|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
112-320 |
4.36e-79 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 253.38 E-value: 4.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 112 IRKGIPHHFRAIVWQLLCSATDMPVKN---QYSELLKMSSPCEKL----IRRDIARTYPEHEFFKGQDSLGQEVLFNVMK 184
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTSAdkdLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 185 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVRLMQEYRLReLFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRS 263
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1583167683 264 QSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQTELM 320
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
152-320 |
9.38e-57 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 192.08 E-value: 9.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 152 KLIRRDIARTYPEHEFFKGQDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVRLMQEYRLRE 230
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 231 LFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIV-FRVGL 309
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 1583167683 310 ALLQVNQTELM 320
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
108-330 |
7.09e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 163.05 E-value: 7.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 108 LKELIRKGIPHHFRAIVWQLLCSATDM--PVKNQYSELLKM-------SSPCEKLIRRDIARTYPEHEFFKGQDSLGQEV 178
Cdd:COG5210 205 LRELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAEN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 179 LFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVRLMQEYRLRELFKPSMAELGLCIYQFEYMLQEQLPDL 257
Cdd:COG5210 285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583167683 258 NTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQTELMQLDMEGMSQY 330
Cdd:COG5210 365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDL 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-707 |
4.74e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIEtlekgqvtRAQEAEenYVIKRELAVVRQQCSSTAEDLQKAQ 437
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELE--------EAQAEE--YELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 438 STIRQLQEQQEnpRLTEDfVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREGE 517
Cdd:COG1196 316 ERLEELEEELA--ELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA--EAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 518 AVASARELKLQLQELSDTWQAHLSRGGRWKEspRKLVLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLL 597
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEE--ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 598 NRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADsmAAVAEMRQRIAELEIQ---REEG 674
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAAleaALAA 546
|
330 340 350
....*....|....*....|....*....|....*
gi 1583167683 675 RIQGQLNHSDSS--QYIRELKDQIEELKTEVRLLK 707
Cdd:COG1196 547 ALQNIVVEDDEVaaAAIEYLKAAKAGRATFLPLDK 581
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-708 |
2.97e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 416 KRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENprltedfvahLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 495
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 496 PDEN-----NVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKL--VLGELQDELMTVRLR 568
Cdd:TIGR02168 746 EERIaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 569 EAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAecKSKEEVMAVRL 648
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 649 READS------------MAAVAEMRQRIAELEIQREEgrIQGQLNhsdsSQYIREL----------KDQIEELKTEVRLL 706
Cdd:TIGR02168 904 RELESkrselrreleelREKLAQLELRLEGLEVRIDN--LQERLS----EEYSLTLeeaealenkiEDDEEEARRRLKRL 977
|
..
gi 1583167683 707 KG 708
Cdd:TIGR02168 978 EN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-707 |
8.49e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 373 KEMEEQIE-IKRLRTEnrlLKQRIETLEKgQVTRAQEAEEnyvIKRELAVVRQQcsSTAEDLQKAQSTIRQLQEQQEnpr 451
Cdd:COG1196 182 EATEENLErLEDILGE---LERQLEPLER-QAEKAERYRE---LKEELKELEAE--LLLLKLRELEAELEELEAELE--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 452 ltedfvaHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVARLQEELKALKVREGEAVASARELKLQLQE 531
Cdd:COG1196 250 -------ELEAELEELEAELAELEAELEELRLELEELELE---------LEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 532 LSDTwqahlsrggrwkesprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKL 611
Cdd:COG1196 314 LEER-------------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 612 QYLAAQNKGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRE 691
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
330
....*....|....*.
gi 1583167683 692 LKDQIEELKTEVRLLK 707
Cdd:COG1196 454 LEEEEEALLELLAELL 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
391-707 |
8.96e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 391 LKQRIETLEKgQVTRAQEAEEnyvIKRELavvrqqcsstaEDLQKAQSTIRqLQEQQENPRLTEDFVAHLETELEQSRLR 470
Cdd:TIGR02168 198 LERQLKSLER-QAEKAERYKE---LKAEL-----------RELELALLVLR-LEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 471 ETETLGALREMQDKVLDMEKRNSSLPDENNvaRLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESP 550
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELY--ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 551 RKL--VLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSES 628
Cdd:TIGR02168 340 AELeeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 629 RRKQAEAECKSKE-EVMAVRLREADSMAAVAEMRQRIAELEiqREEGRIQGQLNhsDSSQYIRELKDQIEELKTEVRLLK 707
Cdd:TIGR02168 420 QQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE--EALEELREELE--EAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
364-702 |
2.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 364 EKEYAAMKSKEMEEQIE-----IKRLRTENRLLKQRIETLEKGQVTRAQEAE-ENYVIKRELAVVRQQCSSTAEDLQKAQ 437
Cdd:TIGR02169 171 KKEKALEELEEVEENIErldliIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 438 STIRQLQEQQENPRLTedfVAHLETELEQSRLR-ETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREG 516
Cdd:TIGR02169 251 EELEKLTEEISELEKR---LEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASL--ERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 517 EAVASARELKLQLQELSDTWQAHLSRGGRWKESprklvLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNL 596
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-----YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 597 LNRVEAERAALQEKLQYLaaqnkglqtqlsESRRKQAEAECKSKEE-VMAVRLREADSMAAVAEMRQRIAELEIQREEGR 675
Cdd:TIGR02169 401 INELKRELDRLQEELQRL------------SEELADLNAAIAGIEAkINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340
....*....|....*....|....*..
