:PRK04863 974 eDAAEMLAKNSDLNEKLRQRLEQA---EQERTRAREQLrQAQAQLAQYNqvlaslKSSYDAKRQMLQELKQELQDLGVPA 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 402 KEEkcqwSKERAGLLQSveaekdkilklsaeilRLEKAVQEERTQnqvfktelareKDSSLVQLSESKRELTELRSALRV 481
Cdd:PRK04863 1051 DSG----AEERARARRD----------------ELHARLSANRSR-----------RNQLEKQLTFCEAEMDNLTKKLRK 1099
|
330
....*....|.
gi 1622845278 482 LQKEKEQLQEE 492
Cdd:PRK04863 1100 LERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
250-425 |
6.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQE---KLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRlkdkvAQMKD 326
Cdd:COG4717 72 ELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-----AELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 327 TLGQAQQRVAELEPLKEQLRGA-QELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAElglhLKEEK 405
Cdd:COG4717 147 RLEELEERLEELRELEEELEELeAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE----AQEEL 222
|
170 180
....*....|....*....|
gi 1622845278 406 CQWSKERAGLLQSVEAEKDK 425
Cdd:COG4717 223 EELEEELEQLENELEAAALE 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
264-513 |
6.46e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.67 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 264 EQEKLLGQLKEVQADKEQSEAELQVAqqenrrlnldLQEAKSWQEEQSAQAQRLKdkvaqmkdtlgQAQQRVAELEPLKE 343
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEA----------LQSALNWLEERKGSLERAK-----------QYQQVIDNFPKLSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 344 QLRgaqelaassQQKATLLGEELASAATArdrTIAELHRsrlEVAEVNGRLAELGLHLKEEKcQWSKERAGLLQSVEAEK 423
Cdd:PRK10929 83 ELR---------QQLNNERDEPRSVPPNM---STDALEQ---EILQVSSQLLEKSRQAQQEQ-DRAREISDSLSQLPQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 424 DKILKLSAEILRLEKAVQ-----EERTQNQVFKTELAREK----DSSLVQLSESKR-ELTELRSALrvLQKEKEQLQEEK 493
Cdd:PRK10929 147 TEARRQLNEIERRLQTLGtpntpLAQAQLTALQAESAALKalvdELELAQLSANNRqELARLRSEL--AKKRSQQLDAYL 224
|
250 260
....*....|....*....|....*...
gi 1622845278 494 QEL---LEYMRKLEA-----RLEKVADE 513
Cdd:PRK10929 225 QALrnqLNSQRQREAeraleSTELLAEQ 252
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
194-508 |
9.23e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 194 EHAELMEQYKGiSRSHGEITeerdilSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLK 273
Cdd:PRK10246 168 ERAELLEELTG-TEIYGQIS------AMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 274 EVQADKEQSEAELQVAQQENRRLNLdLQEAKswQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRG-AQELA 352
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQA-LQQAL--AAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQqIEEVN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 353 ASSQQKATLLGEELASAATARDRTIAELhrsrlevAEVNGRLAElglhlKEEKCQWSKERAG---LLQSVEAEKDKILKL 429
Cdd:PRK10246 318 TRLQSTMALRARIRHHAAKQSAELQAQQ-------QSLNTWLAE-----HDRFRQWNNELAGwraQFSQQTSDREQLRQW 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 430 SAeilRLEKAVQEERTQNQVFKTELAREKDSSLVQLSES---KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:PRK10246 386 QQ---QLTHAEQKLNALPAITLTLTADEVAAALAQHAEQrplRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAA 462
|
..
gi 1622845278 507 LE 508
Cdd:PRK10246 463 LN 464
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-289 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 147 TVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALA----TARQEHAELMEQYKGISRSHGEITEE------- 215
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAElerlqee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 216 ----RDILSRQQGDHVARILELEDDIQTISEKVLTK------EVELD-RLRD----------TVKALTREQEKLLGQLK- 273
Cdd:pfam09787 123 lrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqssssQSELEnRLHQltetliqkqtMLEALSTEKNSLVLQLEr 202
|
170
....*....|....*..
gi 1622845278 274 -EVQADKEQSEAELQVA 289
Cdd:pfam09787 203 mEQQIKELQGEGSNGTS 219
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
276-388 |
1.34e-05 |
|
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: 47.80 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 276 QADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAAS- 354
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIg 136
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622845278 355 --SQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:pfam00529 137 giSRESLVTAGALVAQAQANLLATVAQLDQIYVQIT 172
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-509 |
1.41e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 157 QQERNDLMQLKLQLEGQVTELRSRVQELERALATARQE-HAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELE- 234
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEmHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEn 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 235 -------------DDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNldlq 301
Cdd:pfam05483 255 kmkdltflleesrDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT---- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 302 eakswqEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEplkEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELH 381
Cdd:pfam05483 331 ------EEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 382 RSRLEVAEVNGRLAELGLHLKEEKcQWSK----------ERAGLLQSVEAEkdkILKLSAEILRLEKAVQEERTQNQVFK 451
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKK-QFEKiaeelkgkeqELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845278 452 TELAREK------DSSLVQLSESKRELTELRSALRV-LQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:pfam05483 478 TELEKEKlknielTAHCDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIENLEEK 542
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-492 |
1.45e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 171 EGQVTELRSRVQELERALATARQEHAELMEQYKgisrshgEITEERDILSRQQG--------DHVARILELEDDIQTISE 242
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKLLPqanlladeTLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 243 K---VLTKEVELDRLRDTVKALTREQEkllgQLKEVQADKEQSEAELQVAQQE--------NRRLNLDLQEAKSWQEEQS 311
Cdd:COG3096 908 AqafIQQHGKALAQLEPLVAVLQSDPE----QFEQLQADYLQAKEQQRRLKQQifalsevvQRRPHFSYEDAVGLLGENS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 312 AQAQRLKDKVAQMkdtlgQAQQRVAeleplKEQLRGAQELAASSQQKATllgeELASAATARDRTIAELHRsrlevaevn 391
Cdd:COG3096 984 DLNEKLRARLEQA-----EEARREA-----REQLRQAQAQYSQYNQVLA----SLKSSRDAKQQTLQELEQ--------- 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 gRLAELGLHLKEEkcqwSKERAgllqsvEAEKDKIlklsaeilrlekavQEERTQNQVFKTELarEKdsslvQLSESKRE 471
Cdd:COG3096 1041 -ELEELGVQADAE----AEERA------RIRRDEL--------------HEELSQNRSRRSQL--EK-----QLTRCEAE 1088
|
330 340
....*....|....*....|.
