|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-584 |
2.72e-175 |
|
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: 509.05 E-value: 2.72e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 122 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEDQVTELRS 179
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 180 RVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVK 259
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 260 altreqeKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:pfam07888 161 -------KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 340 PLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSM 419
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 420 EAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEY 499
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 500 MRKLEARLEKVADEKWTEDAATEDEEATAGLScpasltDSEDESPEDMRLPS----YGLCESGNT-----SSSPPGPREP 570
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERPDSPLS------DSEDENPEALQPPRplghYSLCEQGQPdslllATPPPSPRDP 467
|
490
....*....|....
gi 160017771 571 SSLVVINQPAPIAP 584
Cdd:pfam07888 468 ESTVVISQPAPLSS 481
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-118 |
1.31e-39 |
|
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: 140.84 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 15 VNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWssVPESTTDGSPTHASVQFQASYLPKPG 94
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 160017771 95 AQLYQFRYVNRQGRVCGQSPPFQF 118
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-526 |
4.34e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 170 LEDQVTELRSRVQELEaalataRQehSELTEQYKglsrshgELSEERDILsqqqgDHVARILELEDdiqtmsdkvlmKEV 249
Cdd:COG1196 191 LEDILGELERQLEPLE------RQ--AEKAERYR-------ELKEELKEL-----EAELLLLKLRE-----------LEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 250 ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclnteLEEAKSRQEEQGAQVQRLKDKLAHMKDTLG 329
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 330 QAQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAElslhmkeekcqWS 409
Cdd:COG1196 313 ELEERLEELE---EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-----------AE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 410 KERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQshvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQL 489
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
330 340 350
....*....|....*....|....*....|....*..
gi 160017771 490 QTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEA 526
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-437 |
1.40e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQErndLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:COG1196 214 RYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 224 GDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclnteLEEA 303
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-------LAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 160017771 384 RLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLE 437
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-504 |
6.06e-16 |
|
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: 82.04 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 167 KLQLEDQVTELRSRVQELEAALATARQEHS-------ELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQT 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 240 MSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADK-----EQSEAELQTVREENCCLNTELEEAKSRQEEQGAQV 314
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 315 QRLKDKLAHMKDTLGQAQQKV----AELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEV 390
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 391 NGRLAELSLHMKEEKCQWSkERTGLLQSMEAEKDKILKLSAEILRLEKtVQEERTqshvfKTELAREKDSSLVQLSESKR 470
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQ-----RVEEEIRALEPVNMLAIQEY 981
|
330 340 350
....*....|....*....|....*....|....
gi 160017771 471 ELTELRsaLRVLQKEKEQLQTEKQELLEYMRKLE 504
Cdd:TIGR02169 982 EEVLKR--LDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-506 |
8.50e-16 |
|
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: 81.64 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATAR-------QEHSELTEQYKGLSRSHGELSEERDILSQQ 222
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 223 QGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEE 302
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHR 382
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 383 SRLEVAEVNGRLAELSLHmkeekcqwskertglLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSL 462
Cdd:TIGR02168 913 LRRELEELREKLAQLELR---------------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 160017771 463 ---------VQLsESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEAR 506
Cdd:TIGR02168 978 enkikelgpVNL-AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-434 |
3.21e-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: 79.72 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSelteqykglsrshgELSEERDILSQQQG 224
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS--------------ELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILELEDDIQtmsdkvlMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTV-------REENCCLN 297
Cdd:TIGR02168 292 ALANEISRLEQQKQ-------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeeleslEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 298 TELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQL-----RGVQELAASSQQKAALLGEELASAAGA 372
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrreRLQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 373 RDRTIAEL------HRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEIL 434
Cdd:TIGR02168 445 LEEELEELqeelerLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-528 |
1.33e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTmsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:COG1196 394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQ----LRGVQELAASSQQK------AALLGEELASAAGARDRTIA 378
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegfLEGVKAALLLAGLRglagavAVLIGVEAAYEAALEAALAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 379 ELHRSRLEVAEVNGRLAEL--------------------SLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEIL---- 434
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYlkaakagratflpldkirarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrt 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 435 --------------RLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYM 500
Cdd:COG1196 627 lvaarleaalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420
....*....|....*....|....*...
gi 160017771 501 RKLEARLEKVADEKWTEDAATEDEEATA 528
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-525 |
2.13e-14 |
|
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: 77.03 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAagardRTIAELHRSRLeva 388
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAK-----EAIELLKRRKA--- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 389 evnGRLAELSLH-MKEEKCQWSKER----------------------------TGLLQSMEAEKD-----KILKLSAEIL 434
Cdd:TIGR02169 573 ---GRATFLPLNkMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdTLVVEDIEAARRlmgkyRMVTLEGELF 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 435 ----------------RLEKTVQEERTQSHVFKTE-LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELL 497
Cdd:TIGR02169 650 eksgamtggsraprggILFSRSEPAELQRLRERLEgLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
410 420
....*....|....*....|....*....
gi 160017771 498 EYMRKLEARLEKVADE-KWTEDAATEDEE 525
Cdd:TIGR02169 730 QEEEKLKERLEELEEDlSSLEQEIENVKS 758
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-391 |
4.00e-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: 76.25 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTMSDKVLMKEVELDRvrdtvkaLTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEE-------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAElepLKEQLRGVQELAAssQQKAALLGEELASAAGARDRtIAELHRSRLEVA 388
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDN---LQERLSEEYSLTL--EEAEALENKIEDDEEEARRR-LKRLENKIKELG 985
|
...
gi 160017771 389 EVN 391
Cdd:TIGR02168 986 PVN 988
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-509 |
1.60e-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: 74.32 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQlkEFQADKEQSEAELQTVREENcclntELEEAKSRQ 307
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE--LEELSRQISALRKDLARLEA-----EVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLrgvQELAASSQQKAALLGEELASAAgardrtiAELHRSRLEV 387
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELR-------AELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 AEVNGRLAELslhmKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQShvfkTELAREKDSSLVQLSE 467
Cdd:TIGR02168 820 ANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALAL 891
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 160017771 468 SKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEK 509
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-526 |
1.65e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALAT---ARQEHSELTEQYKGLSRSHGELSEERDILSQQQGD 225
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 226 HVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKS 305
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 306 RQEEqgaqvqrLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASaagARDRTIAELHRSRL 385
Cdd:PRK02224 364 EAAE-------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 386 EVAEVNGRLAELSLHMKEEK---CQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTvQEERTQSHvfktelarEKDSSL 462
Cdd:PRK02224 434 TLRTARERVEEAEALLEAGKcpeCGQPVEGSPHVETIEEDRERVEELEAELEDLEEE-VEEVEERL--------ERAEDL 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160017771 463 VQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKwtEDAATEDEEA 526
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK--REAAAEAEEE 566
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-375 |
2.53e-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: 72.10 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILELEDDIQTMSDKVLMKEV-------ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLN 297
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 298 TELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLrgvQELAASSQQKAALLGEELASAAGARDR 375
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-527 |
3.42e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 181 VQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQgDHVARILELEDDIQTMSDKVLMKEVEldrvrdtvkA 260
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEGYELLKEKE---------A 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 261 LTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRlkdklahmkdtlgQAQQKVAELEP 340
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-------------RVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 341 LKEQLRGVQELAASSQQKAAllgEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEekcqwSKERTGLLQSME 420
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE-----LKEELEDLRAEL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 421 AEKDKIL-----KLSAEILRLEKTVQEertqshvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQE 495
Cdd:TIGR02169 374 EEVDKEFaetrdELKDYREKLEKLKRE--------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350
....*....|....*....|....*....|..
gi 160017771 496 LLEYMRKLEARLEKVADEKWTEDAATEDEEAT 527
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
654-682 |
5.74e-13 |
|
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: 63.29 E-value: 5.74e-13
10 20
....*....|....*....|....*....
gi 160017771 654 KECPICKERFPAESDKDALEGHMDGHFFF 682
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHFFF 29
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-459 |
8.57e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 160 RNDLMQLKLQLE-DQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQ 238
Cdd:TIGR02168 219 KAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 239 TMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTvreenccLNTELEEAKSRQEEQGAQVQRLK 318
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 319 DKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELaassqqkaalLGEELASAAGARDRTIAEL-----HRSRLEVAEVNGR 393
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLERLEDRRERLQQEIeellkKLEEAELKELQAE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 394 LAELslhmKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKD 459
Cdd:TIGR02168 442 LEEL----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-528 |
2.22e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLK---LQLEDQVTELRSRVQELEAALATARQEHSELtEQYKGLSRSHGELSEERDILSQ 221
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 222 QQG------DHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQ-EKLLRQLKEFQADKEQSEAELQTVREENC 294
Cdd:COG4717 144 LPErleeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 295 CLNTELEEAKSRQEEQgAQVQRLKDK------------LAHMKDTLGQAQQKVAEL-------------------EPLKE 343
Cdd:COG4717 224 ELEEELEQLENELEAA-ALEERLKEArlllliaaallaLLGLGGSLLSLILTIAGVlflvlgllallflllarekASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 344 QLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWS-KERTGLLQSMEAE 422
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELeQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 423 KDKILklsAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKREltELRSALRVLQKEKEQLQTEKQELLEYMRK 502
Cdd:COG4717 383 DEEEL---RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAE 457
|
410 420
....*....|....*....|....*.
gi 160017771 503 LEARLEKVADEKWTEDAATEDEEATA 528
Cdd:COG4717 458 LEAELEQLEEDGELAELLQELEELKA 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-440 |
4.34e-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: 69.71 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 155 ESQQERNDLMQLKLQLED-QVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILEL 233
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 234 EDDIqtmsdkvlmkevelDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQ 313
Cdd:TIGR02169 846 KEQI--------------KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 314 VQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASS---QQKAALLGEELASAAGARDRTIAELhrsrlevAEV 390
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEEEIRALEPVNMLAIQEY-------EEV 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 160017771 391 NGRLAELslhmkEEKcqwskertglLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:TIGR02169 985 LKRLDEL-----KEK----------RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-513 |
1.01e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAAlatarqeHSELTEQYKGLSRSHGELSEERDILSQQQgdhvARIL 231
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEEL-------KEEIEELEKELESLEGSKRKLEEKIRELE----ERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 232 ELEDDIQTMSDKVlmKEV-ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEncclNTELEEAKSRQEEQ 310
Cdd:PRK03918 270 ELKKEIEELEEKV--KELkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 311 GAQVQRLKDKLAHMKD---TLGQAQQKVAELEPLKEQLRG--VQELAassqqkaallgEELASAAGARDRTIAELHRSRL 385
Cdd:PRK03918 344 KKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGltPEKLE-----------KELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 386 EVAEVNGRLAELSLHMKEEKCQWSK-----------ERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTqshvfKTEL 454
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEK 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 455 AREKDSSLVQLSESKRELTELRSALRVLQKEK-EQLQTEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-521 |
1.04e-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: 67.10 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 276 QADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEplkEQLRGVQELAASS 355
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 356 QQKAALLGEELASaagardrtiaelhrsRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQS-MEAEKDKILKLSA--- 431
Cdd:COG4942 96 RAELEAQKEELAE---------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRAdla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 432 EILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVA 511
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|
gi 160017771 512 DEKWTEDAAT 521
Cdd:COG4942 241 ERTPAAGFAA 250
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-513 |
1.11e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELteqykglsRSHGELSE-ERDILSQQQGDHVA 228
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------LAEAGLDDaDAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQ--KAALLGEELASAAGArdRTIAElhrSRLE 386
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagKCPECGQPVEGSPHV--ETIEE---DRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 387 VAEVNGRLAELslhmkeekcqwskertgllqsmeaeKDKILKLSAEILRLEKTVQEERtqshvfKTELAREKDSSLVQLS 466
Cdd:PRK02224 477 VEELEAELEDL-------------------------EEEVEEVEERLERAEDLVEAED------RIERLEERREDLEELI 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 160017771 467 ESKRE-LTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK02224 526 AERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-518 |
1.27e-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: 68.22 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQ-----LEDQVTELRSRVQELEAALATARQEHSELTEQYKGL---SRSHG-----ELSEE 215
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqARNQNsmymrQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 216 RDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCC 295
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 296 L-------NTELEEAKSRQEEQGAQVQRLKDKLAHMK-DTLGQAQQKV-----------------AELEPLKEQLRG-VQ 349
Cdd:pfam15921 403 LwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMaaiqgkneslekvssltAQLESTKEMLRKvVE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 350 ELAA------SSQQKAALLGEELASAAGARDRTIAELHRSRlevAEVNGRLAELS-LHMKEEKCQWSKERTGLLQSMEAE 422
Cdd:pfam15921 483 ELTAkkmtleSSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 423 KDKILK-LSAEILRLEKTV-QEERTQS--HVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLE 498
Cdd:pfam15921 560 KDKVIEiLRQQIENMTQLVgQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
410 420
....*....|....*....|
gi 160017771 499 YMRKleaRLEKVADEKWTED 518
Cdd:pfam15921 640 AGSE---RLRAVKDIKQERD 656
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
159-495 |
1.37e-10 |
|
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: 64.74 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 159 ERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEE-RDILSQQQGDHVARI-LELEDD 236
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvEDLKTELEKEKLKNIeLTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 237 IQTMSDKVLMKE-----VELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREE--------NCCLNTELEEA 303
Cdd:pfam05483 496 KLLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEfiqkgdevKCKLDKSEENA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELA-ASSQQ------KAALLGEELASAAGA---- 372
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGsAENKQlnayeiKVNKLELELASAKQKfeei 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 373 --------RDRTIAElhRSRLEVAEVNGRLAELSLHMKEE---KCQWS-KERTGLLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:pfam05483 656 idnyqkeiEDKKISE--EKLLEEVEKAKAIADEAVKLQKEidkRCQHKiAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160017771 441 QEERTQSHVfktelarekdSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQE 495
Cdd:pfam05483 734 EQEQSSAKA----------ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-529 |
1.97e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 124 MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYK 203
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 204 G--LSRSHGELSeerDILSQqqgdhVARILELEDDIQ---TMSDKVLMKEVELDRVRDTVKALTREQEKLlrqlKEFQAD 278
Cdd:PRK03918 451 KelLEEYTAELK---RIEKE-----LKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEKL----KKYNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 279 K-EQSEAELQTVREENCCLNTELEEAKSRQEEqgaqVQRLKDKLAHMKDTLGQAQQKVAEL---------EPLKEQLRGV 348
Cdd:PRK03918 519 ElEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkeleelgfESVEELEERL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 349 QELAASSQQKAALLG--EELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERtgllqsMEAEKDKI 426
Cdd:PRK03918 595 KELEPFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEY 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 427 LKLSAEILRLEKTVQEERtqshvfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLqtekQELLEYMRKLEAR 506
Cdd:PRK03918 669 LELSRELAGLRAELEELE--------KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV----EELREKVKKYKAL 736
|
410 420
....*....|....*....|...