gi 1583167683 676 IQgqlnHSDSSQYIRELKDQIEELKTE 702
Cdd:TIGR02169 469 QE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-659 |
3.10e-08 |
|
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: 57.37 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEE----NYVIKRELAVVRQQCSSTAEDL 433
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkeLYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 434 QKAQSTIRQLQEQQEN----PRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELK 509
Cdd:TIGR02168 312 ANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--EEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 510 ALKVREGEAVASARELKLQLQELSDtwqahlsRGGRWKESprklvLGELQDELMTVRLREAQALADGREwrQRVVELETQ 589
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLED-------RRERLQQE-----IEELLKKLEEAELKELQAELEELE--EELEELQEE 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1583167683 590 DNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLS--ESRRKQAEAECKSKEEVMAVRLREADSMAAVAE 659
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-702 |
7.59e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 361 KRLEKEYAAMKSKEMEEQI-------------EIKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQC- 426
Cdd:COG1196 285 EAQAEEYELLAELARLEQDiarleerrreleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAe 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 427 ---SSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE----- 498
Cdd:COG1196 365 ealLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeeeal 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 499 ----NNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLSRgGRWKESPRKLVLGELQDELMTVRLREAQALA 574
Cdd:COG1196 445 eeaaEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 575 -DGREWRQRVVELETQDNIH--RNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmAVRLREA 651
Cdd:COG1196 524 gAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR--GAIGAAV 601
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1583167683 652 DSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKTE 702
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
363-702 |
1.10e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqvTRAQEAEEnyvikrELAVVRQQCSSTAEDLQKAQSTIRQ 442
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE----ERAEELRE------EAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 443 LQEQQENPRLT-----------EDFVAHLETELEQSRLRETETLGALREMQDK-------------------VLDMEKRN 492
Cdd:PRK02224 389 LEEEIEELRERfgdapvdlgnaEDFLEELREERDELREREAELEATLRTARERveeaealleagkcpecgqpVEGSPHVE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 493 SSLPDENNVARLQEELKALKVREG------EAVASARELKLQLQELSDTWQAHLSRggrwkESPRKLVLGELQDELMTVR 566
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIERLEERREDLEEL-----IAERRETIEEKRERAEELR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 567 LREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAqnkgLQTQLSESRRKQAEAEcKSKEEVMAV 646
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIE-RLREKREAL 618
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1583167683 647 RLREADSMAAVAEMRQRIAELEIQREEGRIQG-QLNHSDSSQYIRELKDQIEELKTE 702
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARIEEaREDKERAEEYLEQVEEKLDELREE 675
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-630 |
1.79e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 381 IKRLRTENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHL 460
Cdd:COG4913 612 LAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 461 ETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVARLQEELKALKVREGEAVASARElkLQLQELSDTWQAHL 540
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 541 SRggrwkESPRKLV--LGELQDELMTVRLREAQALADG-----REWRQRVVELETQ-DNIH--RNLLNRVEAER-AALQE 609
Cdd:COG4913 760 GD-----AVERELRenLEERIDALRARLNRAEEELERAmrafnREWPAETADLDADlESLPeyLALLDRLEEDGlPEYEE 834
|
250 260
....*....|....*....|....*.
gi 1583167683 610 KL-QYLAAQNK----GLQTQLSESRR 630
Cdd:COG4913 835 RFkELLNENSIefvaDLLSKLRRAIR 860
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
461-702 |
2.15e-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: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 461 ETELeqsRLRETETlgALREMQDKVLDMEKRNSSLPDENNVAR----LQEELKALKVREgeAVASARELKLQLQELSDTW 536
Cdd:COG1196 176 EAER---KLEATEE--NLERLEDILGELERQLEPLERQAEKAEryreLKEELKELEAEL--LLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 537 QAHLSRGGRWKESPRKL--VLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYL 614
Cdd:COG1196 249 EELEAELEELEAELAELeaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 615 AAQNKGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKD 694
Cdd:COG1196 329 EEELEELEEELEELEEELEEAE-EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
....*...
gi 1583167683 695 QIEELKTE 702
Cdd:COG1196 408 AEEALLER 415
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-641 |
6.58e-07 |
|
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: 52.46 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 426 CSSTAEDLQKAQSTIRQLQEQQENprltedfvahLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQ 505
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 506 EELKALKVREGEAVASARELKLQLQELSDTWQAhLSRGGRWK-----ESPRKLV-LGELQDELMTVRLREAQAL-ADGRE 578
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYR-LGRQPPLAlllspEDFLDAVrRLQYLKYLAPARREQAEELrADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583167683 579 WRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 641
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-699 |
7.97e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTI 440
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 441 RQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEK------------RNSSLPDENNVARLQEEL 508
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAaaieylkaakagRATFLPLDKIRARAALAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 509 KALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKEsprKLVLGELQDELMTVRLREAQALADGREWRQRVVELET 588
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 589 QDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQ-RIAEL 667
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELlEEEEL 747
|
330 340 350
....*....|....*....|....*....|..
gi 1583167683 668 EIQREEGRIQGQLNHSDSSQYIRELKDQIEEL 699
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-707 |
9.92e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtrAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQ 437
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 438 STIRQLQEQQENprlTEDFVAHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREG 516
Cdd:COG4717 156 EELRELEEELEE---LEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 517 EAVASARELKLQlQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQALADGREWrqrvveletqdnihrnl 596
Cdd:COG4717 231 QLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL----------------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 597 LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRI 676
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350
....*....|....*....|....*....|....*.
gi 1583167683 677 QGQLNHSDSS-----QYIRELKDQIEELKTEVRLLK 707
Cdd:COG4717 373 AALLAEAGVEdeeelRAALEQAEEYQELKEELEELE 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-706 |
2.28e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 356 NPKKMKRLEKEYAAMKSKEME---EQIEIKRLRTENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSTAED 432
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 433 LQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKAL 511
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 512 KVREGEAVASARELKL--QLQELSDTWQAH-----------------------------LSRGGRWKESPRKLVLGELQD 560
Cdd:COG4717 226 EEELEQLENELEAAALeeRLKEARLLLLIAaallallglggsllsliltiagvlflvlgLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 561 ELMTVRLREA-------------------------QALADGREWRQRVVELETQDniHRNLLNRVEAERAAL-------- 607
Cdd:COG4717 306 ELQALPALEEleeeeleellaalglppdlspeellELLDRIEELQELLREAEELE--EELQLEELEQEIAALlaeagved 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 608 ----------QEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADsmAAVAEMRQRIAELeiQREEGRIQ 677
Cdd:COG4717 384 eeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEEL--REELAELE 459
|
410 420
....*....|....*....|....*....