gi 1622845278 472 LTELRSALRVLQKEKEQLQEE 492
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQEREQ 1109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-513 |
1.53e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 147 TVLQNQLDESQQERNDLMQLKLQLEgqvtELRSRVQELERALATARQEHAELME-----QYKGISRSHGEITEERDILSR 221
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIE----RLEARLERLEDRRERLQQEIEELLKkleeaELKELQAELEELEEELEELQE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 222 QQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLG------QLKEVQAD--------------KEQ 281
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGlsgilgvlselisvDEG 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 282 SEAELQVAQQEnRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMK-DTLGQAQQRVAELEPLKEQ---------------- 344
Cdd:TIGR02168 535 YEAAIEAALGG-RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPlDSIKGTEIQGNDREILKNIegflgvakdlvkfdpk 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 345 -----------------LRGAQELAASSQQKA---TLLGE-------------ELASAATARDRTIAELhrsRLEVAEVN 391
Cdd:TIGR02168 614 lrkalsyllggvlvvddLDNALELAKKLRPGYrivTLDGDlvrpggvitggsaKTNSSILERRREIEEL---EEKIEELE 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 GRLAELglhlkeekcqwSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvQLSESKRE 471
Cdd:TIGR02168 691 EKIAEL-----------EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE----RIAQLSKE 755
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622845278 472 LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-506 |
1.92e-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: 48.25 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 162 DLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHgeiteERDILSR-QQGDHVARIL--------- 231
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF-----ERDLQARdEQGEEKRRQLvkqvrelea 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTK---EVELDRLRDTVKALTREQEKLLGQLKEVQAdkeqseaelqvaqqENRRLNLDLQEAKSWQE 308
Cdd:pfam01576 757 ELEDERKQRAQAVAAKkklELDLKELEAQIDAANKGREEAVKQLKKLQA--------------QMKDLQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQlrgaqelaasSQQKATLLGEELASAATARDRTIAElhRSRLEva 388
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ----------AQQERDELADEIASGASGKSALQDE--KRRLE-- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 evnGRLAELGLHLKEEKCqwskeragllqSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfKTELAREKDSSlvQLSES 468
Cdd:pfam01576 889 ---ARIAQLEEELEEEQS-----------NTELLNDRLRKSTLQVEQLTTELAAERSTSQ--KSESARQQLER--QNKEL 950
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622845278 469 KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 506
Cdd:pfam01576 951 KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESR 988
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-444 |
2.74e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQE 308
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845278 389 EVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEER 444
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-514 |
2.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 171 EGQVTELRSRVQELERALATARQEHAELMEQykgiSRSHGEITEERDILSRQQGDHV--ARILELEDDIQTISEKVLTKE 248
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAeaARKAEEERKAEEARKAEDAKK 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 249 VELDRLRDTVKALTREQEKllgQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDtl 328
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE-- 1300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 329 gqaQQRVAELEPLKEQLRGAQEL---AASSQQKATLL---GEELASAATARDRTiAELHRSRLEVAEVNGRLAELGLHLK 402
Cdd:PTZ00121 1301 ---KKKADEAKKKAEEAKKADEAkkkAEEAKKKADAAkkkAEEAKKAAEAAKAE-AEAAADEAEAAEEKAEAAEKKKEEA 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 403 EEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSalrvl 482
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK----- 1451
|
330 340 350
....*....|....*....|....*....|..
gi 1622845278 483 QKEKEQLQEEKQELLEYMRKLEaRLEKVADEK 514
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEA 1482
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-507 |
2.79e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQwsKE 411
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 412 RAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTELRSALRVLQKEKEQLQE 491
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|....*.
gi 1622845278 492 EKQELLEymrKLEARL 507
Cdd:COG1579 164 EREELAA---KIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
250-397 |
2.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKswqeeqsAQAQRLKDKVAQMKDT-- 327
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 328 -------LGQAQQRVAELE----PLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRsrlEVAEVNGRLAE 396
Cdd:COG1579 91 yealqkeIESLKRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAEREE 167
|
.
gi 1622845278 397 L 397
Cdd:COG1579 168 L 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
232-514 |
3.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQAdkeqseaELQVAQQENRRLNLDLQEAKSWQEEQS 311
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 312 AQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQElaasSQQKATLLGEElasaatarDRTIAElhrsrlevaevn 391
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEW----RQQTEVLSPEE--------EKELVE------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 gRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfKTELAREKDSSLVQLSESKRE 471
Cdd:COG1340 141 -KIKEL------------EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK----IKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 472 LTELRSALRVLQKEKEQLQEE-----------KQELLEYMRKLEARLEKVADEK 514
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKadelheeiielQKELRELRKELKKLRKKQRALK 257
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
158-492 |
3.35e-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: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 158 QERNDLMQLKLQLEGQVTELRSR----VQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQqgdhvariLEL 233
Cdd:pfam15964 307 KERDDLMSALVSVRSSLAEAQQRessaYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKE--------LAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 234 EDDIQTISEKVLTKEVELDR--LRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQS 311
Cdd:pfam15964 379 QQEKRAQEKEALRKEMKKEReeLGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 312 AQAQRLKDKVAQ-----MKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLE 386
Cdd:pfam15964 459 NQTKMKKDEAEKehreyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLE 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKA----VQEERTQNQVFKTELAREKDSSL 462
Cdd:pfam15964 539 KESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTfiakLKEECCTLAKKLEEITQKSRSEV 618
|
330 340 350
....*....|....*....|....*....|
gi 1622845278 463 VQLSESKRELTElrsALRVLQKEKEQLQEE 492
Cdd:pfam15964 619 EQLSQEKEYLQD---RLEKLQKRNEELEEQ 645
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-495 |
3.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 248 EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAkswQEEQSAQAQRLKDKVAQMKDT 327
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 328 LGQAQQRVAELEPLkEQLRGAQELAassqqkatllgeELASAATARDRtIAELHRSRLEvaEVNGRLAElglhLKEEKcq 407
Cdd:COG3883 92 ARALYRSGGSVSYL-DVLLGSESFS------------DFLDRLSALSK-IADADADLLE--ELKADKAE----LEAKK-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 408 wskeragllQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE 487
Cdd:COG3883 150 ---------AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
....*...
gi 1622845278 488 QLQEEKQE 495
Cdd:COG3883 221 AAAAAAAA 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-510 |
3.89e-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: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEddiqtisekvltkevelDRLRDTVKaLTREQEKLLGQLkevqaDKEQSEAELQVAQQENRRLNLDLQEAKSWQE 308
Cdd:pfam01576 188 MISDLE-----------------ERLKKEEK-GRQELEKAKRKL-----EGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAqRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:pfam01576 245 LQAALA-RLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 EVNGRLAELGLHLKEEK----CQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELarekdSSLVQ 464
Cdd:pfam01576 324 KREQEVTELKKALEEETrsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL-----RTLQQ 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622845278 465 L-SESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKV 510
Cdd:pfam01576 399 AkQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-448 |
4.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 234 EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQ 313
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 314 AQR--------------------------LKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELA 367
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 368 SAATARDRTIAELhrsRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQN 447
Cdd:COG3883 175 AQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
.