gi 160017771 507 LEKVADEKWTEDAATEDEEATAG 529
Cdd:PRK03918 737 LKERALSKVGEIASEIFEELTEG 759
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-372 |
3.44e-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: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRShgelseerdilSQQQG 224
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-----------LYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILEL--EDDIQTMsdkvlmkeveLDRVrDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEE 302
Cdd:COG3883 100 GSVSYLDVLlgSESFSDF----------LDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
149-372 |
6.45e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDL-------MQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRShgelseerdilSQ 221
Cdd:COG3883 28 LQAELEAAQAELDALqaeleelNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-----------LY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 222 QQGDHVARILEL--EDDIQTMSDKVLMkeveLDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTE 299
Cdd:COG3883 97 RSGGSVSYLDVLlgSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE---LEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160017771 300 LEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-528 |
2.55e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 251 LDRVRDtvkaLTREQEKLLRQLKEfQADKEQSEAELQtvreencclnteleeaksrQEEQGAQVQRLKDKLAHMKDTLGQ 330
Cdd:COG1196 188 LERLED----ILGELERQLEPLER-QAEKAERYRELK-------------------EELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 331 AQQKV------------------AELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNG 392
Cdd:COG1196 244 LEAELeeleaeleeleaelaeleAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 393 RLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHvfktELAREKDSSLVQLSESKREL 472
Cdd:COG1196 324 ELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEELLEALRAA 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 473 TELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEATA 528
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-513 |
2.75e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqg 224
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 dhvaRILELEDDIQTMSDKVlmkeVELDRVRDTVKALTREQE----KLLRQLKEFQADKEQSEAELQTVREENCCLNTEL 300
Cdd:PRK02224 427 ----REAELEATLRTARERV----EEAEALLEAGKCPECGQPvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 301 EEAK------SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARD 374
Cdd:PRK02224 499 ERAEdlveaeDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 375 RTIAELHRSRLEVAEVNGRLAELSlhMKEEKCQWSKERTGLLQSMEAE-KDKILKLSAEILRLEKTVQEERtqshvfkTE 453
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIA--DAEDEIERLREKREALAELNDErRERLAEKRERKRELEAEFDEAR-------IE 649
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 454 LAREK----DSSLVQLSESKRELTELRSAlrvLQKEKEQLQTEKQELLEYMRKLEA------RLEKVADE 513
Cdd:PRK02224 650 EAREDkeraEEYLEQVEEKLDELREERDD---LQAEIGAVENELEELEELRERREAlenrveALEALYDE 716
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-361 |
3.02e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.42 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 147 TVLQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHS--ELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 224 GDHVARILELEDDIQTMSDKV--LMKEVELDRVRDTVKALTREQEKLLRQL-----------KEFQADKEQSEAELQTVR 290
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160017771 291 EEnccLNTELEEAKSRQEEQGAQVQRLKDKLAhmkdTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAAL 361
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-514 |
4.14e-09 |
|
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: 59.65 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQEL--EAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqgdhv 227
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 arileLEDDIQtmsdkvlmkeveldRVRDTVKALTREQEKLLRQLKEfqadKEQseaELQTVREENCCLNTELEEAKSrq 307
Cdd:TIGR04523 340 -----LNEQIS--------------QLKKELTNSESENSEKQRELEE----KQN---EIEKLKKENQSYKQEIKNLES-- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 eeqgaQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRlev 387
Cdd:TIGR04523 392 -----QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR--- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 AEVNGRLAELSLHMKEEKCQWSKertgLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKT---ELAREKDSSLVQ 464
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQ----KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEkieKLESEKKEKESK 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 160017771 465 LSESKRELTELRSAL---------RVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:TIGR04523 540 ISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-546 |
4.37e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 158 QERNDLMQLKLQLEDQV-TELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQgdhvARILELEDD 236
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 237 IQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQR 316
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 317 LKDklahmkdtlgqaqqkvaELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:PRK02224 340 HNE-----------------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 397 LSLHMKEEkcqwSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKT-ELARE-KDSSLVQLSESKRE-LT 473
Cdd:PRK02224 403 APVDLGNA----EDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpECGQPvEGSPHVETIEEDRErVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 474 ELRSALRVLQKEKEQLQtEKQELLEYMRKLEARLEKVADEKWT--------EDAATEDEEATAGLSCPASLTDSEDESPE 545
Cdd:PRK02224 479 ELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKR 557
|
.
gi 160017771 546 D 546
Cdd:PRK02224 558 E 558
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
654-680 |
4.60e-09 |
|
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: 51.88 E-value: 4.60e-09
10 20
....*....|....*....|....*..
gi 160017771 654 KECPICKERFPAESDKDALEGHMDGHF 680
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-492 |
4.79e-09 |
|
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: 59.65 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNdlmqlklQLEDQVTELRSRVQELEAalatarqEHSELTEQYKglsrshGELSEERDILSQQQG 224
Cdd:TIGR04523 322 KLEEIQNQISQNNKIIS-------QLNEQISQLKKELTNSES-------ENSEKQRELE------EKQNEIEKLKKENQS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 dHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAK 304
Cdd:TIGR04523 382 -YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQ----KVAELEPLKEQLRGV-QELAASSQQKAALLG--EELASAAGARDRTI 377
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKelksKEKELKKLNEEKKELeEKVKDLTKKISSLKEkiEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 378 AELHRSRLEVAEVNGR--LAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEertqshvfKTELA 455
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE--------KEKKI 612
|
330 340 350
....*....|....*....|....*....|....*..
gi 160017771 456 REKDSslvQLSESKRELTELRSALRVLQKEKEQLQTE 492
Cdd:TIGR04523 613 SSLEK---ELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
228-548 |
5.99e-09 |
|
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: 59.47 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQtvreencclNTELEEAKSRQ 307
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ---------SEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGAQVQRLKDkLAHMKDTLGQAQQkvAELEPLKEQLRgvqELAASSQQKAALLGEELASAAGARDRTIAelhrsrlev 387
Cdd:pfam12128 675 ERKDSANERLNS-LEAQLKQLDKKHQ--AWLEEQKEQKR---EARTEKQAYWQVVEGALDAQLALLKAAIA--------- 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 AEVNGRLAELSlhmkeekcQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQE------ERTQSHVFKTE-LAREKDS 460
Cdd:pfam12128 740 ARRSGAKAELK--------ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERiavrrqEVLRYFDWYQEtWLQRRPR 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 461 SLVQLSESKRELTELRSALRVLQK---------EKEQLQTEKQ--ELLEYMRKLEARLEKVADEKWTEDAATEDEEATAG 529
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklrraklEMERKASEKQqvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGER 891
|
330
....*....|....*....
gi 160017771 530 LSCPASLTDSEDESPEDMR 548
Cdd:pfam12128 892 LAQLEDLKLKRDYLSESVK 910
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-506 |
9.44e-09 |
|
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: 58.98 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQ----LEDQVTELRSRVQELEAALATAR---QEHSELTEQYKGLSRSH-GELSEERDILS 220
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRResqsQEDLRNQLQNTVHELEAAKCLKEdmlEDSNTQIEQLRKMMLSHeGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 221 QQQGDHVARILElEDDIQTMSDKVLMKEV-----ELDR-----------VRDTVKALTRE-QEKLLRQLKEFQADKEQ-- 281
Cdd:pfam15921 195 DFEEASGKKIYE-HDSMSTMHFRSLGSAIskilrELDTeisylkgrifpVEDQLEALKSEsQNKIELLLQQHQDRIEQli 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 282 SEAELQ---------TVREENCCLNTELEEAKSRQEEQGA----QVQRLKDKLAHMKDTLGQAQQKVAE-LEPLKEQLrg 347
Cdd:pfam15921 274 SEHEVEitgltekasSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDkIEELEKQL-- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 348 vqELAASSQQKAALLGEELASAAGARDRTIAELhrsrleVAEVNGRLAELSLHMKEEKCQWSKErTGLLQSMEAEKDKIL 427
Cdd:pfam15921 352 --VLANSELTEARTERDQFSQESGNLDDQLQKL------LADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 428 KLSAEILRLEKTV---------QEERTQSHVFKTELAREKDSSLVQLSESKRELteLRSALRVLQKEKEQLQTEKQELLE 498
Cdd:pfam15921 423 DRNMEVQRLEALLkamksecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEM--LRKVVEELTAKKMTLESSERTVSD 500
|
....*...
gi 160017771 499 YMRKLEAR 506
Cdd:pfam15921 501 LTASLQEK 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-514 |
1.10e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.70 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 130 LEEADGGSDILLVVPKATVLQNQ-----------------------LDESQQER-----NDLMQLKLQLEDQVTE----L 177
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEfntlesaelrlshlhfgyksdetLIASRQEErqetsAELNQLLRTLDDQWKEkrdeL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 178 RSRVQELEAALATARQEHSELTEQYK-----GLSRSHGELSEERDIlsQQQGDHVARILE-LEDDIQTMSDK-----VLM 246
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQEQLPSW--QSELENLEERLKaLTGKHQDVTAKynrrrSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 247 KEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELqtvREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKD 326
Cdd:pfam12128 385 KEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 327 TLGQAQQKVAELEPLKEQlrgvQELAASSQQKAALlgeELASAAGARDRTIAELHRSRLEVAEVNGRLAEL--------- 397
Cdd:pfam12128 462 LLLQLENFDERIERAREE----QEAANAEVERLQS---ELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqag 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 398 SLH--MKEEKCQWSKE-----------RTGLLQSMEAEKDK-ILKLSAEILRLEK--------TVQEERTQSHVFKT--- 452
Cdd:pfam12128 535 TLLhfLRKEAPDWEQSigkvispellhRTDLDPEVWDGSVGgELNLYGVKLDLKRidvpewaaSEEELRERLDKAEEalq 614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 453 ---ELAREKDSSLVQLS----ESKRELTELRSA-------LRVLQKEKEQLQTEKQELL-EYMRKLEARLEKVADEK 514
Cdd:pfam12128 615 sarEKQAAAEEQLVQANgeleKASREETFARTAlknarldLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQL 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-490 |
1.20e-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: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 232 ELEDDIQTMSDkvLMKEveLDRVRDTVKAlTREQEKLLRQLKEFQADKEQSEAELQTVREEncclnteleEAKSRQEEQG 311
Cdd:COG4913 222 DTFEAADALVE--HFDD--LERAHEALED-AREQIELLEPIRELAERYAAARERLAELEYL---------RAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 312 AQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgvQELAASSQQKAALLGEELASAAgardrtiAELHRSRLEVAEVN 391
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALR--EELDELEAQIRGNGGDRLEQLE-------REIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 392 GRLAELslhmkeekcqwskertgllqsmeaeKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRE 471
Cdd:COG4913 359 RRRARL-------------------------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
250
....*....|....*....