gi 1583167683 678 GQLNHSDSSQYIRELKDQIEELKTEVRLL 706
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKAELREL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-635 |
2.44e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 358 KKMKRLEKEYAAMKSkEMEEQIE-IKRLRTENRLLKQRIETLekgQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKA 436
Cdd:TIGR02168 782 AEIEELEAQIEQLKE-ELKALREaLDELRAELTLLNEEAANL---RERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 437 QSTIRQLQEQQEnpRLTEDFVAHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREG 516
Cdd:TIGR02168 858 AAEIEELEELIE--ELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSEL--RRELEELREKLAQLELRLE 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 517 EavasareLKLQLQELSDTwqahlsrggrwkesprklVLGELQDELMTVRLREAQALADGREWRQRVVELETQ-DNIHR- 594
Cdd:TIGR02168 933 G-------LEVRIDNLQER------------------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKiKELGPv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1583167683 595 NLLnrVEAERAALQEKLQYLAAQnkglQTQLSESRRKQAEA 635
Cdd:TIGR02168 988 NLA--AIEEYEELKERYDFLTAQ----KEDLTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
489-704 |
3.36e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 489 EKRNSSLPDENNVARLQEELKAL--KVREGE-AVASARELKLQLQELSDTWQAHLSRGGRwKESPRKLVLGELQDELMTV 565
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELeeKIAELEkALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 566 RLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSE----------------SR 629
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneeaanlrER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 630 RKQAEAECKSKEEVMAVRLREADSMAA-VAEMRQRIAELEIQREEgrIQGQLNH-----SDSSQYIRELKDQIEELKTEV 703
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEdIESLAAEIEELEELIEE--LESELEAllnerASLEEALALLRSELEELSEEL 903
|
.
gi 1583167683 704 R 704
Cdd:TIGR02168 904 R 904
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
351-698 |
4.44e-06 |
|
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: 50.12 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 351 YQVKYNPKKMKRLE------------KEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEK-GQVTRAQEAEenyvIKR 417
Cdd:pfam17380 256 YTVRYNGQTMTENEflnqllhivqhqKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKlEEAEKARQAE----MDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 418 ELAVVRQQcSSTAEDLQKAQSTIRQLQEQQENPRLTEDfvahlETELEQSRLRETETLGALREMQDKvldmekrnsslpd 497
Cdd:pfam17380 332 QAAIYAEQ-ERMAMERERELERIRQEERKRELERIRQE-----EIAMEISRMRELERLQMERQQKNE------------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 498 ennvaRLQEELKAlkvregeavasARELKLQLQElsdtwqahlsRGGRWKESPRKLvlGELQDELMTVRLREAQALADGR 577
Cdd:pfam17380 393 -----RVRQELEA-----------ARKVKILEEE----------RQRKIQQQKVEM--EQIRAEQEEARQREVRRLEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 578 EW---RQRVVELETQDNIHRnlLNRVEAERAalQEKLQYLAAQNKglQTQLSESRRKQAEAECKSKEEVMAVRLR----- 649
Cdd:pfam17380 445 ARemeRVRLEEQERQQQVER--LRQQEEERK--RKKLELEKEKRD--RKRAEEQRRKILEKELEERKQAMIEEERkrkll 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1583167683 650 ----EADSMAAVAEMRQRIAELEIQR-----EEGRIQGQLNHS-------DSSQYIRELKDQIEE 698
Cdd:pfam17380 519 ekemEERQKAIYEEERRREAEEERRKqqemeERRRIQEQMRKAteersrlEAMEREREMMRQIVE 583
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-673 |
4.56e-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: 49.76 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 424 QQCSSTAEDLQKAQSTIRQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKvldmekrnsslpdennVAR 503
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---LKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 504 LQEELKALKVREGEAVASARELKLQLQELSDTWQahlsRGGRwkESPRKLVLGELQDELMTVRLREAQALADGRewRQRV 583
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALY----RLGR--QPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 584 VELETQdnihRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQR 663
Cdd:COG4942 153 EELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|
gi 1583167683 664 IAELEIQREE 673
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
359-698 |
5.96e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQS 438
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP---VDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 439 TI---RQLQEQQENPRLTEDF--VAHLETeLEQSRLRETETLGALREMQDKVLDMEKRNSSLPD----ENNVARLQEELK 509
Cdd:PRK02224 441 RVeeaEALLEAGKCPECGQPVegSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaEDRIERLEERRE 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 510 ALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLvLGELQDELMTVRLREaQALADGREWRQRVVELETQ 589
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-EEEAEEAREEVAELN-SKLAELKERIESLERIRTL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 590 DNIHRNLlnrvEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEE-VMAVRLREADSMAAVAEMRQRIAELE 668
Cdd:PRK02224 598 LAAIADA----EDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELR 673
|
330 340 350
....*....|....*....|....*....|..
gi 1583167683 669 IQREE--GRIQGQLNHSDSSQYIRELKDQIEE 698
Cdd:PRK02224 674 EERDDlqAEIGAVENELEELEELRERREALEN 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-706 |
6.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 386 TENRLLKQRIETLEKGqvtRAQEAEENYVI----KRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQEnpRLTEDFVAHle 461
Cdd:COG4913 578 TRAGQVKGNGTRHEKD---DRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD--ALQERREAL-- 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 462 TELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDennVARLQEELKALKVREGEAVASARELKLQLQELSDTWQahls 541
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAELEAELERLDASSDD---LAALEEQLEELEAELEELEEELDELKGEIGRLEKELE---- 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 542 rggrwkesprklvlgELQDELMTVRLREAQALADGREWR----QRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQ 617
Cdd:COG4913 724 ---------------QAEEELDELQDRLEAAEDLARLELrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 618 nkgLQTQLSESRRKQAEAecksKEEVMAvrlrEADSMAAVAEMRQRIAELEIQREEGRIQGQLN---HSDSSQYIRELKD 694
Cdd:COG4913 789 ---LERAMRAFNREWPAE----TADLDA----DLESLPEYLALLDRLEEDGLPEYEERFKELLNensIEFVADLLSKLRR 857
|
330
....*....|..
