|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1133-1210 |
1.25e-30 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 115.77 E-value: 1.25e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 1133 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1210
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
950-1018 |
8.36e-28 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 107.68 E-value: 8.36e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 950 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1018
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
558-634 |
2.13e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 103.83 E-value: 2.13e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 558 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 634
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1256-1312 |
1.63e-15 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 72.15 E-value: 1.63e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 1256 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1312
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-411 |
3.46e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 182
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 183 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 252
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 253 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 329
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 330 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 409
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
..
gi 321400107 410 LR 411
Cdd:TIGR02168 977 LE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-363 |
8.62e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQD---ESEQSRKRLIEQSRE-----FKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEaa 88
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDilnELERQLKSLERQAEKaerykELKAELRELELALLVLrLEELREELEELQEELKEAE-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 89 flnvykRLIDvpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTL 164
Cdd:TIGR02168 253 ------EELE--------ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 165 KNQAETIALEKEQK--LQNDFAEKERKLQETQMSTTS---KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD- 238
Cdd:TIGR02168 319 EELEAQLEELESKLdeLAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASl 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 239 --EIEMIMTDLERANQRAEVAQREAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIA 311
Cdd:TIGR02168 399 nnEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEalEELREELEEAEQALD 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 312 QLVEDVQRLQASLTKLR------ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 363
Cdd:TIGR02168 479 AAERELAQLQARLDSLErlqenlEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1256-1313 |
9.94e-13 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 64.19 E-value: 9.94e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 1256 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1313
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-369 |
1.34e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsrefkkntpedlrkqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLi 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA-------------------------ELEELEAELEELEAELAELEAEL- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 98 dvpdpvpaldlgQQLQLKVQRLhdieteNQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG1196 270 ------------EELRLELEEL------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 178 klQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEVA 257
Cdd:COG1196 332 --LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 258 QREAETLREQLSSANHSLQLASQIQkapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 337
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350
....*....|....*....|....*....|..
gi 321400107 338 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKEL 369
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-408 |
1.73e-12 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 71.91 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 82 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 157 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 236 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 291
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 292 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 367
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 321400107 368 ELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENA 408
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-429 |
3.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 111 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 190
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 191 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 271 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---ASLTKLRENSASQISQLEQQLSAKNS 347
Cdd:COG1196 363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEeaeEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 348 TLKQLEEKLKgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD---LSGSARRK 424
Cdd:COG1196 436 EEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegfLEGVKAAL 514
|
....*
gi 321400107 425 GKDQP 429
Cdd:COG1196 515 LLAGL 519
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1256-1311 |
5.04e-12 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 62.27 E-value: 5.04e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 1256 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1311
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-375 |
1.61e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 19 QLQRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLN 91
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 92 VYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKNQAETi 171
Cdd:PRK03918 478 LRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 172 aLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERA 250
Cdd:PRK03918 548 -LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LERE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 251 NQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklren 330
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA-------- 680
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 321400107 331 sasQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 375
Cdd:PRK03918 681 ---ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-334 |
2.29e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 105 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 182 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 257 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 334
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
33-374 |
2.69e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 107
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 185
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 186 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQRE 260
Cdd:TIGR04523 317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 261 AETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQ 340
Cdd:TIGR04523 386 IKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLTN 447
|
330 340 350
....*....|....*....|....*....|....*
gi 321400107 341 QLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 374
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-412 |
4.42e-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: 64.69 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 123 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 199
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 200 KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 276
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 277 LASQIQKAPDVEQAIEVLTrSSLEVELAAKEREIAQLVEDVQ---RLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 353
Cdd:TIGR02168 328 LESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 354 EKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRI 412
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-360 |
6.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSfQGEIDALSKRSKEAEAAFLNVYKR 95
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARL-EQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 LidvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKNQAEtiALEK 175
Cdd:COG1196 325 L---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRAE 255
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 256 VAQ--REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 332
Cdd:COG1196 465 LAEllEEAALLEAALAELLEELaEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340
....*....|....*....|....*...
gi 321400107 333 SqiSQLEQQLSAKNSTLKQLEEKLKGQA 360
Cdd:COG1196 545 A--AALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-411 |
6.95e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 7 SMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRSKEAE 86
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 87 AAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQTLKN 166
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 167 QAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMT- 245
Cdd:COG4717 182 LLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLLIAAa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 246 ----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER 308
Cdd:COG4717 258 llallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 309 EIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEVKKELNILKSmEFAPSEG 382
Cdd:COG4717 338 ELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEE-QLEELLG 416
|
410 420
....*....|....*....|....*....
