|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
160-368 |
2.31e-82 |
|
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: 262.24 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 160 VRKGIPHHFRAIVWQLLCDAQTMP---VKDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDtsaDKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 233 AYSLVDREVGYCQGSAFIVGLLLLQMP-EEEAFCVFFKLMQDYRLReLFKPSMAELGLCMYQFECMIQEYLPELFVHFQS 311
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 312 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
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 ... |
200-368 |
2.53e-54 |
|
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: 185.54 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQ-MPEEEAFCVFFKLMQDYRLRE 278
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 279 LFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 406362838 358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
85-414 |
1.12e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 165.36 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 85 LLAKLEEQNRLIETDSKSLRSVNGS-------RRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVN-EWDDVRKKKEKQV 156
Cdd:COG5210 126 LKDSLPTHLPEASSTEKDFSSFKGSsslnsnpELNKEINELSLKEEPQKLRYYELAADKLWISYLDpNPLSFLPVQLSKL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 157 KELVRKGIPHHFRAIVWQLLcdAQTMPVKDQ----YSELLKM-------TSPCEKLIRRDIARTYPEHNFFKEKDSLGQE 225
Cdd:COG5210 206 RELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 226 VLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQMPEEE-AFCVFFKLMQDYRLRELFKPSMAELGLCMYQFECMIQEYLPE 304
Cdd:COG5210 284 NLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 305 LFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQhfqkVIP 384
Cdd:COG5210 364 LYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLD----LLL 439
|
330 340 350
....*....|....*....|....*....|
gi 406362838 385 HQFDGGPEKLIQSayqvkYNSKKMKKLEKE 414
Cdd:COG5210 440 KQLFLHSGKEAWS-----SILKFRHGTDRD 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-702 |
3.14e-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: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKhkcsstynEDFVLQLEKELVQARLSEAESQCALKEMQ 485
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL--------EVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 486 DKVLDIEKKNnsfpDENNIARLQEELIAVKLREAEAIMGLKELRQQVrdleehwqrhvartsgrwkdppkrnavSELQGE 565
Cdd:TIGR02168 304 KQILRERLAN----LERQLEELEAQLEELESKLDELAEELAELEEKL---------------------------EELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 566 LMSIRLREAETQAEMREMKQRMMEMETQ------------NQINS--NQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSE 631
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQletlrskvaqleLQIASlnNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406362838 632 AKRR--QAEIECKNKEEVMAVrLREADSIAAVAELQQHIAELE--IQKEEGKLQGQLNRSDSKQYIRELKDQIAE 702
Cdd:TIGR02168 433 AELKelQAELEELEEELEELQ-EELERLEEALEELREELEEAEqaLDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
389-703 |
6.11e-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: 63.15 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 389 GGPEKLIQSAYQVKynsKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEK------HKCSSTYNEDFVLQ 462
Cdd:TIGR02168 663 GGSAKTNSSILERR---REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 463 LEKELVQARLSEAESQCALKEMQDKVLDiEKKNNSFP----DENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEH 538
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELE-ERLEEAEEelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 539 WQRHVARTSGRWKD-PPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCS 617
Cdd:TIGR02168 819 AANLRERLESLERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 618 LSLKNKGLLAQLSEAkrRQAEIECKNKEEVMAVRLREADsiAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRE-- 695
Cdd:TIGR02168 899 LSEELRELESKRSEL--RRELEELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRrl 974
|
330
....*....|
gi 406362838 696 --LKDQIAEL 703
Cdd:TIGR02168 975 krLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-711 |
7.66e-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: 56.23 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 405 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKhkcsstynedfvlqlEKELVQARLSEAESQcaLKEM 484
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---------------ELKELEARIEELEED--LHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 485 QDKVLDIEKKnnsfPDENNIARLQEELIAVK---------LREAEAIMGLKEL-RQQVRDLEEHWQRHVARTSGRWKDpp 554
Cdd:TIGR02169 778 EEALNDLEAR----LSHSRIPEIQAELSKLEeevsriearLREIEQKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS-- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 555 KRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKR 634
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 635 RQAEIECKNKE--EVMAVRLREADSIAAVAELQQHIAELE------IQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHE 706
Cdd:TIGR02169 932 ELSEIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
....*
gi 406362838 707 LRCLK 711
Cdd:TIGR02169 1012 YEKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-708 |
1.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 406 KKMKKLEKE------YTTIKTKEMEEQGE-----IKRLRTENRLLKQRIETLEKHKCSSTYNEDfvlQLEKELVQARLSE 474