gi 1583167683 695 QIEELKTEVRLL 706
Cdd:COG4913 858 AIREIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
500-708 |
7.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 500 NVARLQEELKALKVREGEAVASARELKL--QLQELSDTWQAHLSRGGRWKE--SPRKLVLGELQDELMTVRLREAQALAD 575
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 576 GREwrQRVVELETQDNIHRNLLNRVEAERAALQ-EKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSM 654
Cdd:COG4913 306 RLE--AELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE----ALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1583167683 655 AAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKTEVRLLKG 708
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-707 |
1.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 354 KYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRllkqRIEtlekgQVTRAQEAEENYVIKRELAVVRQQCSSTAEDL 433
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR----KAE-----EARKAEDAKRVEIARKAEDARKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 434 QKAQSTIRQLQ-EQQENPRLTEDFvahleTELEQSRLREtetlgalremqdkvldmekrnsslpdenNVARLQEELKALK 512
Cdd:PTZ00121 1176 KKAEAARKAEEvRKAEELRKAEDA-----RKAEAARKAE----------------------------EERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 513 VREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQALADGREWRqRVVELETQDNI 592
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 593 HRNLLNRVEAERAALQEKLQYLAAQNKglqtQLSESRRKQAEaECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQRE 672
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350
....*....|....*....|....*....|....*
gi 1583167683 673 EGRIQGQLNHSDSSQYIRELKDQIEELKTEVRLLK 707
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
344-702 |
1.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 344 DKLVLKAYQVKYNPKKMKRleKEYAAMKSKEMEEQIEIKRLRTEnrlLKQRIETLEKGQ--VTRAQEAE--ENYVIKREL 419
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADE---AKKKAEEAKKADeaKKKAEEAKkaEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 420 AVVRQQCSSTAEDLQKAQSTIRQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMqdKVLDMEKRNSSLPDEN 499
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAE 1543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 500 NVARLQEELKALKVREGEAVASARELKLQLQELSDTW-QAHLSRGGRWKESPRKLVLGELQDELMTVRLREAQaladgrE 578
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE------E 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 579 WRQRVVELETQDNIHRNL--LNRVEAERAALQEKLQYLAAQNKGLQTQLS----ESRRK-----QAEAECKSKEEVMAvr 647
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeEDKKKaeeakKAEEDEKKAAEALK-- 1695
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1583167683 648 lREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIR---ELKDQIEELKTE 702
Cdd:PTZ00121 1696 -KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeEDKKKAEEAKKD 1752
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
368-672 |
1.43e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 368 AAMKSKEMEEQIEIkrLRTEnRLLKQRIETLEKGQVTRAQEAEENYVIKR---ELAVVRQQCSS------TAEDLQKAQS 438
Cdd:COG3206 76 LSASDSPLETQIEI--LKSR-PVLERVVDKLNLDEDPLGEEASREAAIERlrkNLTVEPVKGSNvieisyTSPDPELAAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 439 TI---------RQLQEQQENPRLTEDFvahLETELEQSR--LRETETlgALREMQDK--VLDMEKRNSSLpdENNVARLQ 505
Cdd:COG3206 153 VAnalaeayleQNLELRREEARKALEF---LEEQLPELRkeLEEAEA--ALEEFRQKngLVDLSEEAKLL--LQQLSELE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 506 EELKALKVREGEAVASARELKLQLQELSDTWQAHLsrggrwkESPrklVLGELQDELMTVRLREAQALADGREWRQRVVE 585
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELL-------QSP---VIQQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 586 LETQ--------DNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckskeevMAVRLREADSMAAV 657
Cdd:COG3206 296 LRAQiaalraqlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVAREL 366
|
330
....*....|....*.
gi 1583167683 658 -AEMRQRIAELEIQRE 672
Cdd:COG3206 367 yESLLQRLEEARLAEA 382
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
363-668 |
1.09e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.08 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 363 LEKEYAAMKS-----KEMEE--------QIEIKRLRTENRLLK------QRIETLEKGQVTRAQEaeeNYVIKRELAVVR 423
Cdd:PLN03188 938 LEEELASLMHehkllKEKYEnhpevlrtKIELKRVQDELEHYRnfydmgEREVLLEEIQDLRSQL---QYYIDSSLPSAR 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 424 QQCS------STAEDLQKAQSTIRQLQE-------QQENPRLTE------DFVAHLETELEQSRlretetlgALREMQDK 484
Cdd:PLN03188 1015 KRNSllkltySCEPSQAPPLNTIPESTDespekklEQERLRWTEaeskwiSLAEELRTELDASR--------ALAEKQKH 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 485 VLDMEKRNSslpdennvarlqEELKalkvregEAVASARELKLQ-LQELSDTWQAHLSRGGRWKEsprklvlgeLQDELM 563
Cdd:PLN03188 1087 ELDTEKRCA------------EELK-------EAMQMAMEGHARmLEQYADLEEKHIQLLARHRR---------IQEGID 1138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 564 TVRLREAQALADGREWRqrvveletqdnihrnLLNRVEAERAAL----QEKLQYLAAQNKGLQTQLsesrRKQAEAECKS 639
Cdd:PLN03188 1139 DVKKAAARAGVRGAESK---------------FINALAAEISALkverEKERRYLRDENKSLQAQL----RDTAEAVQAA 1199
|
330 340
....*....|....*....|....*....