gi 321400107 383 AGTQDAAKPLEVLLLEKNRSLQSENAALR 411
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELE 445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-353 |
1.16e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 206 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 286 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 353
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-299 |
1.32e-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: 63.15 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 93 ykrlidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 321400107 250 ANQRAEVAQREAETLREQLSSANHSLQLASQ-IQKAPDVEQAIEVLTRSSL 299
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSElISVDEGYEAAIEAALGGRL 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-372 |
2.14e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 LIDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqa 168
Cdd:PRK03918 534 LIKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 169 etiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLE 248
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 249 RANQRAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKL 327
Cdd:PRK03918 673 RELAGLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LL 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 321400107 328 RENSASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 372
Cdd:PRK03918 738 KERALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-355 |
5.63e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLNVYKRL 96
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTL------------ 164
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 165 -------------------------------------KNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAE-- 205
Cdd:COG4717 265 ggsllsliltiagvlflvlgllallflllarekaslgKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLel 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 206 -HKVQSLQTALEKTRTELFDLKTKYDEE------TTAKADEIEMIMTDLERANQRAEvAQREAETLREQLSSANHSLQLA 278
Cdd:COG4717 343 lDRIEELQELLREAEELEEELQLEELEQeiaallAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 279 SQIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLSAKNSTLKQLEEK 355
Cdd:COG4717 422 LEALDEEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-374 |
8.01e-09 |
|
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: 60.47 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ----- 191
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEkltee 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 192 ---------------------------ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK---TKYDEETTAKADEIE 241
Cdd:TIGR02169 260 iselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 242 MIMTDLERANQR-----AEVAQREAE--TLREQLSSANHSLQLASQIQKapDVEQAIEVLTR---------SSLEVELAA 305
Cdd:TIGR02169 340 ELEREIEEERKRrdkltEEYAELKEEleDLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRLQEELQR 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321400107 306 KEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKELNILKS 374
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-438 |
9.33e-09 |
|
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: 60.47 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKN-QAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 202
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSDaSRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 203 EAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 280
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 281 iqkapdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLK 350
Cdd:TIGR02169 816 -----------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 351 QLEEKLKG-QADYEEVKKELNILKsmefapsEGAGTQDAAkplevllLEKNRSLQSE-NAALRISNSDLSGSARRKGKDQ 428
Cdd:TIGR02169 879 DLESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLSElKAKLEALEEELSEIEDPKGEDE 944
|
330
....*....|
gi 321400107 429 PESRRPGSLP 438
Cdd:TIGR02169 945 EIPEEELSLE 954
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-382 |
1.15e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVEQAI 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAE------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 292 EVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNI 371
Cdd:COG4942 170 EA-ERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAER 242
|
250
....*....|.
gi 321400107 372 LKSMEFAPSEG 382
Cdd:COG4942 243 TPAAGFAALKG 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
36-357 |
1.24e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 36 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEaeaaFLNVYKRLIDVPDpvpalDLGQQLQ-L 114
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKE----LREEAQELREKRD-----ELNEKVKeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 115 KVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:COG1340 77 KEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 195 msttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSANHS 274
Cdd:COG1340 154 -----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELHKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 275 LQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLSAKNSTLKQLEE 354
Cdd:COG1340 218 IVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 321400107 355 KLK 357
Cdd:COG1340 275 KLK 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-368 |
2.17e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 172 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 251
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 252 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 317
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 321400107 318 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 368
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-421 |
4.34e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.31 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSrefkkntpedlrkqvapllksfqGEIDALSKRSKEAEAAFLNVYKRLI 97
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQAN-----------------------GELEKASREETFARTALKNARLDLR 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 98 DVpdpvpaLDLGQQLQLKVQRlhDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:pfam12128 657 RL------FDEKQSEKDKKNK--ALAERKDSANERLNSLEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 178 KLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAE 255
Cdd:pfam12128 719 YWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 256 VAQREAETLREQLSSANHSLQlasqIQKApDVEQAIEvltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQI 335
Cdd:pfam12128 793 EVLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS--------------------------ELQQQLARLIADTKLRR 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 336 SQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNS 415
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIA 921
|
....*.