gi 160017771 472 LTELRSALRVLQKEKEQLQ 490
Cdd:COG4913 414 LRDLRRELRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-513 |
4.09e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATArQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTMSDKvlmkEVELDRVRDTVKALTREQEKLLRQLKEFQaDKEQSEAELQTVREENCCLNTE-----LEEA 303
Cdd:PRK03918 322 EINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEklekeLEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE-----------PLKEQLRGvqELAASSQQKAALLGEELASAAG- 371
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRK--ELLEEYTAELKRIEKELKEIEEk 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 372 ---------------ARDRTIAELHRSRLEVAEVNGRLAELSLH-----------MKEEKCQWSKERTGLLQSMEAEKDK 425
Cdd:PRK03918 475 erklrkelrelekvlKKESELIKLKELAEQLKELEEKLKKYNLEelekkaeeyekLKEKLIKLKGEIKSLKKELEKLEEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 426 ILKLsAEILRLEKTVQEERTQSHvfkTELAREKDSSLVQLSESKRELTEL----------RSALRVLQKEKEQLQTEKQE 495
Cdd:PRK03918 555 KKKL-AELEKKLDELEEELAELL---KELEELGFESVEELEERLKELEPFyneylelkdaEKELEREEKELKKLEEELDK 630
|
410
....*....|....*...
gi 160017771 496 LLEYMRKLEARLEKVADE 513
Cdd:PRK03918 631 AFEELAETEKRLEELRKE 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
170-338 |
4.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 170 LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILS-----QQQGDHVARILELEDDIQTMSDKV 244
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCC-LNTELEE--AKSRQEEQGAQVQR-LKDK 320
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEErfAAALGDAVERELREnLEER 774
|
170
....*....|....*...
gi 160017771 321 LAHMKDTLGQAQQKVAEL 338
Cdd:COG4913 775 IDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-389 |
6.03e-08 |
|
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: 55.54 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 179 SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTV 258
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 259 KALTREQEKLLRQLKEF-----------QADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDT 327
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160017771 328 LGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAE 389
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-495 |
8.69e-08 |
|
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: 55.82 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 232 ELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQG 311
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 312 AQVQRLKDKLAHMKDtlgqAQQKVAELEPLKEQLRGVQELAAssQQKAALLGEELasaagarDRTIAELhrsRLEVAEVN 391
Cdd:TIGR00606 772 TLLGTIMPEEESAKV----CLTDVTIMERFQMELKDVERKIA--QQAAKLQGSDL-------DRTVQQV---NQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 392 GRLAELSLHMkEEKCQWSKERTGLLQSMeaeKDKILKLSAEILRLEKTVQeERTQSHVFKTELAREKDSSLVQLSESKRE 471
Cdd:TIGR00606 836 HELDTVVSKI-ELNRKLIQDQQEQIQHL---KSKTNELKSEKLQIGTNLQ-RRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
250 260
....*....|....*....|....
gi 160017771 472 LTELRSALRVLQKEKEQLQTEKQE 495
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKET 934
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
176-513 |
1.01e-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: 55.73 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 176 ELRSRVQELEAALATARQEHSEltEQYKglsrsHGELSEERDILSQQQGDhvarileLEDDIQTMSDkvlmkevELDRVR 255
Cdd:COG3096 282 ELSERALELRRELFGARRQLAE--EQYR-----LVEMARELEELSARESD-------LEQDYQAASD-------HLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 256 DTVkaltREQEKLLRqlkeFQADkeqseaelqtvreencclnteLEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKV 335
Cdd:COG3096 341 TAL----RQQEKIER----YQED---------------------LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 336 AElepLKEQLRGVQElAASSQQKAALlgeELASAAGARDRTIAELHRSRLEVAEVNGRLAELslhmKEEKCQWSKERTGL 415
Cdd:COG3096 392 DS---LKSQLADYQQ-ALDVQQTRAI---QYQQAVQALEKARALCGLPDLTPENAEDYLAAF----RAKEQQATEEVLEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 416 LQSME------AEKDKILKLsaeilrLEKTVQE-ERTQSHVFKTEL---AREKDSSLVQLSESKRELTELRSALRVLQKE 485
Cdd:COG3096 461 EQKLSvadaarRQFEKAYEL------VCKIAGEvERSQAWQTARELlrrYRSQQALAQRLQQLRAQLAELEQRLRQQQNA 534
|
330 340 350
....*....|....*....|....*....|....*...
gi 160017771 486 KEQLQ----------TEKQELLEYMRKLEARLEKVADE 513
Cdd:COG3096 535 ERLLEefcqrigqqlDAAEELEELLAELEAQLEELEEQ 572
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-525 |
1.01e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDIlsqQQGDHV 227
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL---KEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALtreqekLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQ 307
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV 387
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 AEVNGRLAEL-----SLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVfkTELAREKDSSL 462
Cdd:COG4717 405 EELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQELEELK 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160017771 463 VQLSESKRELTELRSALRVLQKEKEQLQTEKQ-ELLEYMRKLearLEKVADEKWTEDAATEDEE 525
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEY---FSRLTDGRYRLIRIDEDLS 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-526 |
1.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 251 LDRVRDTVKALTREQEKLLRQ------LKEFQADKEQSEAELQTVREEncclntELEEAKSRQEEQGAQVQRLKDKLAhm 324
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQaekaerYKELKAELRELELALLVLRLE------ELREELEELQEELKEAEEELEELT-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 kdtlGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAEL---SLHM 401
Cdd:TIGR02168 260 ----AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 402 KEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQshvfktelarekdsslvqlseskreLTELRSALRV 481
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------------------------LETLRSKVAQ 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 160017771 482 LQKEKEQLQTEKQELLEYMRKLEARLEKVADEKwtEDAATEDEEA 526
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEA 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-514 |
1.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELS-EERDILSQQQGDHV 227
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKV------LMKEVELDRVRDTVKALTREQEKLLRQLK---EFQADKEQSEAELQTVREENCCLNT 298
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYeaaleaALAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 299 ELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIA 378
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 379 ELHRSRLEVAEVNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREK 458
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEE----RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 459 DSSLVQLSESKRELTELRSALRVL--------------QKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
158-509 |
1.81e-07 |
|
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: 54.53 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 158 QERNDLMQLKLQLEDQVTELRSR-----------VQELEAA-------LATARQEHSELTEQYKGLSRSHGELSEERDIL 219
Cdd:pfam15964 307 KERDDLMSALVSVRSSLAEAQQRessayeqvkqaVQMTEEAnfektkaLIQCEQLKSELERQKERLEKELASQQEKRAQE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 220 SQQQGDHVARILE-LEDDIQTMSDKVLMKEVELDRVrdtvkalTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNT 298
Cdd:pfam15964 387 KEALRKEMKKEREeLGATMLALSQNVAQLEAQVEKV-------TREKNSLVSQLEEAQKQLASQEMDVTKVCGE---MRY 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 299 ELEEAKSRQEEQGAQVQRLKDKlahmkdTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIA 378
Cdd:pfam15964 457 QLNQTKMKKDEAEKEHREYRTK------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEH 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 379 ELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKT----VQEERTQSHVFKTEL 454
Cdd:pfam15964 531 QLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTfiakLKEECCTLAKKLEEI 610
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160017771 455 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEK 509
Cdd:pfam15964 611 TQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDK 665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-510 |
1.85e-07 |
|
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: 54.80 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 147 TVLQNQLD-------ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgELSEERDIL 219
Cdd:pfam01576 43 NALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 220 SQQQGDHV---ARILELEDDIQTMSDK--VLMKEVEL--DRVRDTVKALTREQEKlLRQLKEFQADKEQSEAELQTVREE 292
Cdd:pfam01576 120 QKLQLEKVtteAKIKKLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEK-AKSLSKLKNKHEAMISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 293 NCCLNTELEEAKSRQE-----------EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQ-LRGVQELaassQQKAA 360
Cdd:pfam01576 199 EEKGRQELEKAKRKLEgestdlqeqiaELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNaLKKIREL----EAQIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 361 LLGEELASAAGARDRtiAELHRSRLEvaevngrlaelslhmkEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:pfam01576 275 ELQEDLESERAARNK--AEKQRRDLG----------------EELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 441 QEErTQSHVFKTELAREKDSSLV-----QLSESKRELTELRSALRVLQKEKEQLQTE-------KQELLEYMRKLEARLE 508
Cdd:pfam01576 337 EEE-TRSHEAQLQEMRQKHTQALeelteQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQ 415
|
..
gi 160017771 509 KV 510
Cdd:pfam01576 416 EL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-380 |
2.38e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 185 EAALATARQEHSELTEQYKGLSRSHGELSEERDILsQQQGDHVARILELEDDiqtmsdkvlmkEVELDRVRDTVKALTRE 264
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWD-----------EIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 265 QEKLLR---QLKEFQADKEQSEAELQTVREencclntELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKV-AELEP 340
Cdd:COG4913 677 LERLDAssdDLAALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 160017771 341 LKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAEL 380
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-407 |
2.67e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQY-----KGLSRSHGELSEERDILS--- 220
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAeke 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 221 QQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTEL 300
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 301 EEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQqkvAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAEL 380
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250 260
....*....|....*....|....*..
gi 160017771 381 HRSRLEVAEVNGRLAELSLHMKEEKCQ 407
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-323 |
3.41e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLS-RSHGELSEERDILSQQQGDHVARI 230
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 231 LELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAKSRQEEQ 310
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE---LEAEIASLERRKSNI 438
|
170
....*....|...
gi 160017771 311 GAQVQRLKDKLAH 323
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
151-444 |
4.12e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 151 NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARI 230
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 231 LELEDDIQTMSDKVLM---KEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREenccLNTELEEAKSRQ 307
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKE----LEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGaqvqrlkdklaHMKDTLGQAQQKVAELEPLKEQlrgVQELAASSQQkaalLGEELASAAGARDRT---IAELHRSR 384
Cdd:COG1340 157 EKNE-----------KLKELRAELKELRKEAEEIHKK---IKELAEEAQE----LHEEMIELYKEADELrkeADELHKEI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 385 LEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKlsaEILRLEKTVQEER 444
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK---EELEEKAEEIFEK 275
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
149-513 |
4.93e-07 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 53.15 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELeaALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQtmsdkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQAD-KEQSEAELQTVREENCCLNTELEEAKSRQ 307
Cdd:COG4192 117 AVADLRNLLQ-----------QLDSLLTQRIALRRRLQELLEQINWLHQDfNSELTPLLQEASWQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGA--QVQRLKDKLAHMKDTLGQ--AQQKVAELEPLKEQLrgvQELAASSQQKAALLGEelASAAGARDRTIAELhrs 383
Cdd:COG4192 186 NLQNElqLLLRLLAIENQIVSLLREvaAARDQADVDNLFDRL---QYLKDELDRNLQALKN--YPSTITLRQLIDEL--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 384 rLEVAEVNGRLAELslhMKEEkcqwsKERTGLLQSMEAEKDKILKLSAEilRLEKTVQEERTQSHVFKTELAREKDSS-- 461
Cdd:COG4192 258 -LAIGSGEGGLPSL---RRDE-----LAAQATLEALAEENNSILEQLRT--QISGLVGNSREQLVALNQETAQLVQQSgi 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 462 ----------------------------LVQLSES-----------------KRELTELRSALRV-LQKEKEQLQTEKQE 495
Cdd:COG4192 327 lllaiallslllavlinyfyvrrrlvkrLNALSDAmaaiaagdldvpipvdgNDEIGRIARLLRVfRDQAIEKTQELETE 406
|
410
....*....|....*...