Cdd:COG1196 200 RQLEPLERQaekaerYRELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELA---ELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 475 AESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSgrwkdpp 554
Cdd:COG1196 277 EELELELEEAQAEEYELLAE---------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 555 krnavsELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKR 634
Cdd:COG1196 341 ------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406362838 635 RQAEIEcknkeevmavrlreadsIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQY--IRELKDQIAELTHELR 708
Cdd:COG1196 415 RLERLE-----------------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEeeEEALLELLAELLEEAA 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
503-714 |
2.55e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 503 NIARLQEELIavKLREAEAIMglKELRQQVRDLE---EHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAET--- 576
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 577 --QAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEiECKNKEEVMAVRLRE 654
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406362838 655 A-----DSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLKGQR 714
Cdd:COG4913 371 LglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
396-702 |
1.02e-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: 52.43 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 396 QSAYQVKYNSKKMKKLEKEytTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHKCSSTYNEDFVLQLEKELVQARLSEA 475
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 476 ESQCALKEMQDKVLDIEKKNNsfpdennIARLQEEliavKLREAEAIMGLKELRQQVRDLEEHWQRHVArtsgrwKDPPK 555
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRE-------LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 556 RNAVSELQGELMSIRLREAETQAEmREMKQ-RMMEMETQNQI-----NSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQL 629
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERA-REMERvRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 630 SEAkRRQAEIECKNKEEVMAVRLREADSiAAVAELQQHIAELE------------IQKEEGKLQGQLNRSDSKQYIRELK 697
Cdd:pfam17380 501 LEE-RKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEErrkqqemeerrrIQEQMRKATEERSRLEAMEREREMM 578
|
....*
gi 406362838 698 DQIAE 702
Cdd:pfam17380 579 RQIVE 583
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-708 |
1.71e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 501 ENNIARLQEEliAVKLREAeaimglKELRQQVRDLE-EHWQRHVARTSGRWKDppKRNAVSELQGELMSIRLREAETQAE 579
Cdd:COG1196 199 ERQLEPLERQ--AEKAERY------RELKEELKELEaELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 580 MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEckNKEEVMAVRLREADSIA 659
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--EELEELEEELEELEEEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 406362838 660 AVAELQQHIAELEIQKEEGKLQGQLNRSDSKQyiRELKDQIAELTHELR 708
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALR 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
392-719 |
1.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 392 EKLIQSAYQVKynsKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHKCSSTYNEDFVLQLEKEL--VQ 469
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKrkLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 470 ARLSEAESQCA-----LKEMQDKVLDIEKKNnsfPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRhva 544
Cdd:PRK03918 259 EKIRELEERIEelkkeIEELEEKVKELKELK---EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 545 rtsgrwkdppkrnaVSELQGELMSIRLREAETQAEMREMKQRMMEMET----QNQINSNQLRRAEQEVTSLQEKVCSLSL 620
Cdd:PRK03918 333 --------------LEEKEERLEELKKKLKELEKRLEELEERHELYEEakakKEELERLKKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 621 KNKGLLAQLSEAKRRQAEIECKNKEEVMAV-RLREADSIAAV--AELQQHiaeleiQKEEGKLQGQLNRSDSKQYIRELK 697
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIeELKKAKGKCPVcgRELTEE------HRKELLEEYTAELKRIEKELKEIE 472
|
330 340
....*....|....*....|..
gi 406362838 698 DQIAELTHELRCLKGQRDFSSR 719
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESE 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
505-714 |
2.21e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 505 ARLQEEliavKLREAEAIMGLKELRQQVRDLEEHwqrhvartsgrwkdppkrnaVSELQGELMSIRLREAETQAEMREMK 584
Cdd:pfam01576 82 SRLEEE----EERSQQLQNEKKKMQQHIQDLEEQ--------------------LDEEEAARQKLQLEKVTTEAKIKKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 585 QRMMEMETQNQINSNQLRRAEQEVTSL-------QEKVCSLS-LKNK--GLLAQLS-----EAKRRQAEIECKNKEEVMA 649
Cdd:pfam01576 138 EDILLLEDQNSKLSKERKLLEERISEFtsnlaeeEEKAKSLSkLKNKheAMISDLEerlkkEEKGRQELEKAKRKLEGES 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406362838 650 VRLREAdsiaaVAELQQHIAELEIQ--KEEGKLQGQLNRSDSKQ--------YIRELKDQIAELTHELRCLKGQR 714
Cdd:pfam01576 218 TDLQEQ-----IAELQAQIAELRAQlaKKEEELQAALARLEEETaqknnalkKIRELEAQISELQEDLESERAAR 287
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
462-640 |
2.47e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVRD 534
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 535 LEEHWQRHVARtsgrwkdppkrnAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQinsnQLRRAEQEVTSLQEk 614
Cdd:COG3206 303 LRAQLQQEAQR------------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEA----ELRRLEREVEVARE- 365
|
170 180
....*....|....*....|....*.