gi 321400107 416 DLSGSA 421
Cdd:pfam12128 922 DHSGSG 927
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
17-356 |
5.37e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREfkkntpedLRKQVAPLLKSFQGEIDALSKRSKEAEA---AFLNVY 93
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRT--------LDDQWKEKRDELNGELSAADAAVAKDRSeleALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 94 KRLIDVPDPVPALDLGQQLQLK-----VQRLHDIETENQklRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTL 164
Cdd:pfam12128 332 GAFLDADIETAAADQEQLPSWQselenLEERLKALTGKH--QDVTAKYNRRRSKIKEQNNRdiagIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 165 KNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQ-TALEKTRTELFD-LKTKYDEETTAKADEIEM 242
Cdd:pfam12128 410 LAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATaTPELLLQLENFDeRIERAREEQEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 243 IMTD--------------LERANQRAEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVE 302
Cdd:pfam12128 490 LQSElrqarkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPE 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 303 L----AAKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 356
Cdd:pfam12128 569 VwdgsVGGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-424 |
6.53e-08 |
|
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: 57.67 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 151 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 229
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 230 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 309
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 310 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 389
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260 270
....*....|....*....|....*....|....*
gi 321400107 390 KPLEVLLLEKNRSLQSENAALRISNSDLSGSARRK 424
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-373 |
7.92e-08 |
|
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: 56.95 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsREFKKNTPEDLRKQVApllkSFQGEIDALsKRSKEAEAAFLNVYKRLI 97
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDS----VKELIIKNL-DNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 98 DVPDPvPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQ 177
Cdd:TIGR04523 478 NKIKQ-NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDF 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 178 KLQNDFAEKErkLQETQmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 257
Cdd:TIGR04523 553 ELKKENLEKE--IDEKN----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 258 QREAETLREQ----LSSANHSLQLASQIQ--------KAPDVEQAIEvltrsslevELAAKEREIAQLVEDvqRLQASLT 325
Cdd:TIGR04523 623 KKENEKLSSIikniKSKKNKLKQEVKQIKetikeirnKWPEIIKKIK---------ESKTKIDDIIELMKD--WLKELSL 691
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 321400107 326 KLRENSASQIsqleqqlsaKNSTLKQLEEKlkgqadYEEVKKELNILK 373
Cdd:TIGR04523 692 HYKKYITRMI---------RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-360 |
8.01e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 25 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 98
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 99 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIAlEKEQK 178
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 179 LQ-NDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 255
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 256 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 332
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 321400107 333 SQISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 360
Cdd:PRK02224 606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-264 |
8.20e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 190 LQETqmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 264
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-352 |
9.11e-08 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 54.14 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 131 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 202
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 203 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 275
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 276 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 352
Cdd:pfam13851 137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-373 |
1.68e-07 |
|
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: 55.98 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 119 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 195
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 196 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 272
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 273 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 331
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 321400107 332 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 373
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-370 |
2.62e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 172 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 251
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 252 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVEQAievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRE 329
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILE--------LMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 321400107 330 NSASQISQLEQQLSAKNSTLKQLEEKLKGQ--ADYEEVKKELN 370
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
2.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 190 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 321400107 270 S 270
Cdd:COG4913 430 S 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-327 |
2.74e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 106 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 181
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 182 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 249
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 250 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 327
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
96-375 |
3.29e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 LIDVPDPVPALDLGQQLQLKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKN 166
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 167 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLk 226
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 227 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA-- 304
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAel 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 305 ------------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKE 368
Cdd:COG3206 283 sarytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLERE 359
|
....*..
gi 321400107 369 LNILKSM 375
Cdd:COG3206 360 VEVAREL 366
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-355 |
4.74e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 151 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 214 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 277
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 278 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 352
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 321400107 353 EEK 355
Cdd:PHA02562 399 VKE 401
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
4.91e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 53.53 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEKDQ--------TALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 321400107 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-414 |
5.52e-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: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 232 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 307
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 308 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLK---------------GQAD 361
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRArleallaalglplpaSAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 362 YEEVKKELNILKsmEFAPSEGAGTQDAAKPLEVLLLEKNR---SLQSENAAL--RISN 414
Cdd:COG4913 382 FAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRelrELEAEIASLerRKSN 437
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-324 |
5.82e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPED---LRKQVAPL---LKSFQGEIDALSKRSKEAEAAF 89
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELeaeIASLERSIAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 90 LNVYKRLIDVPDPVPALDlGQQLQLKVQRlHDIETENQKLREtleEYNKEFAEVKNQEVTIKALKEKIREYEQtlknqae 169
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELE-REIEEERKRR-DKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYRE------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 170 tiALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlkTKYDEETTAKADEIEMIMTDLER 249
Cdd:TIGR02169 393 --KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 250 ANQRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKER------EIAQLVEDVQRLQA 322
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgTVAQLGSVGERYAT 539
|
..