gi 160017771 496 LLEYMRkLEARLEKVADE 513
Cdd:COG4192 407 IEERKR-IEKNLRQTQDE 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-292 |
5.04e-07 |
|
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: 51.46 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDI--LSQQQGDH 226
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 227 VARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREE 292
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-509 |
5.60e-07 |
|
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: 52.80 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQqqgdhva 228
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 rilELEDdiqtmsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:pfam05483 297 ---ELED-----------IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 E-QGAQVQRLKDKLAHMKDTLGQAQQKVAELEplkeqlrgvqELAASSQQKAALLgEELASAAGARDRTIAELHRSRLEV 387
Cdd:pfam05483 363 ElLRTEQQRLEKNEDQLKIITMELQKKSSELE----------EMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 AEVNGRLAELslhmkeekcqwskerTGLLQSMEAEkdkILKLSAEILRLEKTVQEERTQSHVFKTELAREK------DSS 461
Cdd:pfam05483 432 EELKGKEQEL---------------IFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknielTAH 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 160017771 462 LVQLSESKRELTELRSALRV-LQKEKEQLQTEKQELLEYMRKLEARLEK 509
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIENLEEK 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
258-543 |
6.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 258 VKALTREQEKLLRQLKEFQADKEQSE--AELQTVREENCCLNTELEeaksRQEEQGAQVQRLKDKLAhmkDTLGQAQQKV 335
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIE----RYEEQREQARETRDEAD---EVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 336 AELEPLKEQLRGVQELAASSQQKAALLGEELASA-------AGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQW 408
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLrerleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 409 SKERTgllqSMEAEKDKILKLSAEILRLEKTVQEERTQShvfkTELAREKDSSLVQLSESKRELTELRSALRVLQK---- 484
Cdd:PRK02224 331 EECRV----AAQAHNEEAESLREDADDLEERAEELREEA----AELESELEEAREAVEDRREEIEELEEEIEELRErfgd 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160017771 485 ---EKEQLQTEKQELLEYMRKLEARL-EKVADEKWTEDAATEDEEATAGLSCPASLTDSEDES 543
Cdd:PRK02224 403 apvDLGNAEDFLEELREERDELREREaELEATLRTARERVEEAEALLEAGKCPECGQPVEGSP 465
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
214-546 |
8.26e-07 |
|
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: 52.27 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 214 EERDILSQQQGDHVARILELEDDIQTM---SDKVLMKEVELDRVrDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVR 290
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEklgENAESSKRLNENAN-NLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 291 EEnccLNTELEEAKSRQEeqgAQVQRLKDKLAHMKDTLGQAQQKVAElepLKEQLRGVQELAASSqqkaallgEELASAA 370
Cdd:COG5185 321 AE---AEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKE---EIENIVGEVELSKSS--------EELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 371 GARDRTIAELHRSRLEVAEVNGRLAE-LSLHMKEEKCQWSKERT---GLLQSMEAEKDKILKLSAEILRLEKTVQEERTQ 446
Cdd:COG5185 384 DTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQRqieQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 447 shvfktelarekdsslvQLSESKREL-TELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEK-VADEKWTEDAATEDE 524
Cdd:COG5185 464 -----------------RLEEAYDEInRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERqLEGVRSKLDQVAESL 526
|
330 340
....*....|....*....|..
gi 160017771 525 EATAGLSCPASLTDSEDESPED 546
Cdd:COG5185 527 KDFMRARGYAHILALENLIPAS 548
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
172-496 |
8.83e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 172 DQVTELRSRVQELEAALATARQehselteqykglsrSHGELSEERDILSQQQGDhvarileLEDDIQTMSDKvlmkeveL 251
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQY--------------RLVEMARELAELNEAESD-------LEQDYQAASDH-------L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 252 DRVRDTVkaltREQEKLLRQLKEFQADKEQSEAELQTVREenccLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTL--- 328
Cdd:PRK04863 338 NLVQTAL----RQQEKIERYQADLEELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 329 ----GQAQQKVAELEPLKEQ-------LRGVQELAASSQQKAALLGEELASAagARDRTIAELHRSRLEVA-EVNGRLA- 395
Cdd:PRK04863 410 qtraIQYQQAVQALERAKQLcglpdltADNAEDWLEEFQAKEQEATEELLSL--EQKLSVAQAAHSQFEQAyQLVRKIAg 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 396 ELSlhmKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKT----------------ELAREKD 459
Cdd:PRK04863 488 EVS---RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfckrlgknlddedeleQLQEELE 564
|
330 340 350
....*....|....*....|....*....|....*..
gi 160017771 460 SSLVQLSESKRELTELRSALRvlqKEKEQLQTEKQEL 496
Cdd:PRK04863 565 ARLESLSESVSEARERRMALR---QQLEQLQARIQRL 598
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-355 |
1.52e-06 |
|
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: 49.92 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 169 QLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgelseerdilsqqqgdhvaRILELEDDIQTMSDKVLMKE 248
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK---------------------EIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 249 VELDRVRDtvkalTREQEKLLRQLKEFQADKEQSEAELQTVREencclntELEEAKSRQEEQGAQVQRLKDKLAHMKDTL 328
Cdd:COG1579 80 EQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|....*..
gi 160017771 329 gqaQQKVAELEPLKEQLRGVQELAASS 355
Cdd:COG1579 148 ---DEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-510 |
1.95e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQ-------TMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTEL- 300
Cdd:TIGR04523 125 ELNKLEKQKKenkknidKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLs 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 301 --EEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQkvaELEPLKEQLRGVQE--LAASSQQkaallgeelasaagarDRT 376
Cdd:TIGR04523 205 nlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTqlNQLKDEQ----------------NKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 377 IAELHRSRLEVAEVNGRLAELS----------LHMKEEKCQ-WSKERTGLLQSMEAEKD-----------KILKLSAEIL 434
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEkqlnqlkseiSDLNNQKEQdWNKELKSELKNQEKKLEeiqnqisqnnkIISQLNEQIS 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 435 RLEKTVQEERTQShvfktelarekdsslvqlSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKV 510
Cdd:TIGR04523 346 QLKKELTNSESEN------------------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-514 |
3.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 301 EEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARD--RTIA 378
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 379 ELHRSRLEVAEVNGRLAELSLHMKEekcqwskertgllqsmeaekdkILKLSAEILRLEKTVQEERTQshvFKTELAREK 458
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEE----------------------LRELEEELEELEAELAELQEE---LEELLEQLS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 459 DSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-558 |
3.41e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEaELQTVREENcclnTELEEAKSRQEEQGAQVQRlKDKLAHM 324
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAK----KKADEAKKAEEAKKADEAK-KAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 KDTLGQAQQKVAELEPLK-EQLRGVQELAASSQQKAAllgEELASAAGARDRTIAELHRSRLEVAEvngRLAELSLHMKE 403
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKA---EEDKNMALRKAEEAKKAEEARIEEVM---KLYEEEKKMKA 1609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 404 E---KCQWSKERTGLLQSMEAEKDKILKLS---AEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRS 477
Cdd:PTZ00121 1610 EeakKAEEAKIKAEELKKAEEEKKKVEQLKkkeAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 478 ALRVLQKEKEQL------------------QTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEATAglscPASLTDS 539
Cdd:PTZ00121 1690 AAEALKKEAEEAkkaeelkkkeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK----IAHLKKE 1765
|
330
....*....|....*....
gi 160017771 540 EDESPEDMRLPSYGLCESG 558
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEE 1784
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
656-679 |
3.49e-06 |
|
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: 43.71 E-value: 3.49e-06
10 20
....*....|....*....|....
gi 160017771 656 CPICKERFPAESDKDALEGHMDGH 679
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-494 |
4.00e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 252 DRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTEleeaksrqEEQGAQVQRLKDklahMKDTLGQA 331
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS--------EEAKLLLQQLSE----LESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 332 QQKVAELEPLKEQLRgvQELAASSQQKAALLGEELASAAgardrtIAELHRSRLEVAEVNGRLAELSLHMKEEKcqwsKE 411
Cdd:COG3206 232 RAELAEAEARLAALR--AQLGSGPDALPELLQSPVIQQL------RAQLAELEAELAELSARYTPNHPDVIALR----AQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 412 RTGLLQSMEAEKDKIL-KLSAEILRLEKTVQEERTQSHVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKEKEQLQ 490
Cdd:COG3206 300 IAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELE-AELRRLEREVEVARELYESLLQRLEEAR 378
|
....
gi 160017771 491 TEKQ 494
Cdd:COG3206 379 LAEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
220-456 |
4.87e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 220 SQQQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQtvreencclnte 299
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 300 leEAKSRQEEQGAQVQRLKDKLAHMKDTLgQAQQKVAELEPLkeqlrgvqeLAASSQQKAALLGEELASAAGARDRTIAE 379
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEELAELLRAL-YRLGRQPPLALL---------LSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 380 LHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAR 456
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-446 |
7.85e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 165 QLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQykgLSRSHGELSEERDILSQQQgdhvARILELEDDIQTMSDKV 244
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLE----EELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHM 324
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 KDTlgQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAElhrsRLEVAEVNGRLAELSLHMKEE 404
Cdd:COG4372 177 SEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 160017771 405 KCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQ 446
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-540 |
1.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRsrVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDH-V 227
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKAL----TREQEKLLRQLKEFQADKEQSEAELQTVREENcclnTELEEA 303
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALEEELEALEEAL----AEAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKV-----AELEPLKEQLRGVQEL-----AASSQQKAA--LLG-------- 363
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALrdalaEALGLDEAELPFVGELievrpEEERWRGAIerVLGgfaltllv 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 364 -EELASAA--------------------GARDRTIAELHRS----RLEVAE------VNGRLAELSLHMK----EE--KC 406
Cdd:COG4913 494 pPEHYAAAlrwvnrlhlrgrlvyervrtGLPDPERPRLDPDslagKLDFKPhpfrawLEAELGRRFDYVCvdspEElrRH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 407 QWSKERTGLLQSMEA--EKD-----------------KILKLSAEILRLEKTVQEERTQSHVFKTELA------------ 455
Cdd:COG4913 574 PRAITRAGQVKGNGTrhEKDdrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDalqerrealqrl 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 456 -----------------REKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEkwtED 518
Cdd:COG4913 654 aeyswdeidvasaereiAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LD 730
|
490 500
....*....|....*....|..
gi 160017771 519 AATEDEEATAGLSCPASLTDSE 540
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLE 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
202-519 |
1.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 202 YKGLSRSHGELSEERDILSqqqgDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQ 281
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 282 SEAelqtvreenccLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLK------------------- 342
Cdd:PRK03918 240 IEE-----------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklsefyeeylde 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 343 ------------EQLRGVQELAASSQQKAALLGEELASAAGARDRtIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSK 410
Cdd:PRK03918 309 lreiekrlsrleEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 411 ERTGLLQSMEAEK----DKILKLSAEILRLEKTVQEERT----------QSHVFKTELAREKDSSLV-----QLSESKRE 471
Cdd:PRK03918 388 KLEKELEELEKAKeeieEEISKITARIGELKKEIKELKKaieelkkakgKCPVCGRELTEEHRKELLeeytaELKRIEKE 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 472 LTELRSALRVLQKEKEQLQTE---------KQELLEYMRKLEARLEKVADEKWTEDA 519
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLEELEKKA 524
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
149-350 |
1.65e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG1340 34 LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 ---RILELEDDIQTmsdKVLMKEVElDRVRDTVKALTREQEKLLRQLKEFQADKEqSEAELQTVREencclntELEEAKS 305
Cdd:COG1340 114 lrkEIERLEWRQQT---EVLSPEEE-KELVEKIKELEKELEKAKKALEKNEKLKE-LRAELKELRK-------EAEEIHK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 160017771 306 RQEEQGAQVQRLKDKlahMKDTLGQAQQKVAELEPLKEQLRGVQE 350
Cdd:COG1340 182 KIKELAEEAQELHEE---MIELYKEADELRKEADELHKEIVEAQE 223
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-347 |
2.69e-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: 46.67 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 147 TVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALA----TARQEHSELTEQYKGLSRSHGELSEErdiLSQQ 222
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAE---LERL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 223 QGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTR------EQEKLLRQLKEFQADKeqsEAELQTVREENCCL 296
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQssssqsELENRLHQLTETLIQK---QTMLEALSTEKNSL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 160017771 297 NTELEEA-KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRG 347
Cdd:pfam09787 197 VLQLERMeQQIKELQGEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-508 |
3.55e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 155 ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQehselteqykglsrshgELSEERDilsqqqgdhvaRILELE 234
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKR-----------------QLDRESD-----------RNQELQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 235 DDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEfqadKEQSEAELqtvREENCCLNTELEEAKSRQEEQGAQV 314
Cdd:pfam05557 55 KRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADA---REVISCLKNELSELRRQIQRAELEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 315 QRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELAS---------AAGARDRTIAELHRSRL 385
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqdseivkNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 386 EVAEVNGRLAELS---LHMKEEKCQWSKErtglLQSMEAEKDKILKLSAEILRLEKTVQE-ERT-QSHVF---KTELARE 457
Cdd:pfam05557 208 RLREHNKHLNENIenkLLLKEEVEDLKRK----LEREEKYREEAATLELEKEKLEQELQSwVKLaQDTGLnlrSPEDLSR 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160017771 458 KdssLVQLSES----KRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLE 508