gi 406362838 615 vcslslknkgLLAQLSeAKRRQAEIE 640
Cdd:COG3206 366 ----------LYESLL-QRLEEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-707 |
4.86e-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: 50.44 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwQRHVARTSGRWKDPPKRNAVSELQGELMSIRLRE---AETQ 577
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 578 AEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIecknKEEVMAVRLREADS 657
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 406362838 658 IAAVAELQQHIAELEIQKEEgklqgqlnrsdskqyireLKDQIAELTHEL 707
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEE------------------LSEDIESLAAEI 861
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-705 |
1.01e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 361 QMNQAELMQLDMEGMLQHFQKVIphqfdggpekliqsayqVKYNSKKMKKLEkEYTTIKTKEMEEQGE-----IKRLRTE 435
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSIL-----------------VDFEEASGKKIY-EHDSMSTMHFRSLGSaiskiLRELDTE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 436 NRLLKQRI----ETLEKHKCSSTYNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDENNI----ARL 507
Cdd:pfam15921 233 ISYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIiqeqARN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 508 QEELIAVKLREAEAIMG-----LKELRQQVRDLEEHWQRHV---------ARTSGRWKDPPKRNAVSELQGELMSIRLRE 573
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSqlrseLREAKRMYEDKIEELEKQLvlanselteARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 574 AETQAEmREMKQRMMEMETQNQINSNQLRRA--------------------------EQEVTSLQEKVCSLSlKNKGLLA 627
Cdd:pfam15921 391 KELSLE-KEQNKRLWDRDTGNSITIDHLRRElddrnmevqrleallkamksecqgqmERQMAAIQGKNESLE-KVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 628 QLSEAKrrqaEIECKNKEEVMAVRLREADSIAAVAELQQHIAELE--IQKEEGKLQGQLNRSDSK-QYIRELKDQIAELT 704
Cdd:pfam15921 469 QLESTK----EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLR 544
|
.
gi 406362838 705 H 705
Cdd:pfam15921 545 N 545
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
406-720 |
1.67e-05 |
|
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: 48.81 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRtenRLLKQRIETLEKHKCSstynEDFVLQLEKELVQARLSEAESQcaLKEMQ 485
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQEL---KLKEQAKKALEYYQLK----EKLELEEEYLLYLDYLKLNEER--IDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 486 DKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRwkdpPKRNAVSELQGE 565
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER----RKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 566 LMSIRLREAETQAEMREMKQRMMEMETQnQINSNQLRRAEQEVTSLQEKvcSLSLKNKGLLAQLSEAKRRQAEIECKNKE 645
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKEL-EIKREAEEEEEEELEKLQEK--LEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 406362838 646 -EVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQ---YIRELKDQIAELTHELRCLKGQRDFSSRP 720
Cdd:pfam02463 397 lELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
408-680 |
2.41e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 408 MKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHkcsstynEDFVLQLEKELVQARLSEAESQcaLKEMQDK 487
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL-------LPRLNLLADETLADRVEEIREQ--LDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 488 VLDIEKKNNSFPD-ENNIARLQ---EELIAVKLREAEAIMGLKELRQQVRDLEEHWQRhvaRTSGRWKDPPKR-NAVSEL 562
Cdd:PRK04863 910 KRFVQQHGNALAQlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMlAKNSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 563 QgELMSIRLREAEtqAEMREMKQRMmemeTQNQinsNQLRRAEQEVTSLQEkvcSLSLKNKgllaQLSEAKRR------- 635
Cdd:PRK04863 987 N-EKLRQRLEQAE--QERTRAREQL----RQAQ---AQLAQYNQVLASLKS---SYDAKRQ----MLQELKQElqdlgvp 1049
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 406362838 636 ---QAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKL 680
Cdd:PRK04863 1050 adsGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
404-673 |
4.03e-05 |
|
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: 47.37 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 404 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKH--KCSSTYN------EDFVLQLEKELVQARLSEA 475
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERlaKLEAEIDkllaeiEELEREIEEERKRRDKLTE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 476 ESQCALKEMQDKVLDIEKKNNSFpdenniARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRhvartsgrwkdppK 555
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEF------AETRDELKDYREKLEKLKREINELKRELDRLQEELQR-------------L 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 556 RNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRR 635
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 406362838 636 QAEIECKNKEEVMAVRLREADS---IAAVAEL----QQHIAELEI 673
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIqgvHGTVAQLgsvgERYATAIEV 543
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-702 |
4.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 392 EKLIQSAYQVKYNSKKMKKLEKEYttiKTKEMEEQGEIKRlRTENrlLKQRIEtlEKHKCSstynedfvlQLEKELVQAR 471
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAK-KAEE--AKKKAE--EAKKAD---------EAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 472 LSEaESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELR--QQVRDLEEHWQRHVARTSGR 549
Cdd:PTZ00121 1484 KAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 550 WKDPPKRNAVSELQGelMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQL 629