gi 321400107 323 SL 324
Cdd:TIGR02169 540 AI 541
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-414 |
6.91e-07 |
|
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: 54.21 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 125 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 202 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 279
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 280 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKN------STLKQ 351
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaQLLLE 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 352 LEEKLKGQADYE---EVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSL-QSENAALRISN 414
Cdd:pfam02463 413 LARQLEDLLKEEkkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELkKSEDLLKETQL 479
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-376 |
6.93e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLnvykr 95
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL----- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 lidvpdpvpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKN 166
Cdd:pfam05483 445 ----------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 167 QAETIALEKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELF----DLKTKYDE-ETTAKADEI 240
Cdd:pfam05483 509 SDMTLELKKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 241 EMImtdleRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQL 313
Cdd:pfam05483 581 EVL-----KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEI 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 314 VEDVQRlQASLTKLRENS-----------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 376
Cdd:pfam05483 656 IDNYQK-EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-370 |
7.15e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 162 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSL----------------------------Q 212
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKEleelsrqisalrkdlarleaeveqleerI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 213 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIE 292
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 293 VLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 370
Cdd:TIGR02168 828 SLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
109-357 |
9.61e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 109 GQQLQLKVQrlhdIE-TENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAE 185
Cdd:PRK02224 187 GSLDQLKAQ----IEeKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 186 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK-----TKYDEETTAK-----ADEIEMIMTDLERANQRAE 255
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglDDADAEAVEArreelEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 256 VAQREAETLRE---QLSSANHSLQlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL---RE 329
Cdd:PRK02224 339 AHNEEAESLREdadDLEERAEELR-----EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDApvdLG 408
|
250 260
....*....|....*....|....*...
gi 321400107 330 NSASQISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLR 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-374 |
1.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 37 ESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflNVYKRLIDVpdpvpaldlGQQLQLKV 116
Cdd:PRK03918 142 ESDESREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEK---------EKELEEVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEEYNKEFAEV----------------------------KNQEVTIKALKEKIREYEQTLKNQA 168
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELeelkeeieelekeleslegskrkleekiRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 169 ETIALEKE----QKLQNDFAEKERKLQETQMSTT----------SKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT 234
Cdd:PRK03918 287 ELKEKAEEyiklSEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 235 AKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP----------D 286
Cdd:PRK03918 367 AKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgkcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 287 VEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLSAKNstLKQLEEK 355
Cdd:PRK03918 447 EEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN--LEELEKK 523
|
410
....*....|....*....
gi 321400107 356 LKgqaDYEEVKKELNILKS 374
Cdd:PRK03918 524 AE---EYEKLKEKLIKLKG 539
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-466 |
1.24e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 196 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 276 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 340
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 341 QLSAKNSTLKQLEEKLKgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGS 420
Cdd:COG3883 176 QQAEQEALLAQLSAEEA-AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 321400107 421 ARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 466
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
123-419 |
1.27e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 123 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 202 EEAEhkvqSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTD-LERANQRAEV-AQREAETLREQLSSAN--HSLQ 276
Cdd:pfam02463 295 EEEL----KSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEiEELEKELKELeIKREAEEEEEEELEKLqeKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 277 LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE--IAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 348
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400107 349 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSG 419
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-376 |
1.44e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 36 DESEQSRKRLIEQSREFKKNTPEDLRKqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLK 115
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEK-----------ELEELEKAKEEIEEEISKITARI-------------GELKKE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 116 VQRLHD--IETENQKL------RETLEEYNKEF-----AEVKNQEVTIKALKEKIR-------EYEQTLKNQAETIALEK 175
Cdd:PRK03918 421 IKELKKaiEELKKAKGkcpvcgRELTEEHRKELleeytAELKRIEKELKEIEEKERklrkelrELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 176 --------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD 230
Cdd:PRK03918 501 laeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 231 EETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLE 300
Cdd:PRK03918 581 ELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELEKKYSE 658
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 301 VELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 376
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-268 |
1.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 14 RFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 89 FLNVYKRLIDVPDPVPalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE-VKNQEVTIKALKEKIREYEQtlKNQ 167
Cdd:TIGR02168 812 LTLLNEEAANLRERLE--SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEElEELIEELESELEALLNERAS--LEE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 168 AETIALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDL 247
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEALE 960
|
250 260
....*....|....*....|.