Cdd:pfam05557 284 R---IEQLQQReivlKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK 335
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
160-309 |
5.27e-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: 45.78 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 160 RNDLMQ-LKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELseerdilsqqqgdhvariLELEDDIQ 238
Cdd:smart00787 138 RMKLLEgLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQL------------------KQLEDELE 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160017771 239 TMsdkvlmKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEE 309
Cdd:smart00787 200 DC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-525 |
5.48e-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: 46.71 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 162 DLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgelseERDILSQ-QQGDHVARIL--------- 231
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF-----ERDLQARdEQGEEKRRQLvkqvrelea 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 232 ELEDDIQTMSDKVLMK---EVELDRVRDTVKALTREQEKLLRQLKEFQADKEQseaelqtvreenccLNTELEEAKSRQE 308
Cdd:pfam01576 757 ELEDERKQRAQAVAAKkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD--------------LQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQlrgvqelaasSQQKAALLGEELASaaGARDRTIAELHRSRLEva 388
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ----------AQQERDELADEIAS--GASGKSALQDEKRRLE-- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 389 evnGRLAELSLHMKEEKCqwskertgllqSMEAEKDKILKLSAEILRLEKTVQEERTQSHvfKTELAREKDSSlvQLSES 468
Cdd:pfam01576 889 ---ARIAQLEEELEEEQS-----------NTELLNDRLRKSTLQVEQLTTELAAERSTSQ--KSESARQQLER--QNKEL 950
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160017771 469 KRELTELRSALRVLQKE------------KEQLQTEKQElleymRKLEARLEKVADEKWTEDAATEDEE 525
Cdd:pfam01576 951 KAKLQEMEGTVKSKFKSsiaaleakiaqlEEQLEQESRE-----RQAANKLVRRTEKKLKEVLLQVEDE 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-509 |
5.97e-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: 46.71 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 154 DESQQERNDLMQL----KLQLEDQVTELRSRVQELEAalatarqEHSELTEQYKGLSRSHGELSEERDILsqqqgdhVAR 229
Cdd:pfam01576 4 EEEMQAKEEELQKvkerQQKAESELKELEKKHQQLCE-------EKNALQEQLQAETELCAEAEEMRARL-------AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 230 ILELEDDIQTMsdkvlmkEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNT---ELEEAKSR 306
Cdd:pfam01576 70 KQELEEILHEL-------ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkikKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 307 QEEQGAQVQR----LKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHR 382
Cdd:pfam01576 143 LEDQNSKLSKerklLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 383 srlEVAEVNGRLAEL--SLHMKEEKCQWSKERTG--LLQSMEAEKdKILKLSAEILRLEKTVQEERTQS----------- 447
Cdd:pfam01576 223 ---QIAELQAQIAELraQLAKKEEELQAALARLEeeTAQKNNALK-KIRELEAQISELQEDLESERAARnkaekqrrdlg 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160017771 448 ---HVFKTELAREKDSSLVQL---SESKRELTELRSALRVLQKEKE-QLQ----------TEKQELLEYMRKLEARLEK 509
Cdd:pfam01576 299 eelEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRSHEaQLQemrqkhtqalEELTEQLEQAKRNKANLEK 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-565 |
6.49e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 126 ELVTLEEADGGSDILLVVPKATVLQNQL-DESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEhselteqykg 204
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 205 LSRSHGELSEERDILSQQQGD--HVARIleleddIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQS 282
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSdgHAMKV------AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 283 EAELQTVREENCCLNTELEEAKSrqeeqgaQVQRLKDKLAHMKDTLGQAQQKVAELEPL--KEQLRGVQELAASSQQKAA 360
Cdd:pfam15921 775 SQELSTVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALDKASLQFAECQDIiqRQEQESVRLKLQHTLDVKE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 361 LLGEELASAAGARDRTI--AELHRSRLEVAEVNGRLAELSLHmkeekcqwSKERTGLLQSMEAEKDKILKLSAEILRLEK 438
Cdd:pfam15921 848 LQGPGYTSNSSMKPRLLqpASFTRTHSNVPSSQSTASFLSHH--------SRKTNALKEDPTRDLKQLLQELRSVINEEP 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 439 TVQEERTQSHVFKTELAREKDSSLVQLSESkreltELRSalRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEkwtED 518
Cdd:pfam15921 920 TVQLSKAEDKGRAPSLGALDDRVRDCIIES-----SLRS--DICHSSSNSLQTEGSKSSETCSREPVLLHAGELE---DP 989
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 160017771 519 AATEDEEATAGLSCPASLTDSEDESPEdmRLPSYGLCES---GNTSSSPP 565
Cdd:pfam15921 990 SSCFTFPSTASPSVKNSASRSFHSSPK--KSPVHSLLTSsaeGSIGSSSQ 1037
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
145-458 |
8.36e-05 |
|
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: 45.44 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgELSEERDILSQQQG 224
Cdd:pfam19220 77 RLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNR-------ALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQAdkeQSEAELQTVREENCCLNTELEEAK 304
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELET---QLDATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSR 384
Cdd:pfam19220 227 RAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 385 LEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEER----TQSHVFKTELAREK 458
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERaaleQANRRLKEELQRER 384
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-366 |
9.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILELEDDIQTMSDKVLMKEVELDrvRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAK 304
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ---KEKEKKDLI 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160017771 305 SRQEEQGAQVQRLKDKLAHMKdtlgqaqqkvAELEPLKEQLRGVQELAASSQQKAALLGEEL 366
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK----------KENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
271-528 |
9.76e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 271 QLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELeplKEQLRGVQE 350
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL---KEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 351 LAASSQQKAALLGEELASAAGARdRTIAELHR--SRLEVAEVNgrlAELSLHmKE----EKCQWSKERTGLLQSMEAEKD 424
Cdd:COG1340 86 KLNELREELDELRKELAELNKAG-GSIDKLRKeiERLEWRQQT---EVLSPE-EEkelvEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 425 KILKLSAEILRLEKTVQEERTQshvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTE-----------K 493
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKK----IKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKadelheeiielQ 236
|
250 260 270
....*....|....*....|....*....|....*
gi 160017771 494 QELLEYMRKLEARLEKVADEKWTEDAATEDEEATA 528
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-278 |
9.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 151 NQLDESQQERNDLMQLK---LQLEDQVTELR---SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQg 224
Cdd:COG4913 651 QRLAEYSWDEIDVASAEreiAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL- 729
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 DHVARILE---------LEDDIQTMSDKVLMKEVEL-------DRVRDTVKALTREQEKLLRQLKEFQAD 278
Cdd:COG4913 730 DELQDRLEaaedlarleLRALLEERFAAALGDAVERelrenleERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
147-515 |
9.86e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 147 TVLQNQLDESQQERNDLMQLKL--QLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERdilsqqqg 224
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYlkQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL-------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 dhvARILELEDDIQTMSDKVLMKE---VELDRVRDTVKALTREQEKLL-----RQLKEFQADKEQSEAELQTVREENCCL 296
Cdd:TIGR00606 262 ---SKIMKLDNEIKALKSRKKQMEkdnSELELKMEKVFQGTDEQLNDLyhnhqRTVREKERELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 297 NTELEEAKSRQEEQGAQVQRLKDKLaHMKDTLGQAQQKVAELEPLKE------QLRGVQELAASSQQKAALLGEELASAA 370
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHI-RARDSLIQSLATRLELDGFERgpfserQIKNFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 371 GARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVf 450
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLT- 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 451 KTELAREKdsslvqlsESKRELTELRSALRVLQKEKEQLQTEKQ---ELLEYMRKLEARLEKVADEKW 515
Cdd:TIGR00606 497 ETLKKEVK--------SLQNEKADLDRKLRKLDQEMEQLNHHTTtrtQMEMLTKDKMDKDEQIRKIKS 556
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
264-511 |
1.04e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 264 EQEKLLRQLKEFQaDKEQSEAELQTVReencclnTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKE 343
Cdd:PRK03918 146 SREKVVRQILGLD-DYENAYKNLGEVI-------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 344 QLRGvqELAASSQQKAALlgEELASaagardrtiaELHRSRLEVAEVNGRLAELslhmkEEKCQWSKERtgllqsMEAEK 423
Cdd:PRK03918 218 ELRE--ELEKLEKEVKEL--EELKE----------EIEELEKELESLEGSKRKL-----EEKIRELEER------IEELK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 424 DKILKLSAEILRLEKTVQEERTQShvfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKL 503
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
|
....*...
gi 160017771 504 EARLEKVA 511
Cdd:PRK03918 348 KELEKRLE 355
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
149-335 |
1.19e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgELSEERDI---LSQQQGD 225
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-KMYEKGGVcptCTQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 226 HVARILELEDDIQTMSDKVlmkeVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKS 305
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSL----EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
170 180 190
....*....|....*....|....*....|
gi 160017771 306 RQEEQGAQVQRLKDKLAHMKDTLGQAQQKV 335
Cdd:PHA02562 373 EFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-397 |
1.24e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVA 228
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQE 308
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVA 388
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
....*....
gi 160017771 389 EVNGRLAEL 397
Cdd:COG4372 297 LLALLLNLA 305
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
137-506 |
1.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 137 SDILLVVPKATVLQNQLdesQQERNDLMQLKLQLEDQ---VTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgELS 213
Cdd:PRK04863 334 SDHLNLVQTALRQQEKI---ERYQADLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 214 EERDILSQQQGDHVARILELEDDIQTMSDKVlmkEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREen 293
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNA---EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRK-- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 294 ccLNTELEeaKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKaalLGEELASAAgar 373
Cdd:PRK04863 485 --IAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKR---LGKNLDDED--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 374 drtiaelhrsrlEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEaekdkilKLSAEILRLEKTvqeeRTQSHVFKTE 453
Cdd:PRK04863 555 ------------ELEQLQEELEARLESLSESVSEARERRMALRQQLE-------QLQARIQRLAAR----APAWLAAQDA 611
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 454 LAREKDSSLVQLsESKRELTELRSAL----RVLQKEKEQLQTEKQELLEYMRKLEAR 506
Cdd:PRK04863 612 LARLREQSGEEF-EDSQDVTEYMQQLlereRELTVERDELAARKQALDEEIERLSQP 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-530 |
1.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 168 LQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQgdhvARILELEDDIQTMsDKVLMK 247
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE----KRLEELEERHELY-EEAKAK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 248 EVELDRVRDTVKALTreQEKLLRQLKEFQADKEQSEAELQTVREENCCLNT----------ELEEAKSR---------QE 308
Cdd:PRK03918 371 KEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKeikelkkaieELKKAKGKcpvcgreltEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 309 EQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGV--QELAASSQQKAALLGEELASAAGARDrtIAELHRSRLE 386
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYN--LEELEKKAEE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 387 VAEVNGRLAELSLHMK------EEKCQWSKERTGL---LQSMEAEKDKILK-LSAEILRLEKTVQEERTQSHVFKTELAR 456
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKslkkelEKLEELKKKLAELekkLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLE 606
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 457 EKDSSlvqlSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWTE--DAATEDEEATAGL 530
Cdd:PRK03918 607 LKDAE----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElrEEYLELSRELAGL 678
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-614 |
1.84e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 248 EVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKlahmkdt 327
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 328 lgqaqqkvaelepLKEQLRGVQELAASSQQKAALLGEElasaagardrtiaelhrsrlEVAEVNGRLAELSlhmkeekcq 407
Cdd:COG3883 88 -------------LGERARALYRSGGSVSYLDVLLGSE--------------------SFSDFLDRLSALS--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 408 wskertgllQSMEAEKDKILKLSAEILRLEKTvqeertqshvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE 487
Cdd:COG3883 126 ---------KIADADADLLEELKADKAELEAK-----------KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 488 QLQTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEATAGLSCPASLTDSEDESPEDMRLPSYGLCESGNTSSSPPGP 567
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 160017771 568 REPSSLVVINQPAPIAPQFSGPGEASSSDSEAEDEKSVLMAAVQSGG 614
Cdd:COG3883 266 GAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-347 |
2.33e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 230 ILELEDDIQTMSDKVLMKEVEL-----DRVRDTVKALTREQEkLLRQLKEFQADKEQSEaeLQTVREENCCLNTELEEAK 304
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELlnsikPKLRDRKDALEEELR-QLKQLEDELEDCDPTE--LDRAKEKLKKLLQEIMIKV 224
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 160017771 305 SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRG 347
Cdd:smart00787 225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
162-512 |
2.60e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 162 DLMQLKLQLEDQVTElrSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ------GDHVARILELED 235
Cdd:TIGR00618 197 ELLTLRSQLLTLCTP--CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkqqllKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 236 DIQTMSD-------------------KVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADK---EQSEAELQTVREEN 293
Cdd:TIGR00618 275 QEAVLEEtqerinrarkaaplaahikAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQssiEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 294 CCLNTELEEAKSRQEE-------------QGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQE--LAASSQQK 358
Cdd:TIGR00618 355 IHIRDAHEVATSIREIscqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 359 AALLGEELASAAGARDRTIA-----------------------------------ELHRSRLEVAEVNGRLAELSLHMKE 403
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEklekihlqesaqslkereqqlqtkeqihlqetrkkAVVLARLLELQEEPCPLCGSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 404 EKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLV---QLSESKRELTELRSALR 480
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqCDNRSKEDIPNLQNITV 594
|
410 420 430
....*....|....*....|....*....|..