gi 1622845278 448 Q 448
Cdd:COG3883 252 A 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
180-514 |
4.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 180 RVQELERALATARQEHAELMEQYKGISRSHgEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVK 259
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 260 AltrEQEKllgQLKEVQADKEQSEAELQVAQQENRRlnlDLQEAKSWQEEQSAQAQRlKDKVAQMKDTLGQAQQRVAELE 339
Cdd:PTZ00121 1208 A---EEER---KAEEARKAEDAKKAEAVKKAEEAKK---DAEEAKKAEEERNNEEIR-KFEEARMAHFARRQAAIKAEEA 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 340 PLKEQLRGAQELAASSQQKATllgEELASAATARDRtiaelhrsrlevAEVNGRLAELglhlkEEKCQWSKERAGLLQSV 419
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKA---EEKKKADEAKKK------------AEEAKKADEA-----KKKAEEAKKKADAAKKK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 420 EAEK---DKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQ---EEK 493
Cdd:PTZ00121 1338 AEEAkkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaAAK 1417
|
330 340
....*....|....*....|....*.
gi 1622845278 494 QELLEYMRKLEAR-----LEKVADEK 514
Cdd:PTZ00121 1418 KKADEAKKKAEEKkkadeAKKKAEEA 1443
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
151-502 |
4.62e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 151 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDilsrqqgdhvari 230
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRD------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 231 lELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQvaQQENRRLNLDlqeakswqEEq 310
Cdd:COG1340 68 -ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEW--RQQTEVLSPE--------EE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 311 saqaQRLKDKVAQMKdtlgqaqqrvAELEPLKEQLRGAQELaassqqkatllgeelasaatarDRTIAELHRSRLEVAEV 390
Cdd:COG1340 136 ----KELVEKIKELE----------KELEKAKKALEKNEKL----------------------KELRAELKELRKEAEEI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 391 NGRLAELGlhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQnqvfktelareKDSSLVQLSESKR 470
Cdd:COG1340 180 HKKIKELA----EEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE-----------IIELQKELRELRK 244
|
330 340 350
....*....|....*....|....*....|....
gi 1622845278 471 ELTELRSALRVLQKEKEQ--LQEEKQELLEYMRK 502
Cdd:COG1340 245 ELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKK 278
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
176-399 |
5.07e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 176 ELRSRVQELERALATARQEHAELMEQYKGISR---SHGE---ITEERDILSrqqgdHVARILEledDIQTISEkvLTKEV 249
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEeeeLEEERRRLS-----NAEKLRE---ALQEALE--ALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 E---LDRLRDTVKALtREQEKLLGQLKEVQADKEQSEAELQVAQQENRRL--NLDLQEAK-SWQEEQSAQAQRLKDK--- 320
Cdd:COG0497 239 EggaLDLLGQALRAL-ERLAEYDPSLAELAERLESALIELEEAASELRRYldSLEFDPERlEEVEERLALLRRLARKygv 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 321 -VAQMKDTLGQAQQRVAELEplkeqlRGAQELAASSQQKATLLgEELASAAtardrtiAELHRSRLEVA-----EVNGRL 394
Cdd:COG0497 318 tVEELLAYAEELRAELAELE------NSDERLEELEAELAEAE-AELLEAA-------EKLSAARKKAAkklekAVTAEL 383
|
....*
gi 1622845278 395 AELGL 399
Cdd:COG0497 384 ADLGM 388
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
213-509 |
6.02e-05 |
|
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: 46.10 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 213 TEERDILSRQQGDHVARILELEDDIQTI---SEKVLTKEVELDRlRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVA 289
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEklgENAESSKRLNENA-NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 290 QQEnrrLNLDLQEAKSwqeEQSAQAQRLKDKVAQMKDTLgqaQQRVAELEPLKEQLRGAQELAASSqqkatllgEELASA 369
Cdd:COG5185 320 AAE---AEQELEESKR---ETETGIQNLTAEIEQGQESL---TENLEAIKEEIENIVGEVELSKSS--------EELDSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 370 ATARDRTIAELHRSRLEVAEVNGRLAE-----LGLHLKEEKcQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEER 444
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGYAQEILAtledtLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845278 445 TQNQVfktelarekdsslvqlSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 509
Cdd:COG5185 462 QSRLE----------------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-347 |
7.30e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 230 ILELEDDIQTISEKVLTKEVEL-----DRLRDTVKALTREqeklLGQLKEVQADKEQ-SEAELQVAQQENRRLNLDLQEA 303
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELlnsikPKLRDRKDALEEE----LRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIK 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622845278 304 KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRG 347
Cdd:smart00787 224 VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
271-507 |
7.88e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 271 QLKEVQAD---KEQSeaelqVAQQENRRLNLdLQEAKSwQEEQSAQAQRlkdKVAQMKDTLGQAQQRVAELEPLKEQLRG 347
Cdd:PRK11637 48 QLKSIQQDiaaKEKS-----VRQQQQQRASL-LAQLKK-QEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 348 AQelaaSSQQKatLLGEELASAATardrtiaelhrsrlevaevNGRLAELGLHLKEEKCQWSkERA----GLLQsvEAEK 423
Cdd:PRK11637 118 QQ----AAQER--LLAAQLDAAFR-------------------QGEHTGLQLILSGEESQRG-ERIlayfGYLN--QARQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 424 DKI--LKLSAEILRLEKAVQEE-RTQNQVFKTELAREKDSSLVQLSESKRELTELRSAlrvLQKEKEQLQEekqelleyM 500
Cdd:PRK11637 170 ETIaeLKQTREELAAQKAELEEkQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESS---LQKDQQQLSE--------L 238
|
....*..