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKN--MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 630 SEAKRRQAEIECKNKEEVMAVRlreADSIAAVAELQQHIAElEIQKEE---GKLQGQLNR-SDSKQYIRELKDQIAE 702
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAE-EAKKAEedeKKAAEALKKeAEEAKKAEELKKKEAE 1713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-716 |
4.36e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 506 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 585
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 586 RMMEMETQNQINSNQLRRAEQ-------EVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNK---EEVMAVRLREA 655
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESkldelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 406362838 656 DSIAAVAELQQHIAELEIQKEEGKL--------QGQLNRSDSKQYIRELKDQIAELTHELRCLKGQRDF 716
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-677 |
4.78e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQR 541
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 542 HVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAE-MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSL 620
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 621 KNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEE 677
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-704 |
9.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 504 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKD---PPKRNAVSELQGELMSIRL--------- 571
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDAssddlaale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 572 -REAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEckNKEEVMAV 650
Cdd:COG4913 692 eQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD--AVERELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 406362838 651 RLREadsiaavaelQQHIAELEIQKEEGKLQGQLNrsdskQYIRELKDQIAELT 704
Cdd:COG4913 770 NLEE----------RIDALRARLNRAEEELERAMR-----AFNREWPAETADLD 808
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
359-707 |
1.49e-04 |
|
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: 45.27 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 359 LLQMNQAELMQLDMEGMLQHFQKVIphqfdggpeKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQgeIKRLRTENRL 438
Cdd:pfam07888 23 LLVVPRAELLQNRLEECLQERAELL---------QAQEAANRQREKEKERYKRDREQWERQRRELESR--VAELKEELRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 439 LKQRIETLE-KHKCSSTYNEDF-----VLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKknnsfpdenniarlqeELI 512
Cdd:pfam07888 92 SREKHEELEeKYKELSASSEELseekdALLAQRAAHEARIRELEED--IKTLTQRVLERET----------------ELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 513 AVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTsgrwkdppkRNAVSELQGELMSIRLREAETQaEMREMKQRMMEMET 592
Cdd:pfam07888 154 RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL---------RSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 593 QNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAkrrqAEIECKNKEEVMAVRLReadsiaaVAELQQHIAELE 672
Cdd:pfam07888 224 TAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM----AAQRDRTQAELHQARLQ-------AAQLTLQLADAS 292
|
330 340 350
....*....|....*....|....*....|....*
gi 406362838 673 IQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHEL 707
Cdd:pfam07888 293 LALREGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
525-708 |
1.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 525 LKELRQQVRDLEEHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQrmmemETQNQINSNQLRRA 604
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----------LQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 605 EQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEevmAVRLREADSIAAVAELQQHIAELE-IQKEEGKLQGQ 683
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELEEE 214
|
170 180
....*....|....*....|....*
gi 406362838 684 LNRsdSKQYIRELKDQIAELTHELR 708
Cdd:COG4717 215 LEE--AQEELEELEEELEQLENELE 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
504-715 |
1.58e-04 |
|
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: 45.44 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 504 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgrwkdppKRNAVSELQGelMSIRLREAETQAEMREM 583
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRR-----------------EREKAERYQA--LLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 584 KqrmmEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRqaeIECKNKEEVMAVRLREADSIAAVAE 663
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 406362838 664 LQQHIAELEIQKEEgkLQGQLNRSDSKqyIRELKDQIAELTHELRCLKGQRD 715
Cdd:TIGR02169 306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRRD 353
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
462-699 |
2.25e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.47 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSfpdeNNIARLQEE--------LIAVKLREAEAIMGLKELRQQVR 533
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQG----NVLERRQRDaenrsqgnVLERRQRDAENRSQGNVLERRQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 534 DLEEHWQRHVA---------RTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRA 604
Cdd:pfam08017 101 DAENRSQGNVLerrqrdaenKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 605 EQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD--SIAAVAELQQHIAE-------LEIQK 675
Cdd:pfam08017 181 DAENKS-QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnrSQGNVLERRQRDAEnksqgnvLERRQ 259
|
250 260
....*....|....*....|....