gi 160017771 481 VLQKEKEQLQTEKQELLEYMRKLEARLEKVAD 512
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
185-504 |
2.83e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 185 EAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILEL--EDDIQTMSDKVLMKEVELDRVRDTVKAL- 261
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAQHRAQEQQLr 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 262 -----TREQEKLLRQLKEFQA--DKEQSEAELQTVREENcclnTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQK 334
Cdd:COG3096 864 qqldqLKEQLQLLNKLLPQANllADETLADRLEELREEL----DAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 335 VAELEPLKEQLRGV-QELAASSQ--QKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKC-QWSK 410
Cdd:COG3096 940 QADYLQAKEQQRRLkQQIFALSEvvQRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYsQYNQ 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 411 ERTGLLQSMEAEKDKILKLSAEILRLEKTVQEErtqshvfKTELAREKDSSLVQlseskrELTELRSALRVLQKEKEQLQ 490
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQELEQELEELGVQADAE-------AEERARIRRDELHE------ELSQNRSRRSQLEKQLTRCE 1086
|
330
....*....|....
gi 160017771 491 TEKQELLEYMRKLE 504
Cdd:COG3096 1087 AEMDSLQKRLRKAE 1100
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-389 |
2.93e-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: 42.99 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 215 ERDILSQQQGDHVARILELEDDIQTMSDkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREenc 294
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 295 clNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELeplKEQLRGVQELAASSQqkaallgEELASAAGARD 374
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEL---EAELAELEAELEEKK-------AELDEELAELE 155
|
170
....*....|....*
gi 160017771 375 RTIAELHRSRLEVAE 389
Cdd:COG1579 156 AELEELEAEREELAA 170
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
232-517 |
3.21e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 232 ELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQAdkeqseaELQTVREENCCLNTELEEAKSRQEEQG 311
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 312 AQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQElaasSQQKAALLGEElasaagARD--RTIAELhRSRLEVAE 389
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEW----RQQTEVLSPEE------EKElvEKIKEL-EKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 390 vngRLAELSLHMKEEKCQWSKERTgllqSMEAEKDKILKLSAEILRLEKTVQEERTQshvfKTELAREKDSSLVQLSESK 469
Cdd:COG1340 154 ---KALEKNEKLKELRAELKELRK----EAEEIHKKIKELAEEAQELHEEMIELYKE----ADELRKEADELHKEIVEAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 160017771 470 RELTELRSALRVLQKEKEQLQTEKQELLEYMRKLE-ARLEKVADEKWTE 517
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKrEKEKEELEEKAEE 271
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-447 |
4.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 234 EDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQ 313
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 314 VQR--------------------------LKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELA 367
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 368 SAAGARDRTIAELhrsRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQS 447
Cdd:COG3883 175 AQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
145-495 |
4.96e-04 |
|
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: 43.27 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgelseerdilsqqqg 224
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK--------------------- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 dhvaRILELEDDIQT---MSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELqtvreencclnTELE 301
Cdd:pfam10174 542 ----KAHNAEEAVRTnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKI-----------AELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 302 EAKSRQ-EEQGAQVQRLKDklahmkdtlGQAQQKVAELEPLKEQLRGVQELAASSQQKAAllgEELasaagardrtIAEL 380
Cdd:pfam10174 607 SLTLRQmKEQNKKVANIKH---------GQQEMKKKGAQLLEEARRREDNLADNSQQLQL---EEL----------MGAL 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 381 HRSRLEVAEVNGRLA--ELSLHmkeekcqwskERTGLLQSMEAEKDKILKlsaEILRLEKtvqeertqshvfKTELA--R 456
Cdd:pfam10174 665 EKTRQELDATKARLSstQQSLA----------EKDGHLTNLRAERRKQLE---EILEMKQ------------EALLAaiS 719
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 160017771 457 EKDS--SLVQLSESKRELTELRSALrvLQKEKEQL-QTEKQE 495
Cdd:pfam10174 720 EKDAniALLELSSSKKKKTQEEVMA--LKREKDRLvHQLKQQ 759
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
250-530 |
5.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 250 ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLG 329
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 330 QAQQKVAELE----PLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHR-----SRLEVAEVNGRLAEL-SL 399
Cdd:COG4372 112 ELQEELEELQkerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAleqelQALSEAEAEQALDELlKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 400 HMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSAL 479
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 160017771 480 RVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEATAGL 530
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
262-509 |
5.64e-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: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 262 TREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEqgaqvQRLKDKLAHMKdtlgQAQQKVAELEPL 341
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEY-----YQLKEKLELEE----EYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 342 KEQLRGVQELAASSQQKAALLGEELAsaagARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEA 421
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 422 EKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMR 501
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
....*...
gi 160017771 502 KLEARLEK 509
Cdd:pfam02463 392 LKEEELEL 399
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-492 |
6.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 171 EDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEerdilsqqqgdHVARILELEDDiqTMSDKVLMKEVE 250
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNR-----------LLPRLNLLADE--TLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 251 LDRVRDTVKALTREQ---EKLLRQLKEFQADKEQSEAelqtvreenccLNTELEEAKSRQEEQGAQVQRLKD---KLAHM 324
Cdd:PRK04863 903 LDEAEEAKRFVQQHGnalAQLEPIVSVLQSDPEQFEQ-----------LKQDYQQAQQTQRDAKQQAFALTEvvqRRAHF 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 KDTlgQAQQKVAELEPLKEQLRgvqelaassqqkaallgEELASAAGARDRTIAELHRSRLEVAEVNGRLAEL--SLHMK 402
Cdd:PRK04863 972 SYE--DAAEMLAKNSDLNEKLR-----------------QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLksSYDAK 1032
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 403 EEKCQWSKER---TGLLQSMEAEKdkilKLSAEILRLEKTVQEERTQshvfktelareKDSSLVQLSESKRELTELRSAL 479
Cdd:PRK04863 1033 RQMLQELKQElqdLGVPADSGAEE----RARARRDELHARLSANRSR-----------RNQLEKQLTFCEAEMDNLTKKL 1097
|
330
....*....|...
gi 160017771 480 RVLQKEKEQLQTE 492
Cdd:PRK04863 1098 RKLERDYHEMREQ 1110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-361 |
7.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 130 LEEADGGSDILlvvpkaTVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSH 209
Cdd:COG4913 677 LERLDASSDDL------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 210 GE-----------LSEERDILSQQQGDHVARILELEDDI-QTMSDKVLMKEVELDRVRDTVKALtREQEKLLRQLK---- 273
Cdd:COG4913 751 LEerfaaalgdavERELRENLEERIDALRARLNRAEEELeRAMRAFNREWPAETADLDADLESL-PEYLALLDRLEedgl 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 274 -EFQAD-----KEQSEAELQTVREEnccLNTELEEAKSR-----------------------QEEQGAQVQRLKDKL--- 321
Cdd:COG4913 830 pEYEERfkellNENSIEFVADLLSK---LRRAIREIKERidplndslkripfgpgrylrleaRPRPDPEVREFRQELrav 906
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 160017771 322 --AHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAAL 361
Cdd:COG4913 907 tsGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARVL 948
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
248-357 |
8.05e-04 |
|
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: 42.05 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 248 EVELDRVRDTVKALTREQEKLLRQLK----EFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAH 323
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQqlrtELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRY 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 160017771 324 MKDTL--------GQAQQKVAELEPLKEQLRgVQELAASSQQ 357
Cdd:pfam09787 126 LEEELrrskatlqSRIKDREAEIEKLRNQLT-SKSQSSSSQS 166
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-489 |
8.10e-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: 41.45 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 332 QQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQwsKE 411
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 412 RTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQL 489
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
176-326 |
8.10e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 176 ELRSRV---QELEAALATARQEHSELTEQYKGLSRSHGElseerdilsQQQGDHVARILELEDDIQTMSDKVLMKEVELD 252
Cdd:COG2433 367 EVKARVirgLSIEEALEELIEKELPEEEPEAEREKEHEE---------RELTEEEEEIRRLEEQVERLEAEVEELEAELE 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 253 RVRDTVKALTREqeklLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKD--KLAHMKD 326
Cdd:COG2433 438 EKDERIERLERE----LSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKElwKLEHSGE 509
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
149-511 |
8.84e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ---GD 225
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQsslAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 226 HVARILELEDDIQTM-SDKVLMK------------EVELDRVRDTVKAL--TREQEKLLRQLKE---------------- 274
Cdd:pfam05557 168 AEQRIKELEFEIQSQeQDSEIVKnskselaripelEKELERLREHNKHLneNIENKLLLKEEVEdlkrklereekyreea 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 275 --FQADKEQSEAELQTVR--EENCCLNTELEEAKSRQEEQ--------GAQVQRLKDKLAHMKDTLGQAQQKVA----EL 338
Cdd:pfam05557 248 atLELEKEKLEQELQSWVklAQDTGLNLRSPEDLSRRIEQlqqreivlKEENSSLTSSARQLEKARRELEQELAqylkKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 339 EPLKEQLRGVQELAASSQQKAALLGEE----------------LASAAGARDRTIAELH-------------RSRLEVAE 389
Cdd:pfam05557 328 EDLNKKLKRHKALVRRLQRRVLLLTKErdgyrailesydkeltMSNYSPQLLERIEEAEdmtqkmqahneemEAQLSVAE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 390 VNGRLAELSLHMKEEKCQWSKERTGLL-QSMEAEKDKILKLSAEILRLEktVQEERTQSHVFKTELARE--------KDS 460
Cdd:pfam05557 408 EELGGYKQQAQTLERELQALRQQESLAdPSYSKEEVDSLRRKLETLELE--RQRLREQKNELEMELERRclqgdydpKKT 485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 160017771 461 SLVQLSESKRELtelrsALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVA 511
Cdd:pfam05557 486 KVLHLSMNPAAE-----AYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
325-508 |
1.13e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 KDTLGQAQQKVAELEplkeqlRGVQElaaSSQQKAALLGE----ELASAAGARdrtiaELHRSRLEVAEVNGRLAELSLH 400
Cdd:PRK11637 46 RDQLKSIQQDIAAKE------KSVRQ---QQQQRASLLAQlkkqEEAISQASR-----KLRETQNTLNQLNKQIDELNAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 401 MKEEKCQWSKERTGLLQSMEAE----KDKILKLsaeILRLEKTVQEERTQSHVFKTELAREKdsSLVQLSESKRELTELR 476
Cdd:PRK11637 112 IAKLEQQQAAQERLLAAQLDAAfrqgEHTGLQL---ILSGEESQRGERILAYFGYLNQARQE--TIAELKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|..
gi 160017771 477 SALrvlqkekEQLQTEKQELLEYMRKLEARLE 508
Cdd:PRK11637 187 AEL-------EEKQSQQKTLLYEQQAQQQKLE 211
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
180-526 |
1.21e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 180 RVQELEAALATARQEHSELTEQYKGLSRSHgELSEERDILSQQQGDHVARILELEDDIQtmsdkvLMKEVELDRVRDTVK 259
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEEARKAEDAKKAEAARKAEE------VRKAEELRKAEDARK 1201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 260 ALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKvAELE 339
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEE---AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK-AEEA 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 340 PLKEQLRGVQELAASSQQKAAllgEELASAAGARDRtiAELHRSRLEV---AEVNGRLAELSLHMKEEKcqwskertgll 416
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKA---EEKKKADEAKKK--AEEAKKADEAkkkAEEAKKKADAAKKKAEEA----------- 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 417 qsmeAEKDKILKLSAEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQEl 496
Cdd:PTZ00121 1342 ----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA- 1416
|
330 340 350
....*....|....*....|....*....|
gi 160017771 497 leyMRKLEARLEKVADEKWTEDAATEDEEA 526
Cdd:PTZ00121 1417 ---KKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-289 |
1.43e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKLQLEDQ----------------VTELRSRVQELEAALATARQ----EHS---ELTEQYKGL 205
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQlgsgpdalpellqspvIQQLRAQLAELEAELAELSArytpNHPdviALRAQIAAL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 206 --------SRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKvlmkEVELDRVRDTVKALTREQEKLLRQLKEFQA 277
Cdd:COG3206 304 raqlqqeaQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
170
....*....|..