gi 1622845278 501 RKLEARL 507
Cdd:PRK11637 239 RANESRL 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-513 |
9.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 176 ELRsRVQELERALATARQEHAELMEQYKGISRSHgEITEERDILSRQQGDHV------ARILELEDDIQTISEKVLTKEV 249
Cdd:PTZ00121 1186 EVR-KAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAkkdaeeAKKAEEERNNEEIRKFEEARMA 1263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAElqvaqqENRRLnldlQEAKSWQEEQSaQAQRLKDKVAQMKDTLG 329
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE------EKKKA----DEAKKKAEEAK-KADEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 330 QAQQRvAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRlevAEVNGRLAELglhlkEEKCQWS 409
Cdd:PTZ00121 1333 AAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---AEEKKKADEA-----KKKAEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 410 KERAGLLQSVEAEKDKI--LKLSAEILR----LEKAVQEERTQNQV-------FKTELAREKDSSLVQLSESKRELTELR 476
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKAdeAKKKAEEKKkadeAKKKAEEAKKADEAkkkaeeaKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622845278 477 SAlrvlQKEKEQLQEEKQELLEYMRKLEARleKVADE 513
Cdd:PTZ00121 1484 KA----DEAKKKAEEAKKKADEAKKAAEAK--KKADE 1514
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
147-592 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 147 TVLQNQLDESQQERNDLMQLKLQLEGQVTE---LRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQ 223
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 224 GDHV--------------ARILELEDDIQTIS-EKVLTKEVELDRLRdTVKALTREQEKLLGQLKEVQADKEQSEAELQV 288
Cdd:pfam15921 600 NDRRlelqefkilkdkkdAKIRELEARVSDLElEKVKLVNAGSERLR-AVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 289 AQQENR-----------RLNLDLQEAKSWQEEQSAQAQRLKD------KVA-----QMKDTLGQAQQRVAELEPLKEQLR 346
Cdd:pfam15921 679 LKRNFRnkseemetttnKLKMQLKSAQSELEQTRNTLKSMEGsdghamKVAmgmqkQITAKRGQIDALQSKIQFLEEAMT 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 347 GAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSkERAGLLQSVEAEKDKi 426
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQEQESVR- 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 427 LKL-----------------SAEILRLEKAVQEERTQNQVFKTE-----LAREKDSSLVQLSESKRELTELRSALRVLQK 484
Cdd:pfam15921 837 LKLqhtldvkelqgpgytsnSSMKPRLLQPASFTRTHSNVPSSQstasfLSHHSRKTNALKEDPTRDLKQLLQELRSVIN 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 485 EKEQLQEEKQELLEYMRKLEARLEKVADekwnEDAATDEEAAAGLSCPAALTDSEDESPEDMRLPPYGL--CEHRDPGSS 562
Cdd:pfam15921 917 EEPTVQLSKAEDKGRAPSLGALDDRVRD----CIIESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLhaGELEDPSSC 992
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622845278 563 PAGPREASPLVVIS---------QPAPISPHLSGPAEDS 592
Cdd:pfam15921 993 FTFPSTASPSVKNSasrsfhsspKKSPVHSLLTSSAEGS 1031
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
211-355 |
1.58e-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: 43.76 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 211 EITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTRE-------QEKLLGQLKEVQADKEQSE 283
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEieevearIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845278 284 AELQVAQQENRRLNL--DLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQR----VAELEPLKEQLRGAQELAASS 355
Cdd:COG1579 94 LQKEIESLKRRISDLedEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLAELEAELEELEAEREELAAK 171
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
241-397 |
2.05e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 241 SEKVLTKEVELDRLRDTVKALTReqekLLG----QLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQR 316
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELAD----LLSlerqGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 317 LKDKVAQMKDTLGQAQQRVAEL----EPLKEQLRGAQEL-------AASSQQKATLLGEELASAATARdrtIAELHRSRl 385
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLnqqiAALRRQLAALEAAldasekrDRESQAKIADLGRRLNVALAQR---VQELNRYR- 196
|
170
....*....|..
gi 1622845278 386 evAEVNGRLAEL 397
Cdd:PRK09039 197 --SEFFGRLREI 206
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
247-366 |
2.32e-04 |
|
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: 43.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 247 KEVELDRLRDTVKALTrEQEKllgQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQaqrLKDKVAQMKD 326
Cdd:pfam02841 185 KEAVEEAILQTDQALT-AKEK---AIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ---LIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622845278 327 TLGQAQQRVAELEpLKEQLRgaqELAASSQQKATLLGEEL 366
Cdd:pfam02841 258 QLLAEQERMLEHK-LQEQEE---LLKEGFKTEAESLQKEI 293
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-278 |
2.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEgqvtELRSRVQELERALATARQEHAELMEQYKGISRshgEITEERDILSR-QQGDHV 227
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEE---ELDELQDRLEAaEDLARL 745
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 228 ARILELEDDIQTISEKVLTKEVElDRLRDTVKALTREQEKLLGQLKEVQAD 278
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-513 |
3.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 145 KATVLQNQLDESQQERndLMQLKLQLEGQVTELRSRVQELERALATARQ-------EHAELMEQYKGISRSHGEITEERD 217
Cdd:COG4913 324 ELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAALRAEAAALLEALEEELE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 218 ILSRQQGDHVARILELEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEvQADKEQSE----AEL-QVAQQE 292
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEA-------EIASLERRKSNIPARLLALRDALAE-ALGLDEAElpfvGELiEVRPEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 293 ------------NRRLNL-----DLQEAKSW----QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE----P----LKE 343
Cdd:COG4913 474 erwrgaiervlgGFALTLlvppeHYAAALRWvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDfkphPfrawLEA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 344 QLRG---------AQELA---------------ASSQQKAT--------LLGEELASAATARDRTIAELHRSRLEVAEVN 391
Cdd:COG4913 554 ELGRrfdyvcvdsPEELRrhpraitragqvkgnGTRHEKDDrrrirsryVLGFDNRAKLAALEAELAELEEELAEAEERL 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 392 GRLAELGLHLKEEKCQWSKeragLLQSVEAEKDkILKLSAEILRLEKAVQEERTQNQVFKtELARekdsslvQLSESKRE 471
Cdd:COG4913 634 EALEAELDALQERREALQR----LAEYSWDEID-VASAEREIAELEAELERLDASSDDLA-ALEE-------QLEELEAE 700
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622845278 472 LTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
155-259 |
3.64e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 155 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGI-SRSHGEITEERDILSRQqgdhvARILEL 233
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREISRLD-----REIERL 477
|
90 100
....*....|....*....|....*.