gi 406362838 676 EEGKLQGQLNRSDSKQYIRELKDQ 699
Cdd:pfam08017 260 RDAENRSQGNVLERRQRDAENRSQ 283
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-711 |
2.59e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 392 EKLIQSAYQVKYNSKKMKKLEKEYTTIKT-----KEMEEQGEIKRLRTENRLLKQRIETLEKH-----KCSSTYNEDfVL 461
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnKIISQLNEQ-IS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQQVRDLE 536
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 537 EHWQR---HVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEmrEMKQRMMEMETQNQINSNQLRRAEQEVTSLQE 613
Cdd:TIGR04523 426 KEIERlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK--VLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 614 KVCSLSLKNKGLLAQLSEAKRRQAEIECKNKeevmavrlreadsiaavaELQQHIAELEiqKEEGKLQGQLNRSDSKQYI 693
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKK------------------EKESKISDLE--DELNKDDFELKKENLEKEI 563
|
330
....*....|....*...
gi 406362838 694 RELKDQIAELTHELRCLK 711
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLK 581
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
506-683 |
3.83e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 43.70 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 506 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvaRTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 585
Cdd:pfam08017 137 RSQGNVLERRQRDAENRSQGNVLERRQRDAEN-------RSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLER 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 586 RMMEMETQNQINSNQLRRAEQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQ 665
Cdd:pfam08017 210 RQRDAENRSQGNVLERRQRDAENRS-QGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLE 288
|
170
....*....|....*...
gi 406362838 666 QHIAELEIQKEEGKLQGQ 683
Cdd:pfam08017 289 RRQRDAENKSQVGQLIGK 306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
404-715 |
4.40e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 404 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTE-------NRLLKQRIETLEKHKcsSTYNEDfVLQLEKELVQARLSEAE 476
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkYNDLKKQKEELENEL--NLLEKE-KLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 477 SQCAL----------KEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKL---REAEAIMGLKELRQQVRDLEEHWQRHV 543
Cdd:TIGR04523 199 LELLLsnlkkkiqknKSLESQISELKKQNNQL--KDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 544 ARTSGRWKDppKRNAVSELQGELMSirLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSL----- 618
Cdd:TIGR04523 277 EQNNKKIKE--LEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkelt 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 619 ------SLKNKGLLAQLSEAKRRQAEIECKNKE--------EVMAVRLREADSIAavAELQQHIAELEIQKEEGKLQGQL 684
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIEKLKKENQSYKQEiknlesqiNDLESKIQNQEKLN--QQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350
....*....|....*....|....*....|....
gi 406362838 685 ---NRSDSKQYIRELKDQIAELTHELRCLKGQRD 715
Cdd:TIGR04523 431 lkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
469-703 |
4.55e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 43.31 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 469 QARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIA--RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVA-- 544
Cdd:pfam08017 66 RQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAenRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLer 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 545 -------RTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSlQEKVCS 617
Cdd:pfam08017 146 rqrdaenRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRS-QGNVLE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 618 LSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAavaelQQHIAELEIQKEEGKLQGqlNRSDSKQYIRELK 697
Cdd:pfam08017 225 RRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRS-----QGNVLERRQRDAENRSQG--NVLERRQRDAENK 297
|
....*.