gi 160017771 278 DKEQSEAELQTV 289
Cdd:COG3206 380 AEALTVGNVRVI 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
240-397 |
1.53e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 240 MSDKVLMKEVELDRVRDTVKALTrEQEKLLRQLKE-FQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLK 318
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELA-DLLSLERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 319 DKLAHMKDTLGQAQQKVAEL----EPLKEQLRGVQEL-------AASSQQKAALLGEELASAAGARdrtIAELHRSRlev 387
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLnqqiAALRRQLAALEAAldasekrDRESQAKIADLGRRLNVALAQR---VQELNRYR--- 196
|
170
....*....|
gi 160017771 388 AEVNGRLAEL 397
Cdd:PRK09039 197 SEFFGRLREI 206
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
150-344 |
1.69e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELseerdilsqQQGDhvAR 229
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLL---------PDAE--EN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 230 ILELEDDIQTMSDKVLMKEVELDRVRdtvKALTREqeklLRQLKEFQADKEqSEAELQtvreencclnteLEEAKSRQEE 309
Cdd:pfam05667 403 IAKLQALVDASAQRLVELAGQWEKHR---VPLIEE----YRALKEAKSNKE-DESQRK------------LEEIKELREK 462
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 160017771 310 qgaqvqrlkdklahMKDTLGQAQQK-------VAELEPLKEQ 344
Cdd:pfam05667 463 --------------IKEVAEEAKQKeelykqlVAEYERLPKD 490
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-497 |
1.85e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 169 QLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVARILELEDDIQTMSDKVLMKE 248
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 249 VELDRVRDTVKA-------LTREQEKLLRQLKEFQA-------DKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQV 314
Cdd:pfam01576 440 SELESVSSLLNEaegknikLSKDVSSLESQLQDTQEllqeetrQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 315 QRLKDKLAHMKDTLgqaQQKVAELEPLKEQLRGVQ-ELAASSQQKaallgEELASAAGARDRTiaelhRSRLEvaevnGR 393
Cdd:pfam01576 520 STLQAQLSDMKKKL---EEDAGTLEALEEGKKRLQrELEALTQQL-----EEKAAAYDKLEKT-----KNRLQ-----QE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 394 LAELSLHMKEEKcqwskertGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVfkteLAREKDSSLVQLSeskRELT 473
Cdd:pfam01576 582 LDDLLVDLDHQR--------QLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEA----EAREKETRALSLA---RALE 646
|
330 340
....*....|....*....|....
gi 160017771 474 ELRSALRVLQKEKEQLQTEKQELL 497
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDLV 670
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-548 |
2.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 245 LMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEaELQTVREENcclnTELEEAKSRQEEQgAQVQRLKDKlahm 324
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEK----KKADEAKKKAEEA-KKADEAKKK---- 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 325 kdtlGQAQQKVAELEPLKEQLRGVQELAASSQQKAAllGEELASAAGARDRTIAELHRSrlevAEVNGRLAELslhmkeE 404
Cdd:PTZ00121 1453 ----AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKA----AEAKKKADEA------K 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 405 KCQWSKERTGLLQSMEAEKDKILKLSAEILRLE--KTVQEERTQSHVFKTELAREkdsslvqlsESKRELTELRSALRVL 482
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAK 1587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 483 QKEKEQLQtEKQELLEYMRKLEA-RLEKVADEKWTEDAATEDEEATAGLSCPASLTDSEDESPEDMR 548
Cdd:PTZ00121 1588 KAEEARIE-EVMKLYEEEKKMKAeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-526 |
2.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 228 ARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNTELEEAKsRQ 307
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE---AKKKAEEAK-KA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 308 EEQGAQVQRLKDKLAHMKDTLGQAQQKvAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV 387
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKA-AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 388 ---AEVNGRLAELSLHMKEEKcqwSKERTGLLQSMEAEKDKILKLSAEILR----LEKTVQEERTQSHVFKTELAREKDS 460
Cdd:PTZ00121 1397 kkkAEEDKKKADELKKAAAAK---KKADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 461 SLVQLSESKRELTELRSALRVLQKEKEQLQTEKQElleymrKLEARLEKVADEKWTEDAATEDEEA 526
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA------KKKADEAKKAEEAKKADEAKKAEEA 1533
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
253-520 |
2.17e-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: 41.49 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 253 RVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQ 332
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 333 QKVAELEPLKEQLRGVQEL--AASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEkcQWSK 410
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETqeRINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ--SSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 411 ERTGLLQSMEAEKDKILKLS-AEILRLEKTVQEERTQSHVFKTELAREKDSSLVQLSESKRE-LTELR-------SALRV 481
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHeVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDiLQREQatidtrtSAFRD 421
|
250 260 270
....*....|....*....|....*....|....*....
gi 160017771 482 LQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWTEDAA 520
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-526 |
2.31e-03 |
|
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: 40.29 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 375 RTIAELHRSRLEVAEVNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERTQSHVFKTEL 454
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELE----DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 455 -----AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWTEDAATEDEEA 526
Cdd:COG1579 83 gnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
150-344 |
2.43e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 150 QNQLDESQQERNDLMQLKLQLEDQVTELrSRVQELEAaLATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDHVAR 229
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEI-SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 230 ILELEDDIQTMSDKVLMKE--VELDRVRDtvKALTREQE-KLLRQLKEFQADK----EQSEAELQTVREEN-CCLNTELE 301
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEEraREMERVRL--EEQERQQQvERLRQQEEERKRKklelEKEKRDRKRAEEQRrKILEKELE 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 160017771 302 EAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQ-KVAELEPLKEQ 344
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERrREAEEERRKQQ 546
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
247-366 |
2.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 247 KEVELDRVRDTVKALTrEQEKllrQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEqgaQVQRLKDKLAHMKD 326
Cdd:pfam02841 185 KEAVEEAILQTDQALT-AKEK---AIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQE---HVKQLIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 160017771 327 TLGQAQQKVAELEpLKEQLRGVQElaaSSQQKAALLGEEL 366
Cdd:pfam02841 258 QLLAEQERMLEHK-LQEQEELLKE---GFKTEAESLQKEI 293
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
420-510 |
3.04e-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: 38.84 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 420 EAEKDKILKLSAEILRLEKTVQEERTQSHvfktELAREKDSSLVQLSESKRELTELRSALR----VLQKEKEQLQTEKQE 495
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLE----DLERELALLQAKERQLEKKLKTLEQKLKnekeELQRLKNALQQIKTQ 130
|
90
....*....|....*
gi 160017771 496 LLEYMRKLEARLEKV 510
Cdd:pfam11559 131 FAHEVKKRDREIEKL 145
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
152-345 |
3.38e-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: 39.70 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGD-HVARI 230
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFAlPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 231 LELEDDIQTMSDkvLMKEVELDRVRDTVKALTREQEKLLRQLKE-FQADKEQSEAELQTVREENCCLNTELEEAKSRQEE 309
Cdd:pfam06008 121 SRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRIQTwFQSPQEENKALANALRDSLAEYEAKLSDLRELLRE 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 160017771 310 QGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQL 345
Cdd:pfam06008 199 AAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQL 234
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
176-399 |
3.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 176 ELRSRVQELEAALATARQEHSELTEQYKGLSR---SHGE---LSEERDILSqqqgdHVARILEledDIQTMSDkvLMKEV 249
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEeeeLEEERRRLS-----NAEKLRE---ALQEALE--ALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 250 E---LDRVRDTVKALtREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNT----------ELEEAKSRQeeqgAQVQR 316
Cdd:COG0497 239 EggaLDLLGQALRAL-ERLAEYDPSLAELAERLESALIELEEAASE---LRRyldslefdpeRLEEVEERL----ALLRR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 317 LKDK----LAHMKDTLGQAQQKVAELEPLKEQLrgvQELaassQQKAALLGEELASAAgardrtiAELHRSRLEVA---- 388
Cdd:COG0497 311 LARKygvtVEELLAYAEELRAELAELENSDERL---EEL----EAELAEAEAELLEAA-------EKLSAARKKAAkkle 376
|
250
....*....|..
gi 160017771 389 -EVNGRLAELSL 399
Cdd:COG0497 377 kAVTAELADLGM 388
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
145-435 |
3.92e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQg 224
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE- 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 225 dhvarilELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCC-LNTELEEA 303
Cdd:pfam02463 802 -------ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKeELLQELLL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 304 KSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160017771 384 RLEVAEVNGRLAELSLHM----------KEEKCQWSKERTGLLQSMEAEKDKILKLSAEILR 435
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELgkvnlmaieeFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
185-528 |
4.36e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 185 EAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGDH--VARILELEDDIQTMSDKVLMKEVELDRVRDTvkalT 262
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlaVAFEADPEAELRQLNRRRVELERALADHESQ----E 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 263 REQEKLLRQLKEFQADKEQSEAELQTVREENccLNTELEEAK---SRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIReqlDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFE 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 340 PLKEQLRGVQELAASSQQKAALLGE----------ELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCqws 409
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQL--- 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 410 kertgllqsmeAEKDKIL-KLSAEILRLEKTVQEertqshvFKTELAR---EKDSSLVQLSESKREltELRSALRVLQKE 485
Cdd:PRK04863 1016 -----------AQYNQVLaSLKSSYDAKRQMLQE-------LKQELQDlgvPADSGAEERARARRD--ELHARLSANRSR 1075
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 160017771 486 KEQLQTEKQELLEYMRKLEARLEKVadekwTEDAATEDEEATA 528
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKL-----ERDYHEMREQVVN 1113
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
280-373 |
4.36e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 280 EQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgVQELAASSQQKA 359
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ-EKAAETSQERKQ 216
|
90
....*....|....
gi 160017771 360 ALlgEELASAAGAR 373
Cdd:PRK11448 217 KR--KEITDQAAKR 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
127-345 |
5.39e-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: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 127 LVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARqehSELTEQYKGLS 206
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG---SDLAAREDALN 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 207 RSHGELSEERD-ILSQQQGDHVARILELEDDIQTMSdkvlmkevELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAE 285
Cdd:TIGR00618 743 QSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGA--------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160017771 286 LQTVREENC-CLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQL 345
Cdd:TIGR00618 815 DEDILNLQCeTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
138-435 |
5.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 138 DILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQ----YKGLSRSHGELS 213
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQErvreHALSIRVLPKEL 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 214 EERDILSQQQGDH----VARILELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQEKLLRQLKEFQAdkeQSEAELQTV 289
Cdd:TIGR00618 675 LASRQLALQKMQSekeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN---QSLKELMHQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 290 REENCClntELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAEL-EPLKEQLRGVQELAASSQQKAALLGEELAS 368
Cdd:TIGR00618 752 ARTVLK---ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDtHLLKTLEAEIGQEIPSDEDILNLQCETLVQ 828
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 369 AAGARDRTIAELHRSRLEVAEVNGRLAElSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILR 435
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEE-CSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALI 894
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
165-400 |
5.56e-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: 39.33 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 165 QLKLQLEDqvTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSeerdilsqqqgdhvarileleddiqtmsdkv 244
Cdd:pfam00529 46 DVLFQLDP--TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELA------------------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 245 lmkeveldrvrdtvkALTREQEKLLRQLKEFQADKEQSEAELQTVREencclntELEEAKSRQEEQGAQVQRLKDKLAHM 324
Cdd:pfam00529 93 ---------------ISRQDYDGATAQLRAAQAAVKAAQAQLAQAQI-------DLARRRVLAPIGGISRESLVTAGALV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160017771 325 KDTLGQAQQKVAELEPLKEQLRGVQElAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV-AEVNGRLAELSLH 400
Cdd:pfam00529 151 AQAQANLLATVAQLDQIYVQITQSAA-ENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIrAPVDGTVAFLSVT 226
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
460-514 |
5.79e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 160017771 460 SSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4026 125 QNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEN 179
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
251-490 |
6.01e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.67 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 251 LDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREEnccLNtELEEAKSRQEEQgAQVQRLKDKLAHM---KDT 327
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQ---LE-ELEAAALQPGEE-EELEEERRRLSNAeklREA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 328 LGQAQQKVAELEP-----LKEQLRGVQELAASSQQKAALLgEELASAAGARDRTIAELHR--SRLEV-----AEVNGRLA 395
Cdd:COG0497 228 LQEALEALSGGEGgaldlLGQALRALERLAEYDPSLAELA-ERLESALIELEEAASELRRylDSLEFdperlEEVEERLA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 396 EL-SLHMK-----EEKCQWskertglLQSMEAEKDKILKLSAEILRLEKTVQEERTQshvfktelarekdsslvqLSESK 469
Cdd:COG0497 307 LLrRLARKygvtvEELLAY-------AEELRAELAELENSDERLEELEAELAEAEAE------------------LLEAA 361
|
250 260
....*....|....*....|...
gi 160017771 470 RELTELRS-ALRVLQKE-KEQLQ 490
Cdd:COG0497 362 EKLSAARKkAAKKLEKAvTAELA 384
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
171-490 |
6.13e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 171 EDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELseeRDILSQ----QQGDHVARILELEDDIqtmsDKVLM 246
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL---NKLLPQanllADETLADRLEELREEL----DAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 247 KEVELDRVRDTVKALTREQEKLLR---QLKEFQADKEQSEAELQTVREENCCLnTEL---------EEAKSRQEEQGAQV 314
Cdd:COG3096 908 AQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFAL-SEVvqrrphfsyEDAVGLLGENSDLN 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 315 QRLKDKLAHM-------KDTLGQAQQKVAE----LEPLKEQLRGVQELAASSQQKAALLG-----EELASAAGARDRTIA 378
Cdd:COG3096 987 EKLRARLEQAeearreaREQLRQAQAQYSQynqvLASLKSSRDAKQQTLQELEQELEELGvqadaEAEERARIRRDELHE 1066
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 379 ELHRSRlevaevnGRLAELslhmkeekcqwskERTglLQSMEAEKDkilKLSAEILRLEKTVQEERTQSHVFKT------ 452
Cdd:COG3096 1067 ELSQNR-------SRRSQL-------------EKQ--LTRCEAEMD---SLQKRLRKAERDYKQEREQVVQAKAgwcavl 1121
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 160017771 453 ELAREKDsslVQLSESKRELT-----ELRS-------ALRVLQKEKEQLQ 490
Cdd:COG3096 1122 RLARDND---VERRLHRRELAylsadELRSmsdkalgALRLAVADNEHLR 1168
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
226-339 |
6.16e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 226 HVARI-LELEDDIQTMSDKVLMKEVELDRVRDTVKALTREQE--KLLRQLKEFQADKEQSEAELQTVREENCCLNTELEE 302
Cdd:COG4026 88 HVERMkLPLGHDVEYVDVELVRKEIKNAIIRAGLKSLQNIPEynELREELLELKEKIDEIAKEKEKLTKENEELESELEE 167
|
90 100 110
....*....|....*....|....*....|....*..