gi 1622845278 234 EDDIQTISEKVLTKEVELDRLRDTVK 259
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKELWK 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-513 |
4.02e-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: 42.60 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 375 RTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTEL 454
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELE----DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 455 -----AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 513
Cdd:COG1579 83 gnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-507 |
4.51e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 145 KATVLQ---NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILsr 221
Cdd:PRK01156 330 KLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 222 qqgdhVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLK----EVQADKEQSEAELQVAQQENRRLN 297
Cdd:PRK01156 408 -----KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 298 LDLQ----EAKSWQEEQSAQAQRL----KDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQEL-----AASSQQKATLLG- 363
Cdd:PRK01156 483 EKIReieiEVKDIDEKIVDLKKRKeyleSEEINKSINEYNKIESARADLEDIKIKINELKDKhdkyeEIKNRYKSLKLEd 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 364 -----EELASAATARDRTIAELHRSRLEvaEVNGRL--AELGLH--------LKEEKCQWSKERAGLLQSVEAEKDKILK 428
Cdd:PRK01156 563 ldskrTSWLNALAVISLIDIETNRSRSN--EIKKQLndLESRLQeieigfpdDKSYIDKSIREIENEANNLNNKYNEIQE 640
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 429 LSAEILRLEKAVQEERTQNQVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARL 507
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEIT-SRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
158-513 |
4.57e-04 |
|
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: 43.56 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 158 QERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGIS-RSHGEITEERDILSRQQGD-HVARILEleD 235
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlKLEEEIQENKDLIKENNATrHLCNLLK--E 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 236 DIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnrrlnlDLQEAKSWQEEQSaqaQ 315
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYK---K 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 316 RLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELH--RSRLEVAEVNGR 393
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdiKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 394 LAELGLHLKEEK-CQWSKERAGLLQSVEAEKDK----ILKLSAEILRLEKAVqeeRTQNQvfktELAREKDSSLVQLSES 468
Cdd:pfam05483 314 ALEEDLQIATKTiCQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELL---RTEQQ----RLEKNEDQLKIITMEL 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622845278 469 KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL--EARLEKVADE 513
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdeKKQFEKIAEE 433
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
271-405 |
4.90e-04 |
|
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: 43.59 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 271 QLKEVqadKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQA-QQRVAELEP-LKEQLRGA 348
Cdd:pfam07111 521 QLSEV---AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAlQEKVAEVETrLREQLSDT 597
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 349 QEL---AASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNG-RLAELGLHLKEEK 405
Cdd:pfam07111 598 KRRlneARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGqRLARRVQELERDK 658
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-398 |
5.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 166 LKLQLEGQVTELRSRVQELERALATARQEHAELmeqyKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVl 245
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIG----AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV- 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 246 TKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDkvaqmk 325
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE------ 714
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845278 326 dtlgQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRsrlEVAEVNGRLAELG 398
Cdd:COG1196 715 ----ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALG 780
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
232-513 |
5.97e-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: 43.42 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEK------------------------LLGQLKEVQADKEQSEAELQ 287
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKekleleeeyllyldylklneeridLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 288 VA-----QQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLL 362
Cdd:pfam02463 261 EKeeeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 363 GEELAS--AATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILR-LEKA 439
Cdd:pfam02463 341 EKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqLEDL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845278 440 VQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQ---LQEEKQELLEYMRKLEARLEKVADE 513
Cdd:pfam02463 421 LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKsedLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
152-457 |
6.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNdlmqlklQLEGQVTELRSRVQELERALATARQEHAELMEQYKgisrshgEITEERDILSRQQGDHVARIL 231
Cdd:COG4372 39 ELDKLQEELE-------QLREELEQAREELEQLEEELEQARSELEQLEEELE-------ELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRL-----NLDLQEAKSW 306
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeqelqALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 307 QEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLE 386
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELARE 457
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-514 |
6.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRShgeiteerdiLSRQQgdhvA 228
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ----------LQAAQ----A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNldlQEAKSWQE 308
Cdd:COG4372 95 ELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE---EQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 EVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSES 468
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622845278 469 KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
228-490 |
7.03e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILELEDDIQTISekvltkeVELDRLRDTVKALTREQEKLLGQLKEVQADKE----QSEAELQVAQQENRRLNLDLQEA 303
Cdd:PHA02562 174 DKIRELNQQIQTLD-------MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 304 KSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELE-----PL-KEQLRGAQELAASSQQKATLLGEELASAATARDRti 377
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcPTcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 378 aelhrsrlevaevngrlaelglhLKEEKCQW---SKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTEL 454
Cdd:PHA02562 325 -----------------------LEEIMDEFneqSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEEL 381
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622845278 455 AREKDsslvqlseskrELTELRSALRVLQKEKEQLQ 490
Cdd:PHA02562 382 AKLQD-----------ELDKIVKTKSELVKEKYHRG 406
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
152-386 |
7.64e-04 |
|
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: 42.80 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 152 QLDESQQERNDLMQLKLQLEgqvtelRSRVQELERaLATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARIL 231
Cdd:pfam17380 354 RQEERKRELERIRQEEIAME------ISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKE--VELDRLRDTVKALTREQEKLLGQ---LKEVQADKEQSEAELQVAQQENRR-LNLDLQEAKS 305
Cdd:pfam17380 427 AEQEEARQREVRRLEEEraREMERVRLEEQERQQQVERLRQQeeeRKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 306 WQEEQSAQAQRLKDKVAQMKDTLGQAQQ-RVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARD--RTIAELHR 382
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREmmRQIVESEK 586
|
....
gi 1622845278 383 SRLE 386
Cdd:pfam17380 587 ARAE 590
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
149-515 |
8.43e-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: 42.37 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQE-------RNDLMQLKLQLEGQVTELRSRVQELERALATARQehaelmeqykgisrshgeITEERDILsR 221
Cdd:pfam05622 64 LQKQLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNEELTSLAEEAQA------------------LKDEMDIL-R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 222 QQGDHVARileLEDDIQTISEKVltkeVELDRLRDTVKAL----------TREQEKllgQLKEVQADKEQSEAELQVAQQ 291
Cdd:pfam05622 125 ESSDKVKK---LEATVETYKKKL----EDLGDLRRQVKLLeernaeymqrTLQLEE---ELKKANALRGQLETYKRQVQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 292 ENRRLNLDLQEAKSWQ------EEQSAQAQRLKDKVAQMKDTL---------GQAQQRvaeleplkeQLRGAQELAASSQ 356
Cdd:pfam05622 195 LHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDTLretneelrcAQLQQA---------ELSQADALLSPSS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 357 QKATLLGEELASAATaRDRTIAELHRSRL----EVAEVNGRLAELGLHLkeEKCQWSKERagLLQSVEAEKDKILKLSAE 432
Cdd:pfam05622 266 DPGDNLAAEIMPAEI-REKLIRLQHENKMlrlgQEGSYRERLTELQQLL--EDANRRKNE--LETQNRLANQRILELQQQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 433 ILRLEKAVQEERTQNQVFKTeLAREKDSSLVQLSESKRELTELRSALRVLQ-KEKEQLQEEKQELLEYMRKLEARLeKVA 511
Cdd:pfam05622 341 VEELQKALQEQGSKAEDSSL-LKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKDEDM-KAM 418
|
....