gi 1583167683 640 KEevMAVRLREADSMAAVAEMRQRIAELE 668
Cdd:PLN03188 1200 GE--LLVRLKEAEEALTVAQKRAMDAEQE 1226
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-712 |
1.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 354 KYNPKKMKRLEKEyAAMKSKEMEEQIEIKRL-RTENRLLKQRIETLEKGQVTRAQEAEENYVI-KRELAVVRQQCSSTAE 431
Cdd:pfam02463 166 RLKRKKKEALKKL-IEETENLAELIIDLEELkLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 432 DLQKAQSTI---RQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpDENNVARLQEEL 508
Cdd:pfam02463 245 LLRDEQEEIessKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD-DEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 509 KALKVREGEAVASARELKLQLQELSDTWQAHLSRggRWKESPRKLVLGELQDELMTVRLREAQAL--ADGREWRQRVVEL 586
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLESERLssAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 587 ETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAE 666
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1583167683 667 LEIQREEGRIQGQLNHSDSSQ-YIRELKDQIEELKTEVRLLKGPPTF 712
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAH 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-707 |
1.24e-04 |
|
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: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 362 RLEKEYAAMKSKEMEEQIEIKRLRTENRLLK--------QRIETLEKgQVTRAQEAEENyvIKRELAVVRQQCSS----- 428
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLER-EIERLERELEE--RERRRARLEALLAAlglpl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 429 --TAEDLQKAQSTIRQLQEQqenprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnVARLQE 506
Cdd:COG4913 376 paSAEEFAALRAEAAALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR--LLALRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 507 EL-KALKVREGEA--VAsarELkLQLQELSDTWQ------------------AHLSRGGRWKES---------------- 549
Cdd:COG4913 448 ALaEALGLDEAELpfVG---EL-IEVRPEEERWRgaiervlggfaltllvppEHYAAALRWVNRlhlrgrlvyervrtgl 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 550 -------------PRKLVL------GELQDEL--------------------------MTVRLREAQALADGREWRQRVV 584
Cdd:COG4913 524 pdperprldpdslAGKLDFkphpfrAWLEAELgrrfdyvcvdspeelrrhpraitragQVKGNGTRHEKDDRRRIRSRYV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 585 eLeTQDNIHRnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRK------------------QAEAECKSKEEVMAv 646
Cdd:COG4913 604 -L-GFDNRAK--LAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvaSAEREIAELEAELE- 678
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1583167683 647 RLREADSmaAVAEMRQRIAELEIQREEGRIQ-GQLNHSdssqyIRELKDQIEELKTEVRLLK 707
Cdd:COG4913 679 RLDASSD--DLAALEEQLEELEAELEELEEElDELKGE-----IGRLEKELEQAEEELDELQ 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
374-707 |
1.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 374 EMEEQIEIKrlrtENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAvvrqqcsstAEDLQKAQSTIRQLQEQQENprlt 453
Cdd:PRK02224 191 QLKAQIEEK----EEKDLHERLNGLES-ELAELDEEIERYEEQREQA---------RETRDEADEVLEEHEERREE---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 454 edfVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVARLQEELKALkvrEGEAVASARE-LKLQLQEL 532
Cdd:PRK02224 253 ---LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREeLEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 533 SDTWQAHLSRGGRWKESPRklvlgelqdelmtvRLREAQALADGR--EWRQRVVELETQDNIHRNLLNRVEAERAALQEK 610
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAE--------------SLREDADDLEERaeELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 611 LQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQ--GQ-LNHSDSSQ 687
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCPecGQpVEGSPHVE 468
|
330 340
....*....|....*....|
gi 1583167683 688 YIRELKDQIEELKTEVRLLK 707
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
498-707 |
1.27e-04 |
|
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: 45.82 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 498 ENNVARLQEELKALKvREGEAVASARELKLQLQELsdtwQAHLSrGGRWKESPRKL-----VLGELQDELMTVRLREAQA 572
Cdd:TIGR02168 192 EDILNELERQLKSLE-RQAEKAERYKELKAELREL----ELALL-VLRLEELREELeelqeELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 573 LADGREWRQRVVELETQDNI-------HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAecksKEEVMA 645
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL----AEELAE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1583167683 646 VRLREADSMAAVAEMRQRIAELEIQREEgriqgqlnhsdSSQYIRELKDQIEELKTEVRLLK 707
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEE-----------LESRLEELEEQLETLRSKVAQLE 392
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
344-707 |
2.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 344 DKLVLKAYQVKyNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRllKQRIETLEKG--QVTRAQEAE---ENYVIKRE 418
Cdd:PTZ00121 1332 DAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKaeEKKKADEAKkkaEEDKKKAD 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 419 LAVVRQQCSSTAEDLQKAQSTIRQLQEQQENprlTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE 498
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKK---AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 499 NNVARLQEELKalkvREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTV-RLREAQALADGR 577
Cdd:PTZ00121 1486 DEAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAE 1561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 578 EWRQrvVELETQDNIHRNL-LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEevmavrLREADSMAA 656
Cdd:PTZ00121 1562 EKKK--AEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE------LKKAEEEKK 1633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1583167683 657 VAEMRQRIAELEIQREEgriqgQLNHSDSSQYIR--ELKDQIEELKTEVRLLK 707
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAE-----ELKKAEEENKIKaaEEAKKAEEDKKKAEEAK 1681
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-617 |
2.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 375 MEEQIEIKRLRTENRL--LKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENprl 452
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRK-ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 453 TEDFVAHLETELEQSRLRETETLG--ALREMQDKVLDMEKRNSSL-----PDENNVARLQEELKALKVR-EGEAVASARE 524
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELsarytPNHPDVIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 525 LKLQLQELsdtwqahlsrggrwkesprKLVLGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLNRVEAer 604
Cdd:COG3206 318 LEAELEAL-------------------QAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-- 376
|
250
....*....|...
gi 1583167683 605 AALQEKLQYLAAQ 617
Cdd:COG3206 377 ARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-636 |
2.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 357 PKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqvtraqeaeenyvikRELAVVRQQCSSTAEDLQKA 436
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-----------------RRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 437 QSTIRQLQEQQenprltedfvAHLETELEQSRLRETETLGALREM--QDKVLDMEKRNSSLPDENNVARLQEELKALKVR 514
Cdd:COG4942 82 EAELAELEKEI----------AELRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 515 egeavasARELKLQLQELSdtwqahlsrggrwkesprklvlgELQDELMTVRLREAQALADGREWRQRvveLETQDNIHR 594
Cdd:COG4942 152 -------AEELRADLAELA-----------------------ALRAELEAERAELEALLAELEEERAA---LEALKAERQ 198
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1583167683 595 NLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE 636
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-533 |
3.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 354 KYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTE----NRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSST 429
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEleklEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 430 AEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEK----------RNSSLPDEN 499
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelREEYLELSR 673
|
170 180 190
....*....|....*....|....*....|....