gi 406362838 698 DQIAEL 703
Cdd:pfam08017 298 SQVGQL 303
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
411-715 |
5.06e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 411 LEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHkcsSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLD 490
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER---AEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 491 IEKKNNSFPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGR-WKDPPKRNAVSELQG 564
Cdd:PRK02224 396 LRERFGDAPVdlgnaEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQpVEGSPHVETIEEDRE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 565 ELMSIRLREAETQAEMREMKQRMMEMEtqnqinsnQLRRAEQEVTSLQEKVCSLSlknkGLLAQ---LSEAKRRQAEIEC 641
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLE----ELIAErreTIEEKRERAEELR 543
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406362838 642 KNKEEVMAvRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLKGQRD 715
Cdd:PRK02224 544 ERAAELEA-EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE 616
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
439-682 |
8.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 439 LKQRIETLEKHKCSSTynedfvlqlEKELVQARLSEAESQCALKEMQDKVLD-IEKKNNSFPDE-----NNIARLQEELI 512
Cdd:PRK11281 41 VQAQLDALNKQKLLEA---------EDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKlrqaqAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 513 AVkLREAEAIMGLKELRQ---QVRDLEEHWQrhvartsgrwkdppkrNAVSELQGELMSIRLREAETQAEMREMKQRMME 589
Cdd:PRK11281 112 EE-TRETLSTLSLRQLESrlaQTLDQLQNAQ----------------NDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 590 METQ---NQINSNQLR-------RAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKR-----RQAEIEcknkEEVMAvrLRE 654
Cdd:PRK11281 175 IRNLlkgGKVGGKALRpsqrvllQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRdyltaRIQRLE----HQLQL--LQE 248
|
250 260
....*....|....*....|....*...
gi 406362838 655 ADSIAAVAELQQHIAELEIQKEEGKLQG 682
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQA 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-623 |
8.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 408 MKKLEKEYTTIKTKemeeQGEIKRLR-TENRLLKQRIETLEKHKcsSTYNEdfvLQLEKELVQARLSEAESQcaLKEMQD 486
Cdd:COG4717 48 LERLEKEADELFKP----QGRKPELNlKELKELEEELKEAEEKE--EEYAE---LQEELEELEEELEELEAE--LEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 487 KVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhWQRHVARTsgrwkdppKRNAVSELQGEL 566
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE-LEAELAEL--------QEELEELLEQLS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 567 MSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNK 623
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-708 |
9.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHK-CSSTYNEDFVLQLEKELVQARLSEAESQcaLKEM 484
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEER--LEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 485 QDKVLDIEKKnnsfpdENNIARLQEELiaVKLREAEAIMGLKELRQQVRDLEEHWQRhvartsgrwkdppkrnaVSELQG 564
Cdd:COG4717 159 RELEEELEEL------EAELAELQEEL--EELLEQLSLATEEELQDLAEELEELQQR-----------------LAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 565 ELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQ-----------LRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAK 633
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406362838 634 RRQAEIECKNKEEvmaVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQyIRELKDQIAELTHELR 708
Cdd:COG4717 294 AREKASLGKEAEE---LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREAEELEEELQ 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-710 |
1.48e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgrwkdppkRNAVSELQGELMSIRLREAETQAEM 580
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------EQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 581 REMKQRMMEMETQNQINSNQlrraEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIA- 659
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 660 ---AVAELQQHIAELEIQKEE-GKLQGQLNR--SDSKQYIRELKDQIAELTHELRCL 710
Cdd:COG4942 176 leaLLAELEEERAALEALKAErQKLLARLEKelAELAAELAELQQEAEELEALIARL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
462-719 |
1.98e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 532
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 533 RDLEEHWQRHVARTSGRWKdpPKRNAVSELQGELMsiRLREAETQAEMREMKQRMMEMETQNQInSNQLRRAEQEVTSLQ 612
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELS--AADAAVAKDRSELE--ALEDQHGAFLDADIETAAADQEQLPSW-QSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 613 EKVCSLSLKNKGLLAQLSEakRRQAEIEcKNKEEVMAVRlREADSIAAVAE--LQQHIAELEIQKEEGKLQGQLNRSDSK 690
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKE--QNNRDIA-GIKDKLAKIR-EARDRQLAVAEddLQALESELREQLEAGKLEFNEEEYRLK 443
|
250 260
....*....|....*....|....*....