gi 1622845278 512 DEKW 515
Cdd:pfam05622 419 EERY 422
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
216-443 |
9.30e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 216 RDILsrqqgDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEV-QAD-KEQSEAELqvaQQEN 293
Cdd:COG0497 144 RELL-----DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELeAAAlQPGEEEEL---EEER 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 294 RRLN------LDLQEAKSW--QEEQSAQAQrlkdkvaqmkdtLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEE 365
Cdd:COG0497 216 RRLSnaeklrEALQEALEAlsGGEGGALDL------------LGQALRALERLAEYDPSLAELAERLESALIELEEAASE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 366 LASAATArdrtiAELHRSRLEvaEVNGRLAELgLHLK-------EEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEK 438
Cdd:COG0497 284 LRRYLDS-----LEFDPERLE--EVEERLALL-RRLArkygvtvEELLAYAEELRAELAELENSDERLEELEAELAEAEA 355
|
....*
gi 1622845278 439 AVQEE 443
Cdd:COG0497 356 ELLEA 360
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
149-350 |
9.60e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELE----------RALATARQEHA----ELMEQYKGISRSHGEITE 214
Cdd:COG1340 27 LKEKRDELNEELKELAEKRDELNAQVKELREEAQELRekrdelnekvKELKEERDELNeklnELREELDELRKELAELNK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 215 ER---DILSRqqgdhvaRILELEDDIQTiseKVLTKEVElDRLRDTVKALTREQEKLLgQLKEVQADKEQSEAELQVAQQ 291
Cdd:COG1340 107 AGgsiDKLRK-------EIERLEWRQQT---EVLSPEEE-KELVEKIKELEKELEKAK-KALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 292 ENRRLNLDLQEAkswqeeqSAQAQRLKDkvaQMKDTLGQAQQRVAELEPLKEQLRGAQE 350
Cdd:COG1340 175 EAEEIHKKIKEL-------AEEAQELHE---EMIELYKEADELRKEADELHKEIVEAQE 223
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
149-347 |
1.05e-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: 42.63 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEE-----RDILSRQQ 223
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEErarirRDELHEEL 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 224 GDHVARILELEDDIQTIsekvltkEVELDRLrdtVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEN--RRLNldlq 301
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRC-------EAEMDSL---QKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNDveRRLH---- 1134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622845278 302 eaKSWQEEQSAQAQR-LKDKvaqmkdTLGQAQQRVAELEPLKEQLRG 347
Cdd:COG3096 1135 --RRELAYLSADELRsMSDK------ALGALRLAVADNEHLRDALRL 1173
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
250-372 |
1.31e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.15 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLG 329
Cdd:COG5283 22 RVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSSLEQTNRQLE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622845278 330 QAQQRVAELEPLKEQLRGA-QELAASSQQKATLLGeeLASAATA 372
Cdd:COG5283 102 RQQQRLARLGARQDRLKAArARLQRLAGAGAAAAA--IGAALAA 143
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
250-514 |
1.34e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 250 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRL------NLDLQEAKsWQEEQSAQAQRLKDKvaq 323
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRadrrekQVIEKESR-WREQAEDQENQRQEK--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 324 MKDTLGQAQQRVAELEP-LKEQLRGAQELAASSQQkatLLGEELASAATARDRTIAELHR-----SRLEVAEVNGRLAEL 397
Cdd:pfam15558 111 LERARQEAEQRKQCQEQrLKEKEEELQALREQNSL---QLQERLEEACHKRQLKEREEQKkvqenNLSELLNHQARKVLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 398 GLHLKEE----------KCQWSKERAGLLQSVEAE--KDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQL 465
Cdd:pfam15558 188 DCQAKAEellrrlsleqSLQRSQENYEQLVEERHRelREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQA 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845278 466 SESK-----------RELTELRSALRVLQKEKEQLQEE--KQELLEYMRKLEARLEKVADEK 514
Cdd:pfam15558 268 RQVAhktvqdkaqraRELNLEREKNHHILKLKVEKEEKchREGIKEAIKKKEQRSEQISREK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
149-319 |
1.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAEL---MEQYKGIS---RSHGE-------ITEE 215
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskIEQFQKVIkmyEKGGVcptctqqISEG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 216 RDILSR--------QQG-----DHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQS 282
Cdd:PHA02562 298 PDRITKikdklkelQHSlekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622845278 283 EAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKD 319
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
147-327 |
1.53e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 147 TVLQNQLDESQQERNdlmQLKLQLEGQVTELRSRVQELEralaTARQEHAELMEQYKGISRSHGEITEERDILSRQQGDH 226
Cdd:TIGR04523 464 ESLETQLKVLSRSIN---KIKQNLEQKQKELKSKEKELK----KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 227 VARILELEDDIQTIsEKVLTKEV----------ELDRLRDTVKALTREQEKLLGQLKEVQADK--------------EQS 282
Cdd:TIGR04523 537 ESKISDLEDELNKD-DFELKKENlekeideknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKkdlikeieekekkiSSL 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622845278 283 EAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDT 327
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
261-402 |
1.71e-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: 41.25 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 261 LTREQEKLLGQLKEVQADKEQSEAELQVAQQenrrLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEP 340
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845278 341 L-------------KEQLRGAQE--LAASSQQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELGLHLK 402
Cdd:pfam00529 132 LapiggisreslvtAGALVAQAQanLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
171-339 |
1.74e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 171 EGQV------TELRSRVQELERALATARQEHAELmeqykgisrshgeiteerdilsRQQGDHVARILELEDDIQTISEKV 244
Cdd:COG1566 69 KGQVlarldpTDLQAALAQAEAQLAAAEAQLARL----------------------EAELGAEAEIAAAEAQLAAAQAQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 245 LTKEVELDRLRDTVK--ALTREQekllgqLKEVQADKEQSEAELQVAQQenrrlNLDLQEAKSWQEEQSAQAQRlkdKVA 322
Cdd:COG1566 127 DLAQRELERYQALYKkgAVSQQE------LDEARAALDAAQAQLEAAQA-----QLAQAQAGLREEEELAAAQA---QVA 192
|
170
....*....|....*..
gi 1622845278 323 QMKDTLGQAQQRVAELE 339
Cdd:COG1566 193 QAEAALAQAELNLARTT 209
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
153-398 |
2.34e-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: 41.48 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 153 LDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATAR--QEHAELMEQYKGISRSHgEITEERDILS------RQQG 224
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETLADRLE-ELREELDAAQeaqafiQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 225 DHVARILELEDDIQT-------ISEKVLTKEVELDRLRDTVKALT-----REQ-----------------EKLLGQLKEV 275
Cdd:COG3096 917 KALAQLEPLVAVLQSdpeqfeqLQADYLQAKEQQRRLKQQIFALSevvqrRPHfsyedavgllgensdlnEKLRARLEQA 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 276 QADKEQSEAELQVAQQENRRLNLDLQEAKSwqeeqSAQAQRlkdkvaqmkDTLGQAQQRVAELEplkeqLRGAQELAASS 355
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKS-----SRDAKQ---------QTLQELEQELEELG-----VQADAEAEERA 1057
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622845278 356 QQKATLLGEELASAATARDRTIAELHRSRLEVAEVNGRLAELG 398
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-339 |
2.52e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 126 ELVTLEEADGGSDILLVVPKATVLQNQL-DESQQERNDLMQLKLQLEGQVTELRSRVQELERA-------LATARQEHAE 197
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtnklkmqLKSAQSELEQ 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 198 LMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDtvkaltrEQEKLLGQLKEVQA 277
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE-------EKNKLSQELSTVAT 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845278 278 DKEQSEAELQVAQQENRrlnldlqeakswqeeqsaqaqRLKDKVAQMKDTLGQAQQRVAELE 339
Cdd:pfam15921 784 EKNKMAGELEVLRSQER---------------------RLKEKVANMEVALDKASLQFAECQ 824
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
162-309 |
2.58e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 162 DLMQLKLQLEGQVTELRSR--------------VQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQqgdhV 227
Cdd:smart00787 113 LLMDKQFQLVKTFARLEAKkmwyewrmklleglKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEE----L 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILELEDDIQTIsekvltKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQ 307
Cdd:smart00787 189 RQLKQLEDELEDC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
..