gi 1583167683 500 NVARLQEELKALKVREGEAVASARELKLQLQELS 533
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-702 |
3.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtRAQEAEEnyvIKRELAVVRQQCSSTAEDLQKAQ 437
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEE---LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 438 STIRQLQEQQENprlTEDFVAHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREGE 517
Cdd:PRK03918 266 ERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL--EEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 518 avasARELKLQLQELSDtwqahlsrggrwkespRKLVLGELQDELMTVRLREAQAladgREWRQRVVELETQDNIhrNLL 597
Cdd:PRK03918 340 ----LEELKKKLKELEK----------------RLEELEERHELYEEAKAKKEEL----ERLKKRLTGLTPEKLE--KEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 598 NRVEAERAALQEKLQYLAAQNKGLQTQLSESRR-----KQAEAEC---------KSKEEVMAVRLREadsMAAVAEMRQR 663
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCpvcgrelteEHRKELLEEYTAE---LKRIEKELKE 470
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1583167683 664 IAELE--IQREEGRIQGQLNHSDSSQYIRELKDQIEELKTE 702
Cdd:PRK03918 471 IEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
363-707 |
3.96e-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: 43.96 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtRAQEAEENYvikrelAVVRQQCSSTAEDLQKAQSTIRQ 442
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKA----KASEAEQLR------QNLEKQQSSLAEAEQRIKELEFE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 443 LQEQQENPRLTEDF------VAHLETELEQ-----SRLRET-ETLGALRE--------------MQDKVLDMEKRNSSLP 496
Cdd:pfam05557 179 IQSQEQDSEIVKNSkselarIPELEKELERlrehnKHLNENiENKLLLKEevedlkrklereekYREEAATLELEKEKLE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 497 DE----------------------NNVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHLS-----RGGRWKES 549
Cdd:pfam05557 259 QElqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKkiedlNKKLKRHK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 550 P------RKLVLGELQDELMTVRLR----EAQALADGREWRQRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNK 619
Cdd:pfam05557 339 AlvrrlqRRVLLLTKERDGYRAILEsydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 620 GLQTQLSESRRKQAEAE-CKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDS----------SQY 688
Cdd:pfam05557 419 TLERELQALRQQESLADpSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpaAEA 498
|
410
....*....|....*....
gi 1583167683 689 IRELKDQIEELKTEVRLLK 707
Cdd:pfam05557 499 YQQRKNQLEKLQAEIERLK 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
359-703 |
4.03e-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: 44.19 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLekgQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQS 438
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC---AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 439 TIRQ-----------LQEQQENPRLTEDFVAHLETELEQSRLRETETLGALRemqdkvldmekrnsslpDENNVARLQEE 507
Cdd:TIGR00618 481 IHLQetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR-----------------GEQTYAQLETS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 508 LKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKL--VLGELQDEL-MTVRLREAQALADGREWRQRVV 584
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTeKLSEAEDMLACEQHALLRKLQP 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 585 ELETQDnihrnllnrVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKS-KEEVMAVRLREADsmaavaEMRQR 663
Cdd:TIGR00618 624 EQDLQD---------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlPKELLASRQLALQ------KMQSE 688
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1583167683 664 IAELEIQREEgriqgqLNHSDSSqyIRELKDQIEELKTEV 703
Cdd:TIGR00618 689 KEQLTYWKEM------LAQCQTL--LRELETHIEEYDREF 720
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-532 |
4.10e-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: 42.60 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 380 EIKRLRTENRLLKQRIETLEKgQVTRAQEAEENyvIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAh 459
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-ELAALEARLEA--AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583167683 460 LETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVARLQEELKALKVREGEAVAsarELKLQLQEL 532
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAELDEELA---ELEAELEEL 161
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
362-680 |
7.15e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 362 RLEKEYAAMKSKEMEEQIE----IKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSTAeDLQKAQ 437
Cdd:pfam01576 240 KKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL-DTTAAQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 438 STIRQLQEQQ--ENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKV----LDMEKRNSSLPDENNvaRLQEELKAL 511
Cdd:pfam01576 319 QELRSKREQEvtELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnkANLEKAKQALESENA--ELQAELRTL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 512 KVREGEAVASARELKLQLQELsdtwQAHLSRGGRWKESpRKLVLGELQDELMTVRLREAQALADGREWRQRVVELETQDN 591
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQEL----QARLSESERQRAE-LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 592 IHRNLLN--------------RVEAERAALQEKL-------QYLAAQNKGLQTQLSESRRKQAE--AECKSKEEVMAVRL 648
Cdd:pfam01576 472 DTQELLQeetrqklnlstrlrQLEDERNSLQEQLeeeeeakRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQ 551
|
330 340 350
....*....|....*....|....*....|...
gi 1583167683 649 READsmAAVAEMRQRIAELE-IQREEGRIQGQL 680
Cdd:pfam01576 552 RELE--ALTQQLEEKAAAYDkLEKTKNRLQQEL 582
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
364-700 |
9.78e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 364 EKEYAAMKSKEMEEQI-----EIKRLRTENRLLKQRIETLEKG----------------QVTRAQE-------AEENYVI 415
Cdd:pfam05622 8 EKDELAQRCHELDQQVsllqeEKNSLQQENKKLQERLDQLESGddsgtpggkkylllqkQLEQLQEenfrletARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 416 K-----RELAVVRQQcsstAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRlRETETLGALREmQDKVLdmEK 490
Cdd:pfam05622 88 KceeleKEVLELQHR----NEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYK-KKLEDLGDLRR-QVKLL--EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 491 RNSSLPDENnvARLQEELKalkvREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKL-----VLGELQDELMTV 565
Cdd:pfam05622 160 RNAEYMQRT--LQLEEELK----KANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLeekleALQKEKERLIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 566 R--LREAQ-----ALADGREWRQRVVELETQDNIHRNLlnRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECK 638
Cdd:pfam05622 234 RdtLRETNeelrcAQLQQAELSQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1583167683 639 SKEEVMAVR--LREADSMAavaemRQRIAELEIQREE--GRIQGQLNHS-DSSQYIRELKDQIEELK 700
Cdd:pfam05622 312 LLEDANRRKneLETQNRLA-----NQRILELQQQVEElqKALQEQGSKAeDSSLLKQKLEEHLEKLH 373
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-699 |
1.05e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 382 KRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQ-KAQSTIRQLQEQQEnprLTEDFVAHL 460
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKC---LKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 461 ETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvarlQEELKALKVRE-GEAVASA-RELKLQLQELSdtwqa 538
Cdd:pfam15921 169 NTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYE------HDSMSTMHFRSlGSAISKIlRELDTEISYLK----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 539 hlsrgGRwkesprklvLGELQDELmtvrlreaQALADGREWRQRVVELETQDNIHRnLLNRVEAERAALQEKLQYLAAQN 618
Cdd:pfam15921 238 -----GR---------IFPVEDQL--------EALKSESQNKIELLLQQHQDRIEQ-LISEHEVEITGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 619 KGLQTQL---SESRRKQAE------AECKSKEEVMAVRLREADSMaavaeMRQRIAELEIQREEGRIQGQLNHSDSSQYI 689
Cdd:pfam15921 295 NSIQSQLeiiQEQARNQNSmymrqlSDLESTVSQLRSELREAKRM-----YEDKIEELEKQLVLANSELTEARTERDQFS 369
|
330
....*....|...