gi 160017771 303 AKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELE 339
Cdd:COG4026 168 LREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-505 |
6.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 145 KATVLQ---NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQ 221
Cdd:PRK01156 330 KLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 222 QQGDHVARILELEDDIQTMSDKVLMKEVELDRVRDTVKAL-----------TREQEKLLRQLKEFQADKEQSEAELQTVR 290
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgtTLGEEKSNHIINHYNEKKSRLEEKIREIE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 291 EENCCLNTELEEAKSRQEE-QGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRGVQELaaSSQQKAALLG------ 363
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI--KNRYKSLKLEdldskr 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 364 EELASAAGARDRTIAELHRSRLEvaEVNGRLAELSLHMKEEKCQWS----------KERTGLLQSMEAEKDKILKLSAEI 433
Cdd:PRK01156 568 TSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPddksyidksiREIENEANNLNNKYNEIQENKILI 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 434 LRLEKTVQEERTQSHVFKTELAREKDSSlVQLSES--------------KRELTELRSALRVLQKEKEQLQ---TEKQEL 496
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEIT-SRINDIednlkksrkalddaKANRARLESTIEILRTRINELSdriNDINET 724
|
....*....
gi 160017771 497 LEYMRKLEA 505
Cdd:PRK01156 725 LESMKKIKK 733
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
250-320 |
6.55e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 6.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160017771 250 ELDRVRDTVKALTREQEKLLRQLKEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDK 320
Cdd:COG4026 136 ELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKK 206
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
146-526 |
7.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 146 ATVLQNQLDESQQERNDLMQLKLQLE---DQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQ 222
Cdd:PRK01156 168 YDKLKDVIDMLRAEISNIDYLEEKLKssnLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 223 QgDHVARileLEDDIQTMSDK---VLMKEVELDRVRDTVKALT-----------REQEKLLRQLKEFQADKEQSEAELQT 288
Cdd:PRK01156 248 E-DMKNR---YESEIKTAESDlsmELEKNNYYKELEERHMKIIndpvyknrnyiNDYFKYKNDIENKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 289 VrEENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQQKVAELEPLKEQLRgvqELAASSQQKAALLGEELAS 368
Cdd:PRK01156 324 Y-HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE---EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 369 AAGARDRTIAELHRSRLEVAEVNGRLAELslhmkeekcqwsKERTGLLQSMEAEkdkiLKLSAEILrlektvqEERTQSH 448
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSL------------NQRIRALRENLDE----LSRNMEML-------NGQSVCP 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160017771 449 VFKTELAREKDSSLVQlsESKRELTELRSALRVLQKEKEQLQTEKQELleymRKLEARLEKVADEKW-TEDAATEDEEA 526
Cdd:PRK01156 457 VCGTTLGEEKSNHIIN--HYNEKKSRLEEKIREIEIEVKDIDEKIVDL----KKRKEYLESEEINKSiNEYNKIESARA 529
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
263-345 |
7.90e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.35 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 263 REQEKLLRQlkEFQADKEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQA-QQKVAELEP- 340
Cdd:pfam07111 512 REQGEAERQ--QLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAlQEKVAEVETr 589
|
....*
gi 160017771 341 LKEQL 345
Cdd:pfam07111 590 LREQL 594
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
149-515 |
8.33e-03 |
|
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: 39.29 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQE-------RNDLMQLKLQLEDQVTELRSRVQELEAALATARQehselteqykglsrshgeLSEERDILsQ 221
Cdd:pfam05622 64 LQKQLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNEELTSLAEEAQA------------------LKDEMDIL-R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 222 QQGDHVARileLEDDIQTMSDKV-----LMKEVELDRVRDTVKAL-TREQEKllrQLKEFQADKEQSEA------ELQTV 289
Cdd:pfam05622 125 ESSDKVKK---LEATVETYKKKLedlgdLRRQVKLLEERNAEYMQrTLQLEE---ELKKANALRGQLETykrqvqELHGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 290 REENCCLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQAQqkvaeleplkEQLRGVQELAASSQQKAALLGEELASA 369
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETN----------EELRCAQLQQAELSQADALLSPSSDPG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 370 agarDRTIAELHRSrlEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSM--EAEK-------------DKILKLSAEIL 434
Cdd:pfam05622 269 ----DNLAAEIMPA--EIREKLIRLQHENKMLRLGQEGSYRERLTELQQLleDANRrkneletqnrlanQRILELQQQVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 435 RLEKTVQEERTQSHVFKTeLAREKDSSLVQLSESKRELTELRSALRVLQ-KEKEQLQTEKQELLEYMRKLEARLeKVADE 513
Cdd:pfam05622 343 ELQKALQEQGSKAEDSSL-LKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKDEDM-KAMEE 420
|
..
gi 160017771 514 KW 515
Cdd:pfam05622 421 RY 422
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
169-524 |
8.46e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 39.54 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 169 QLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgelsEERDILSQQQGdhvARILELEDDIQTMSDKVLMKE 248
Cdd:pfam15818 25 QYEEQIGKIIVETQELKWQKETLQNQKETLAKQHK----------EAMAVFKKQLQ---MKMCALEEEKGKYQLATEIKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 249 VELDRVRDTVKALTREQEKLLRQLKEFQAD-------KEQSEAELQTVREENCCLNTELEEAKSRQEEQGAQVQ---RLK 318
Cdd:pfam15818 92 KEIEGLKETLKALQVSKYSLQKKVSEMEQKlqlhllaKEDHHKQLNEIEKYYATITGQFGLVKENHGKLEQNVQeaiQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 319 DKLAhmkdTLGQAQQkvAELEPLKEQLRGV-QELAASSQQKAALLGEELASAAgARDRTIAELH-RSRLEVaEVNGRLAE 396
Cdd:pfam15818 172 KRLS----ALNKKQE--SEICSLKKELKKVtSDLIKSKVTCQYKMGEENINLT-IKEQKFQELQeRLNMEL-ELNKKINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 397 LSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEIlRLEKTVQEERTQSHVFKTELAREKdsslvqLSESKRELTELR 476
Cdd:pfam15818 244 EITHIQEEK----QDIIISFQHMQQLLQQQTQANTEM-EAELKALKENNQTLERDNELQREK------VKENEEKFLNLQ 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160017771 477 S----ALRVLQKEKEQLQTEKQEL---LEYMRKLEARLEKVADEKWTEDAATEDE 524
Cdd:pfam15818 313 NehekALGTWKKHVEELNGEINEIkneLSSLKETHIKLQEHYNKLCNQKKFEEDK 367
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
149-367 |
8.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQERNDLMQLKlQLEDQVTELRSRVQELEAALATArqeHSELTEQYKGLSRSHGELSEerdilSQQqgdhva 228
Cdd:PRK11281 106 LKDDNDEETRETLSTLSLR-QLESRLAQTLDQLQNAQNDLAEY---NSQLVSLQTQPERAQAALYA-----NSQ------ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 229 RILELEDdiqtmsdkvlmkevELDRVRDTVKALTREQEKLLR-QLKEFQADKEQSEAELQTvreencclNTELEE-AKSR 306
Cdd:PRK11281 171 RLQQIRN--------------LLKGGKVGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEG--------NTQLQDlLQKQ 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160017771 307 QEEQGAQVQRLKDKLAHMKDT-----LGQAQQKVAELEplkeqlrgVQELAASSQQKaALLGEELA 367
Cdd:PRK11281 229 RDYLTARIQRLEHQLQLLQEAinskrLTLSEKTVQEAQ--------SQDEAARIQAN-PLVAQELE 285
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
156-513 |
8.79e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 156 SQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSR-------SHGE--------LSEERDILS 220
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKsllanrfSFGPaldelekqLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 221 Q-----QQGDHV-AR--ILELEDDIQTMSDKV-----LMKEVE------LDRVRDTVKALTRE-----QEKLLRQLKEFQ 276
Cdd:PRK04778 183 QfveltESGDYVeAReiLDQLEEELAALEQIMeeipeLLKELQtelpdqLQELKAGYRELVEEgyhldHLDIEKEIQDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 277 ADKEQSEAELQT-----VREENCCLNTELE--------EAKSRQEEQGAQvQRLKDKLAHMKDtlgQAQQKVAELEPLKE 343
Cdd:PRK04778 263 EQIDENLALLEEldldeAEEKNEEIQERIDqlydilerEVKARKYVEKNS-DTLPDFLEHAKE---QNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 344 QLrgvqELAASSQQKAALLGEELASAagardrtIAELHRSRLEVAEVNGRLAELSLHMKEekcqwskertgLLQSMEAEK 423
Cdd:PRK04778 339 SY----TLNESELESVRQLEKQLESL-------EKQYDEITERIAEQEIAYSELQEELEE-----------ILKQLEEIE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 424 DKILKLSAEILRLEKtvqEERTqshvfktelAREKDSSLVQ-LSESKRELtelrsalrvlqkEKEQLQTEKQELLEYMRK 502
Cdd:PRK04778 397 KEQEKLSEMLQGLRK---DELE---------AREKLERYRNkLHEIKRYL------------EKSNLPGLPEDYLEMFFE 452
|
410
....*....|.
gi 160017771 503 LEARLEKVADE 513
Cdd:PRK04778 453 VSDEIEALAEE 463
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
151-283 |
9.33e-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: 38.94 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 151 NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHS--ELTEQYKGLSRShgELSEERDILSQQQGDHVA 228
Cdd:pfam00529 82 DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLArrRVLAPIGGISRE--SLVTAGALVAQAQANLLA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 160017771 229 RILELeDDIQ---TMSDKVLMKEVELDRVRDTVKALTREQekllrQLKEFQADKEQSE 283
Cdd:pfam00529 160 TVAQL-DQIYvqiTQSAAENQAEVRSELSGAQLQIAEAEA-----ELKLAKLDLERTE 211
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
253-496 |
9.66e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 253 RVRDTVKALTREqeklLRQLKEFQADKEQSEAELQTVREenccLNTELEEAKSRQEEQGAQVQRLKDKLAHMKDTLGQ-A 331
Cdd:PRK10929 72 QVIDNFPKLSAE----LRQQLNNERDEPRSVPPNMSTDA----LEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQlP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 332 QQKVAELEPLKEQLRGVQELAASS----QQKAALLGEELASaagardrtiaelHRSRLEVAEvngrLAELSLHMKEEkcq 407
Cdd:PRK10929 144 QQQTEARRQLNEIERRLQTLGTPNtplaQAQLTALQAESAA------------LKALVDELE----LAQLSANNRQE--- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 408 WSKERTGLLQSMEAEKDKILklsaEILRLEKTVQEER-TQSHVFKTELAREKDSSL----VQLSESKRELTEL--RSALR 480
Cdd:PRK10929 205 LARLRSELAKKRSQQLDAYL----QALRNQLNSQRQReAERALESTELLAEQSGDLpksiVAQFKINRELSQAlnQQAQR 280
|
250
....*....|....*.
gi 160017771 481 VLQKEKEQLQTEKQEL 496
Cdd:PRK10929 281 MDLIASQQRQAASQTL 296
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
149-302 |
9.83e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 38.75 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 149 LQNQLDESQQErndLMQLKLQLEDQVTELRSRVQ--------------ELEAALATARQEHSELTEQYKG-----LSRSH 209
Cdd:pfam00038 122 LEAKIESLKEE---LAFLKKNHEEEVRELQAQVSdtqvnvemdaarklDLTSALAEIRAQYEEIAAKNREeaeewYQSKL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160017771 210 GELSEERDILSQQQGDHVARILELEDDIQTMsdkvlmkEVELDRVRDTVKALTRE----QEKLLRQLKEFQADKEQSEAE 285
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQSL-------EIELQSLKKQKASLERQlaetEERYELQLADYQELISELEAE 271
|
170
....*....|....*..
gi 160017771 286 LQTVREENCCLNTELEE 302
Cdd:pfam00038 272 LQETRQEMARQLREYQE 288
|
|
| |