gi 406362838 691 QYIRELKDQIAELTHELRCLKGQRDFSSR 719
Cdd:pfam12128 444 SRLGELKLRLNQATATPELLLQLENFDER 472
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
406-708 |
2.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHKCSS-TYNE--DFVLQLEKEL--VQARLSEAESQca 480
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeEYIKlsEFYEEYLDELreIEKRLSRLEEE-- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 481 LKEMQDKVLDIEKKnnsfpdENNIARLQEELIAVKlREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDppkrnavs 560
Cdd:PRK03918 323 INGIEERIKELEEK------EERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE-------- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 561 ELQGELMSIRLREAETQAEMREMKQRMMEMETQnqinSNQLRRAEQEVTSLQEK--VC----------------SLSLKN 622
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKcpVCgrelteehrkelleeyTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 623 -----KGLLAQLSEAKRRQAEIECKNKEEVMAVRLRE-ADSIAAVAE---------LQQHIAELEIQKEE-GKLQGQLNR 686
Cdd:PRK03918 464 iekelKEIEEKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEklkkynleeLEKKAEEYEKLKEKlIKLKGEIKS 543
|
330 340 350
....*....|....*....|....*....|....*..
gi 406362838 687 SDS---------------KQYIRELKDQIAELTHELR 708
Cdd:PRK03918 544 LKKelekleelkkklaelEKKLDELEEELAELLKELE 580
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
410-715 |
2.43e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 410 KLEKEYTTI--KTKEMEEQGEIK-RLRTENRLLKQRIETLEKHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQD 486
Cdd:pfam15921 445 QMERQMAAIqgKNESLEKVSSLTaQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 487 KV-LDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvARTSG--RWKDPPKRNAVSELQ 563
Cdd:pfam15921 525 RVdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH-GRTAGamQVEKAQLEKEINDRR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 564 GELMSIRLREAETQAEMREMKQRM--MEMETQNQINSNQLR-RAEQEVTSLQEKVCSLSLKNKGLLAQLSEA----KR-- 634
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVsdLELEKVKLVNAGSERlRAVKDIKQERDQLLNEVKTSRNELNSLSEDyevlKRnf 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 635 RQAEIECKNKEEVMAVRLREADSiaavaELQQHIAELE---------------IQKEEGKLQGQLNRSDSK-QYIRE--- 695
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQS-----ELEQTRNTLKsmegsdghamkvamgMQKQITAKRGQIDALQSKiQFLEEamt 758
|
330 340
....*....|....*....|....*...
gi 406362838 696 --------LKDQIAELTHELRCLKGQRD 715
Cdd:pfam15921 759 nankekhfLKEEKNKLSQELSTVATEKN 786
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
456-494 |
2.87e-03 |
|
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial proteins of unknown function.
Pssm-ID: 429008 Cd Length: 200 Bit Score: 39.95 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|....*....
gi 406362838 456 NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKK 494
Cdd:pfam06570 6 NQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQKK 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
508-703 |
3.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 508 QEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNAVSELQGELmsiRLREAETQAEMREMKQRM 587
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL---AGRLREVTLEGEGGSAGG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 588 MEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIE---CKNKEEVMAVRLREADSIAAVAEL 664
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEeerLEEELEEEALEEQLEAEREELLEE 740
|
170 180 190
....*....|....*....|....*....|....*....
gi 406362838 665 QQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAEL 703
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
445-715 |
3.33e-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: 40.65 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 445 TLEKHKCSSTYNEDFVLQLEK-ELVQARLSEaeSQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLRE--AEA 521
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRaELLQNRLEE--CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESrvAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 522 IMGLKELRQQVRDLEEHwQRHVARTSGRWKDppKRNAVS-----------ELQGELMSIRLREAETQAEMREMKQRMMEM 590
Cdd:pfam07888 86 KEELRQSREKHEELEEK-YKELSASSEELSE--EKDALLaqraahearirELEEDIKTLTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 591 etqnqinSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEiecknkEEVMAVRLREADSIAA--VAELQQHI 668
Cdd:pfam07888 163 -------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQ------RDTQVLQLQDTITTLTqkLTTAHRKE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 406362838 669 AELEIQKEEGK-LQGQLNRSDSKqyirelkdqIAELTHELRCLKGQRD 715
Cdd:pfam07888 230 AENEALLEELRsLQERLNASERK---------VEGLGEELSSMAAQRD 268
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
556-713 |
3.36e-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: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 556 RNAVSELQGELMSIRLREAETQAEMREMKQR--MMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAK 633
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 634 RRQAEIecKNKEEVMAVRLREADSIAAVAELQQH-------IAEL--EIQKEEGKLQGQLNR--SDSKQYIRELKDQIAE 702
Cdd:COG3206 254 DALPEL--LQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALraQIAALRAQLQQEAQRilASLEAELEALQAREAS 331
|
170
....*....|.