gi 1583167683 690 RE---LKDQIEEL 699
Cdd:pfam15921 370 QEsgnLDDQLQKL 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-700 |
1.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLlKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQsti 440
Cdd:PTZ00121 1206 RKAEEERKAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--- 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 441 rQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGAlREMQDKVLDMEKRNSSLPDennvaRLQEELKALKVREGEAVA 520
Cdd:PTZ00121 1282 -ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK-----KAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 521 SARELKLQLQElsdtwqahlSRGGRWKESPRKLVLGELQDELMTVRLREaQALADGREWRQRVVELETQDNIHRnllnRV 600
Cdd:PTZ00121 1355 AADEAEAAEEK---------AEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKK----KA 1420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 601 EAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaECKSKEEVM--AVRLREADSMAAVAEMRQRIAELEIQREEGRiqg 678
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKkkAEEAKKADEAKKKAEEAKKADEAKKKAEEAK--- 1496
|
330 340
....*....|....*....|..
gi 1583167683 679 qlNHSDSSQYIRELKDQIEELK 700
Cdd:PTZ00121 1497 --KKADEAKKAAEAKKKADEAK 1516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
431-698 |
1.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 431 EDLQKAQSTIRQLQEQQEnpRLT---EDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVARLQEE 507
Cdd:COG4913 235 DDLERAHEALEDAREQIE--LLEpirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE---------LEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 508 LKALKVREGEAVASARELKLQLQELSdtwQAHLSRGGRWKEsprklvlgelqdelmtvrlreaqaladgrEWRQRVVELE 587
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELE---AQIRGNGGDRLE-----------------------------QLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 588 TQdnihrnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAEL 667
Cdd:COG4913 352 RE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260 270
....*....|....*....|....*....|...
gi 1583167683 668 --EIQREEGRiqgqlnHSDSSQYIRELKDQIEE 698
Cdd:COG4913 425 eaEIASLERR------KSNIPARLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-706 |
1.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 361 KRLEKEYAAMKSKEMEE-QIEIKRLRTENRLLKQRIETLEKgqvtRAQEAEENYV-IKRELAVVRQQCSSTAEDLQKAQS 438
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQ----ELSDASRKIGeIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 439 TIRQLQEQQENprlTEDFVAHLETELEQSRLretetlgALREMQDKVLDMEKRnsslPDENNVARLQEELKALKVREGEA 518
Cdd:TIGR02169 745 DLSSLEQEIEN---VKSELKELEARIEELEE-------DLHKLEEALNDLEAR----LSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 519 VASARELKLQLQELSDTwqahlsrggrwKESPRKLVlGELQDELMTVRLREAQALADGREWRQRVVELETQDNIHRNLLN 598
Cdd:TIGR02169 811 EARLREIEQKLNRLTLE-----------KEYLEKEI-QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 599 RVEAERAALQEKLqylaaqnKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGriqg 678
Cdd:TIGR02169 879 DLESRLGDLKKER-------DELEAQLRELERKIEELE----AQIEKKRKRLSELKAKLEALEEELSEIEDPKGED---- 943
|
330 340
....*....|....*....|....*...
gi 1583167683 679 qLNHSDSSQYIRELKDQIEELKTEVRLL 706
Cdd:TIGR02169 944 -EEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
347-526 |
2.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 347 VLKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRlrTENRLLKQRIETLEKGQVTRAQEaEENYVIKRELAVVRQQC 426
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 427 SSTAEDLQKAQSTIR----QLQEQQENPRLTEDFVAHLETEL---EQSRLRETETLGALREMQDKVLDMEKRNSSLPDE- 498
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDe 1753
|
170 180 190
....*....|....*....|....*....|...
gi 1583167683 499 ---NNVARL--QEELKALKVREGEAVASARELK 526
Cdd:PTZ00121 1754 eekKKIAHLkkEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
430-674 |
2.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 430 AEDLQKAQSTIRQLQEQQENPRLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvarLQEELK 509
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-----LSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 510 ALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLvLGELQDELMTVRLREAQALADGREWRQRVVELETQ 589
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA-GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 590 dnihRNLLNRVEAERAALQEKLQylaaqnkGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEI 669
Cdd:pfam07888 198 ----RNSLAQRDTQVLQLQDTIT-------TLTQKLTTAHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
....*
gi 1583167683 670 QREEG 674
Cdd:pfam07888 266 QRDRT 270
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
357-521 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 357 PKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgQVTRAQEaeenyvikrelavvRQQCSSTAEDLQKA 436
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-RIKKYEE--------------QLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 437 QSTIRQLQEQQEnprLTEDFVAHLETELEQSRLRETETLGALREMQDKVLDMEKRNsslpdENNVARLQEELKALKVREG 516
Cdd:COG1579 95 QKEIESLKRRIS---DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL-----DEELAELEAELEELEAERE 166
|
....*
gi 1583167683 517 EAVAS 521
Cdd:COG1579 167 ELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
581-706 |
2.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 581 QRVVELETQDNIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSmaAVAEM 660
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP--DVIAL 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1583167683 661 RQRIAELE--IQREEGRIQGQLNHSDSSQYIRE--LKDQIEELKTEVRLL 706
Cdd:COG3206 297 RAQIAALRaqLQQEAQRILASLEAELEALQAREasLQAQLAQLEARLAEL 346
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
569-702 |
4.66e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.39 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 569 EAQALADGREWRQRVvELETQdnihrNLLNRVEAEraalQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSkeevmavRL 648
Cdd:PTZ00491 667 AARHQAELLEQEARG-RLERQ-----KMHDKAKAE----EQRTKLLELQAESAAVESSGQSRAEALAEAEA-------RL 729
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1583167683 649 READSMAAVAEMR---QRI---AELEIQREegRIQGQLNHSDSS-----QYIRELKDqIEELKTE 702
Cdd:PTZ00491 730 IEAEAEVEQAELRakaLRIeaeAELEKLRK--RQELELEYEQAQneleiAKAKELAD-IEATKFE 791
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-496 |
4.76e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 348 LKAYQVKYNPKKMKRLEKEYAA----MKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEEN-YVIKREL--- 419
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERARemerVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrKILEKELeer 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 420 --AVV---------------RQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEDFVAHLEtelEQSRLretETLGALREMQ 482
Cdd:pfam17380 505 kqAMIeeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRL---EAMEREREMM 578
|
170
....*....|....