gi 1622845278 308 EE 309
Cdd:smart00787 263 EQ 264
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
154-498 |
2.59e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 154 DESQQER----NDLMQLKLQLEGQVTELRsRVQELERALATARQEH-AELMEQYKGISRSHGEITEERDILSRQQGDHVA 228
Cdd:COG5278 102 NPEQQARldelEALIDQWLAELEQVIALR-RAGGLEAALALVRSGEgKALMDEIRARLLLLALALAALLLAAAALLLLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 229 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSWQE 308
Cdd:COG5278 181 ALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLEVA 388
Cdd:COG5278 261 ALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 EVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSES 468
Cdd:COG5278 341 AAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAE 420
|
330 340 350
....*....|....*....|....*....|
gi 1622845278 469 KRELTELRSALRVLQKEKEQLQEEKQELLE 498
Cdd:COG5278 421 ALELAEALAEALALAEEEALALAAASSELA 450
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
263-379 |
2.60e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 39.14 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 263 REQEKLLGQLKEVQADkeqSEAELQVAQQENRRLNLDLQE-AKSWQEEQSAQAQRLKDKVAQmkDTLGQA-QQRVAELEP 340
Cdd:PRK14473 49 RDAEKVREQLANAKRD---YEAELAKARQEAAKIVAQAQErARAQEAEIIAQARREAEKIKE--EARAQAeQERQRMLSE 123
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622845278 341 LKEQLRGAQELAASSqqkatLLGEELasAATARDRTIAE 379
Cdd:PRK14473 124 LKSQIADLVTLTASR-----VLGAEL--QARGHDALIAE 155
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
165-345 |
2.68e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 165 QLKLQLEGQVTELR---SRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTIS 241
Cdd:pfam06008 23 NLTKQLQEYLSPENahkIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 242 EKVLTKEVELDRLrdTVKALTREQE---KLLGQLKEVQADKEQSEAELQVA----------------QQENRRL------ 296
Cdd:pfam06008 103 EKVATLGENDFAL--PSSDLSRMLAeaqRMLGEIRSRDFGTQLQNAEAELKaaqdllsriqtwfqspQEENKALanalrd 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 297 -----NLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQL 345
Cdd:pfam06008 181 slaeyEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQL 234
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
130-503 |
2.75e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 41.11 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 130 LEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSH 209
Cdd:COG4995 98 LAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 210 GEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVA 289
Cdd:COG4995 178 ALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAAL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 290 QQenRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASA 369
Cdd:COG4995 258 LA--LAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLAL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 370 ATARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQV 449
Cdd:COG4995 336 LLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAA 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1622845278 450 FKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKL 503
Cdd:COG4995 416 LALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRL 469
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
151-345 |
3.05e-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: 40.18 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 151 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGdhvari 230
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 231 lelEDDIQtisEKVLTKEVELDRLRDTVKALTRE----QEKLLGQLKEVQADKEQSEAELQVAQQENRRLNLDLQEAKSW 306
Cdd:pfam15905 147 ---EDGTQ---KKMSSLSMELMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622845278 307 QEEQ----------SAQAQRLKDKVAQMKDTLGQAQQrvaELEPLKEQL 345
Cdd:pfam15905 221 TEKLleyitelscvSEQVEKYKLDIAQLEELLKEKND---EIESLKQSL 266
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
247-414 |
3.19e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 247 KEVELDRLRDTVKA-----------LTREQEKLLG-QLKEVQADKEQSEAELQVAQQENRRLNldlqeakswqeeqsAQA 314
Cdd:COG2433 357 KKVPPDVDRDEVKArvirglsieeaLEELIEKELPeEEPEAEREKEHEERELTEEEEEIRRLE--------------EQV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 315 QRLKDKVAQMKDTLGQAQQRVAELEplkEQLRgaqeLAASSQQKATLLGEELasaaTARDRTIAELHRsrlEVAEVNGRL 394
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLE---RELS----EARSEERREIRKDREI----SRLDREIERLER---ELEEERERI 488
|
170 180
....*....|....*....|
gi 1622845278 395 AELGLHLKEEKCQWSKERAG 414
Cdd:COG2433 489 EELKRKLERLKELWKLEHSG 508
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
185-496 |
3.37e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 185 ERALATARQEHAELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDdiqtisekvltkEVELDRLRDTVKALTRE 264
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADP------------EAELRQLNRRRVELERA 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 265 QEKLLGQLKEVQADKEQSEAELQVAQQENRRLNL----DLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAEL-- 338
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLladeTLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLqs 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 339 EPLK-EQLRGAQELAASSQQkatllgeelasaaTARDRTIAelhrsrleVAEVNGRLAELGLHlkeekcqwskERAGLLq 417
Cdd:PRK04863 933 DPEQfEQLKQDYQQAQQTQR-------------DAKQQAFA--------LTEVVQRRAHFSYE----------DAAEML- 980
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845278 418 svEAEKDKILKLSAeilRLEKAVQEERTQnqvfkTELAREKDSslvQLSESKRELTELRSALRVLQkekEQLQEEKQEL 496
Cdd:PRK04863 981 --AKNSDLNEKLRQ---RLEQAEQERTRA-----REQLRQAQA---QLAQYNQVLASLKSSYDAKR---QMLQELKQEL 1043
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
252-372 |
3.39e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.62 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 252 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQEnrrlnldLQEAKSwqEEQSAQAQRLKDKVAQmkdtlgQA 331
Cdd:PRK12472 207 DEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKA-------LAAAKT--DEAKARAEERQQKAAQ------QA 271
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622845278 332 QQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATA 372
Cdd:PRK12472 272 AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKA 312
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
401-505 |
4.05e-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: 39.12 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 401 LKEEKCQwskeraglLQSVEAEKDKILK-LSAEILRLEKAVQEERTQNQVFKTELAR-EKDsslvqlsesKRELTELRSA 478
Cdd:pfam13851 31 LKEEIAE--------LKKKEERNEKLMSeIQQENKRLTEPLQKAQEEVEELRKQLENyEKD---------KQSLKNLKAR 93
|
90 100
....*....|....*....|....*..