gi 406362838 703 LTHELRCLKGQ 713
Cdd:COG3206 332 LQAQLAQLEAR 342
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
463-672 |
4.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 463 LEKEL--VQARLSEAESqcALKEMQDK--VLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDleeh 538
Cdd:COG3206 180 LEEQLpeLRKELEEAEA--ALEEFRQKngLVDLSEEAKLL--LQQLSELESQLAEARAELAEAEARLAALRAQLGS---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 539 wqrhvartsgrwkdppKRNAVSELQG--ELMSIRLREAETQAEMREMKQRMMEmetqnqiNSNQLRRAEQEVTSLQEKVC 616
Cdd:COG3206 252 ----------------GPDALPELLQspVIQQLRAQLAELEAELAELSARYTP-------NHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 406362838 617 SLSLKNK-GLLAQLSEAKRRQAEIEcknkEEVMAVRLReadsIAAVAELQQHIAELE 672
Cdd:COG3206 309 QEAQRILaSLEAELEALQAREASLQ----AQLAQLEAR----LAELPELEAELRRLE 357
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-713 |
4.94e-03 |
|
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: 40.43 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 575 ETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkEEVMAVRLRE 654
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERI 749
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406362838 655 ADSIAAVAELQQHIAEL--EIQKEEGKLQGQL-NRSDSKQYIRELKDQIAELTHELRCLKGQ 713
Cdd:TIGR02168 750 AQLSKELTELEAEIEELeeRLEEAEEELAEAEaEIEELEAQIEQLKEELKALREALDELRAE 811
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-640 |
5.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 405 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRT----ENRLLKQRiETLekhkcsstyneDFVLQLEKELVQARLSEAESQCA 480
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKvlkkESELIKLK-ELA-----------EQLKELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 481 -LKEMQDKVLDIEKKNNSFPDE-NNIARLQEELIAV--KLREAEAimGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKR 556
Cdd:PRK03918 526 eYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELekKLDELEE--ELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 557 -----NAVSELQGELMSIRLREAE---TQAEMREMKQRMMEMEtqNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQ 628
Cdd:PRK03918 604 ylelkDAEKELEREEKELKKLEEEldkAFEELAETEKRLEELR--KELEELEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
250
....*....|..
gi 406362838 629 LSEAKRRQAEIE 640
Cdd:PRK03918 682 LEELEKRREEIK 693
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
402-667 |
6.23e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 402 KYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIEtLEKHKcsstyneDFVLQLEKELVQARLSEAESQcAL 481
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA-VEQKK-------EECSKLENQLKKAHNAEEAVR-TN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 482 KEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKElrQQVRDLEEHWQRHVARTS-------------- 547
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQMKEQNkkvanikhgqqemk 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 548 ----------GRWKDPPKRNAVSELQGELMSIRLReaeTQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVcs 617
Cdd:pfam10174 632 kkgaqlleeaRRREDNLADNSQQLQLEELMGALEK---TRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEI-- 706
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 406362838 618 LSLKNKGLLAQLSEAKRRQAEIEC------KNKEEVMAVRlREADSIaaVAELQQH 667
Cdd:pfam10174 707 LEMKQEALLAAISEKDANIALLELssskkkKTQEEVMALK-REKDRL--VHQLKQQ 759
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-637 |
6.93e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 391 PEKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHkcsstynedfVLQLEKELVQA 470
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------LAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 471 RLSEAESQCALKEMQD---KVLDIEKKNNSFP---------DENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEh 538
Cdd:COG4942 89 EKEIAELRAELEAQKEelaELLRALYRLGRQPplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 539 wqrhvartsgrwkdppkrnavsELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSL 618
Cdd:COG4942 168 ----------------------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*....
gi 406362838 619 SLKNKGLLAQLSEAKRRQA 637
Cdd:COG4942 226 EALIARLEAEAAAAAERTP 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
505-672 |
8.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 505 ARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRwkdppkRNAVSELQGELMSIRLREAETQAEMREMK 584
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG------SLTGGSRRELLAALLEAEAELEELAERLA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406362838 585 QRMMEMETQNQINSNQLRRAEQEVTSLQEkvcsLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAEL 664
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLE----EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
....*...
gi 406362838 665 QQHIAELE 672
Cdd:COG1196 766 ERELERLE 773
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