gi 1583167683 483 DKVLDMEKRNSSLP 496
Cdd:pfam17380 579 RQIVESEKARAEYE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-708 |
4.80e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 469 LRETETLGALREMQDKVLDMEKRNSSLPDEnnVARLQEELKALKVREGEAVASARELKLQLQELSDTWQAHlsrGGRWKE 548
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL---KERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 549 SPRKLvlGELQDELMTVRlREAQALAdgrewrQRVVELETQDNIHRNLLNRVEAERAalQEKLQYLAAQNKGLQTQLSES 628
Cdd:TIGR02169 742 LEEDL--SSLEQEIENVK-SELKELE------ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 629 RRKQAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDssqyIRELKDQIEELKTEVRLLKG 708
Cdd:TIGR02169 811 EARLREIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLES 882
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
416-588 |
5.84e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 416 KRELAVVRQQCSSTAEDLQKAQSTIRQLqeqqenprltEDFVAHLETELEQSRLrETETLGALREMQDKVLDMekrnssL 495
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKL----------ESSIKQVEEELEELKE-QNEELEKQYKVKKKTLDL------L 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 496 PD-ENNVARLQEELKALKVRegeavasarelklqLQELSDTWQAH----------LSRGGRWKESPRKLVLGELQDelMT 564
Cdd:pfam05667 397 PDaEENIAKLQALVDASAQR--------------LVELAGQWEKHrvplieeyraLKEAKSNKEDESQRKLEEIKE--LR 460
|
170 180
....*....|....*....|....*.
gi 1583167683 565 VRLREAQALADGRE--WRQRVVELET 588
Cdd:pfam05667 461 EKIKEVAEEAKQKEelYKQLVAEYER 486
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
391-667 |
6.53e-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: 40.12 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 391 LKQRIETLEKG----QVTRAQEAEENYVIKRELAVVRQQCSSTAEDLQKAQSTIRQLQEQQENPRLTEdfVAHLETELEQ 466
Cdd:pfam07111 167 LTSKAEGLEKSlnslETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPE--VHSQTWELER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 467 SRLreTETLGALREmqdkvldmekrnsslpdenNVARLQEELKALKVRegeaVASARELkLQLQElsdtwqahlsrggrw 546
Cdd:pfam07111 245 QEL--LDTMQHLQE-------------------DRADLQATVELLQVR----VQSLTHM-LALQE--------------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 547 KESPRKLvlgELQDELMTVRLREAQALAdgREWRQRV----VELETQDNIHRNLLNRVEAERAALQEK------------ 610
Cdd:pfam07111 284 EELTRKI---QPSDSLEPEFPKKCRSLL--NRWREKVfalmVQLKAQDLEHRDSVKQLRGQVAELQEQvtsqsqeqailq 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1583167683 611 --LQYLAAQ-------NKGLQTQLS---ESRRKQ----AEAECKSKEEVMAVRLREADSMAAVAEMRQRIAEL 667
Cdd:pfam07111 359 raLQDKAAEvevermsAKGLQMELSraqEARRRQqqqtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARI 431
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
353-703 |
7.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 353 VKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEK---------GQVTRAQEAEENYVI----KREL 419
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleekvKELKELKEKAEEYIKlsefYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 420 AVVRQQCSSTAEDL-QKAQSTIRQLQEQQE-NPRLTEDFVAHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSSLP 496
Cdd:PRK03918 306 LDELREIEKRLSRLeEEINGIEERIKELEEkEERLEELKKKLKELEKRLEELEERhELYEEAKAKKEELERLKKRLTGLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 497 DENNVARLQ----------EELKALKVREGEAVASARELKLQLQELSDTWQAHLSRGGRWKESPRKLVLGELQDELMTVR 566
Cdd:PRK03918 386 PEKLEKELEelekakeeieEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 567 LREAQALADGREWRQRVVELETQDNIHRNLL-------------------NRVEAERAA-----LQEKLQYLAAQNKGLQ 622
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlkeleeklkkyNLEELEKKAeeyekLKEKLIKLKGEIKSLK 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 623 TQLS-----ESRRKQAEAECKSKEEVMAVRLREADSMA--AVAEMRQRIAELEIQREEgriqgQLNHSDSSQYIRELKDQ 695
Cdd:PRK03918 546 KELEkleelKKKLAELEKKLDELEEELAELLKELEELGfeSVEELEERLKELEPFYNE-----YLELKDAEKELEREEKE 620
|
....*...
gi 1583167683 696 IEELKTEV 703
Cdd:PRK03918 621 LKKLEEEL 628
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-650 |
9.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 348 LKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGqVTRAQEAE-ENYVIKREL------- 419
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA-IEELKKAKgKCPVCGRELteehrke 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 420 --AVVRQQCSSTAEDLQKAQSTIRQLQEQQEN--------PRL-----TEDFVAHLETELEQSRLRETE--------TLG 476
Cdd:PRK03918 453 llEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeSELiklkeLAEQLKELEEKLKKYNLEELEkkaeeyekLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 477 ALREMQDKVLDMEKRNSSLPD--------ENNVARLQEELKALKVR-EGEAVASARELKLQLQELSDTWQAHLSRGGRWK 547
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEElkkklaelEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583167683 548 ESPRKL-VLGELQDELMTVRLREAQALADGREWRQRVVELETQ--DNIHRNL----------LNRVEAERAALQEKLQYL 614
Cdd:PRK03918 613 ELEREEkELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELreeylelsreLAGLRAELEELEKRREEI 692
|
330 340 350
....*....|....*....|....*....|....*...
gi 1583167683 615 AAQNKGLQTQLSEsrRKQAEAECKSKEEVMA--VRLRE 650
Cdd:PRK03918 693 KKTLEKLKEELEE--REKAKKELEKLEKALErvEELRE 728
|
|
| |