gi 1622845278 479 LRVLQKEKEQLQEEKQELLEYMRKLEA 505
Cdd:pfam13851 94 LKVLEKELKDLKWEHEVLEQRFEKVER 120
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
460-514 |
4.21e-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: 4.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622845278 460 SSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4026 125 QNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEN 179
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
232-456 |
4.64e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.43 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 232 ELEDDIQTISEKVLTKEVEL--DRLRDTVKALTREQEKLLGQLKEV-QADKEQSEAELQVAQQENRRLNLDlQEAKSWQE 308
Cdd:pfam13166 264 PLPAERKAALEAHFDDEFTEfqNRLQKLIEKVESAISSLLAQLPAVsDLASLLSAFELDVEDIESEAEVLN-SQLDGLRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAqaqRLKD--KVAQMKDTLgqaqqrvAELEPLKEQLRGAQELAASSQQKATLLGEELASAATArdrtiAELHrsrlE 386
Cdd:pfam13166 343 ALEA---KRKDpfKSIELDSVD-------AKIESINDLVASINELIAKHNEITDNFEEEKNKAKKK-----LRLH----L 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 387 VAEVNGRLAELglhlKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAR 456
Cdd:pfam13166 404 VEEFKSEIDEY----KDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-496 |
4.74e-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: 40.34 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 149 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERAL-ATARQEHAELMEQYKGISRSHGEITEERDILSRQQgdhV 227
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTeKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ---C 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 228 ARILELEDDIQTISEKVLTKEVELDRLRdtvkaLTREQEKLLGQLKEVQADKEQSEAE-LQVAQQENRRLNLDLQEAKSW 306
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETH 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 307 QEEQSAQAQRLKDKVAQMKDTLGQaqqrvaELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELHRSRLE 386
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAA------REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 387 VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKlsaeilrlekavQEERTQNQVfktelaREKDSSLVQLS 466
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ------------EEEQFLSRL------EEKSATLGEIT 848
|
330 340 350
....*....|....*....|....*....|
gi 1622845278 467 ESKRELTELRSALRVLQKEKEQLQEEKQEL 496
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
125-396 |
5.68e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 40.00 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 125 DELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKG 204
Cdd:COG0840 108 ALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 205 ISRSHGEITEERDILSRQQgdhVARILELEDDIQTISEKVLTKEVELDRlRDTVKALTREQEKLLGQLKEVQADKEQSEA 284
Cdd:COG0840 188 LLALVALAIILALLLSRSI---TRPLRELLEVLERIAEGDLTVRIDVDS-KDEIGQLADAFNRMIENLRELVGQVRESAE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 285 ELQVAQQENRRLNLDLQEAkswQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAEleplkeqlrgAQELAASSQQKATLLGE 364
Cdd:COG0840 264 QVASASEELAASAEELAAG---AEEQAASLEETAAAMEELSATVQEVAENAQQ----------AAELAEEASELAEEGGE 330
|
250 260 270
....*....|....*....|....*....|..
gi 1622845278 365 ELASAATArdrtIAELHRSRLEVAEVNGRLAE 396
Cdd:COG0840 331 VVEEAVEG----IEEIRESVEETAETIEELGE 358
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
373-504 |
5.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 373 RDRTIAELHrsrlevaevngrlaELGL-HLKEEKCQWSKERAGLLQSveaekdKILKLSAEILRLEKAVQEERTqnqVFK 451
Cdd:PRK05771 18 KDEVLEALH--------------ELGVvHIEDLKEELSNERLRKLRS------LLTKLSEALDKLRSYLPKLNP---LRE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622845278 452 TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLE 504
Cdd:PRK05771 75 EKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE 127
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
420-510 |
5.83e-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: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 420 EAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAREKDSSLVQLSESKRELTELRSALR----VLQKEKEQLQEEKQE 495
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLE----DLERELALLQAKERQLEKKLKTLEQKLKnekeELQRLKNALQQIKTQ 130
|
90
....*....|....*
gi 1622845278 496 LLEYMRKLEARLEKV 510
Cdd:pfam11559 131 FAHEVKKRDREIEKL 145
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
283-499 |
7.01e-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: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 283 EAELQVAQQENRRLNLDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQA--------QQRVAELEPLKEQLRGAQELAAS 354
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 355 SQQKATLL-------------GEELASAATARDRTIAELHRSRLEVAEVNGRLAELGlhlkeekcqWSKERAGLLQSVEA 421
Cdd:COG3096 915 HGKALAQLeplvavlqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFS---------YEDAVGLLGENSDL 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845278 422 EKdkilKLSAeilRLEKAvQEERTQnqvfKTELAREKDSslvQLSESKRELTELRSALRVLQkekEQLQEEKQELLEY 499
Cdd:COG3096 986 NE----KLRA---RLEQA-EEARRE----AREQLRQAQA---QYSQYNQVLASLKSSRDAKQ---QTLQELEQELEEL 1045
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
211-513 |
7.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 211 EITEERDILSR-QQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQ----LKEVQADKEQSEAE 285
Cdd:PTZ00121 1040 DVLKEKDIIDEdIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEeakkTETGKAEEARKAEE 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 286 LQVAQQENRRLN--LDLQEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELaassqQKAtllg 363
Cdd:PTZ00121 1120 AKKKAEDARKAEeaRKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV-----RKA---- 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 364 EELASAATARDrtiAELHRSRLEVaevngRLAELGLHLKEEKcqwskeRAGLLQSVEAEKDKilklSAEILRLEkavqEE 443
Cdd:PTZ00121 1191 EELRKAEDARK---AEAARKAEEE-----RKAEEARKAEDAK------KAEAVKKAEEAKKD----AEEAKKAE----EE 1248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845278 444 RTQNQVFKTELAREKDSSLVQL---SESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARleKVADE 513
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAaikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADE 1319
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-257 |
7.54e-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: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 130 LEEADGGSDILlvvpkaTVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHAELMEQYKGISRSH 209
Cdd:COG4913 677 LERLDASSDDL------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622845278 210 GEITEERDILSRQQGDHVARileLEDDIQTISEKVLTKEVELDRLRDT 257
Cdd:COG4913 751 LEERFAAALGDAVERELREN---LEERIDALRARLNRAEEELERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
309-514 |
7.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 309 EQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRTIAELhRSRLEVA 388
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 389 EVNGRLAELGLHLKEekcqwSKERAGLLQSVEAeKDKILKLSAEILRLEKAVQEErtqnqvfkteLAREKDsslvQLSES 468
Cdd:COG3883 96 YRSGGSVSYLDVLLG-----SESFSDFLDRLSA-LSKIADADADLLEELKADKAE----------LEAKKA----ELEAK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622845278 469 KRELTELRSALRVLQKEKEQLQEEKQELLEymrKLEARLEKVADEK 514
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLA---QLSAEEAAAEAQL 198
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
330-498 |
8.00e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.99 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 330 QAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAATARDRtiAELHRSRLEVAEVNGRLAELGLHLKEEkcqwS 409
Cdd:pfam08614 11 RLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLE--QLLAQLREELAELYRSRGELAQRLVDL----N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 410 KERAGLLQSVEAEKDKILKLSAEILRLEKAVQEertqnqvfKTELAREKDSSLVQLsesKRELTELRSALRVLQKEKEQL 489
Cdd:pfam08614 85 EELQELEKKLREDERRLAALEAERAQLEEKLKD--------REEELREKRKLNQDL---QDELVALQLQLNMAEEKLRKL 153
|
....*....
gi 1622845278 490 QEEKQELLE 498
Cdd:pfam08614 154 EKENRELVE 162
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
373-511 |
8.18e-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: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845278 373 RDRTIAELHRSrLEVAEVNGRLAELGLHLKEEKCQWSKERAGllQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKT 452
Cdd:COG2433 365 RDEVKARVIRG-LSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845278 453 ELAR-EKDSSLVQLSESK-----RELTELRSALRVLQKEKEQLQEEKQEL------LEYMRKLEARLEKVA 511
Cdd:COG2433 442 RIERlERELSEARSEERReirkdREISRLDREIERLERELEEERERIEELkrklerLKELWKLEHSGELVP 512
|
|
| |