gi 321400107 248 ERANQRAEVAQREAETLREQL 268
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKI 981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-290 |
1.83e-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: 52.07 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDAtatvLANRQDESEQSRKRLIEQsrefkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEaaflnvykr 95
Cdd:COG4942 28 ELEQLQQEIAE----LEKELAALKKEEKALLKQ-------------------LAALERRIAALARRIRALE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 lidvpdpvpaldlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAevknqEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG4942 76 --------------QELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|....*
gi 321400107 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVEQA 290
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-347 |
2.04e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.77 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 86 EAAFLnvyKRLIDVPDPVPALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARL---KKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 166 N--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQ----LASQIQKAPDVEQAIEV-------LT 295
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskfLSQLVNTLEPVFQKLSVlqleldgLF 1160
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 321400107 296 RSSLEVELAAKEREIAqLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNS 347
Cdd:COG5022 1161 WEANLEALPSPPPFAA-LSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFS 1211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-361 |
2.12e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKntpedlrkqvapLLKSFQGEIDALSKRSKEAEAAflNVYKR 95
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQR------------LAEYSWDEIDVASAEREIAELE--AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 LIDVPDpvpalDLgQQLQlkvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG4913 680 LDASSD-----DL-AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAP-DVEQAIEVLTRSSLEVE--------LAAKEREiaqlVED 316
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIrEIKERIDPLNDSLKRIPfgpgrylrLEARPRP----DPE 895
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 321400107 317 VQRLQASLTKLRENSASQISQLEQqlsAKNSTLKQLEEKLKGQAD 361
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSE---ARFAALKRLIERLRSEEE 937
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-412 |
2.27e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 171 IALEKEQKLQNDFAEKERKLQETQmsTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkydEETTAKADEIEMIMTDLERA 250
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 251 NQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 330
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA-------ELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 331 -----SASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQS 405
Cdd:COG4372 173 lqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
....*..
gi 321400107 406 ENAALRI 412
Cdd:COG4372 253 EEVILKE 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-319 |
3.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 321400107 273 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 319
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-364 |
4.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlknqaetialEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAELESELEEAREA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 197 TT---SKLEEAEHKVQSLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE--QLSSA 271
Cdd:PRK02224 379 VEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAEALLEagKCPEC 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 272 NHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 349
Cdd:PRK02224 458 GQPVEGSPHVETIEEDRERVEELEaeLEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
250
....*....|....*
gi 321400107 350 KQLEEKLKGQADYEE 364
Cdd:PRK02224 537 ERAEELRERAAELEA 551
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
7.62e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 91 NVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 171 ---IALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEktrtelfDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-373 |
7.73e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRL 96
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknqeVTIKALKEKIREYEQTLknqAETIALEKE 176
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA------------ALAAALQNIVVEDDEVA---AAAIEYLKA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 177 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 257 AQREAETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE 329
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 321400107 330 NSASQISQ-LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 373
Cdd:COG1196 729 QLEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
119-416 |
9.08e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 119 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 191 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 269
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 270 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 345
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321400107 346 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD 416
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
46-354 |
1.03e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 46 IEQSREFKKntpEDLRKQvaplLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETE 125
Cdd:COG3206 162 LEQNLELRR---EEARKA----LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 126 NQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAE 205
Cdd:COG3206 228 LAEARAELAE----------AEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 206 HKVQSLQTALEKTRTELfdlktkydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAP 285
Cdd:COG3206 291 PDVIALRAQIAALRAQL--------------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 286 dveqaievltrsslevelaAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 354
Cdd:COG3206 348 -------------------ELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTVGNVRVIDP 393
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-358 |
1.19e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 84 EAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 160 YEQTLkNQAETIALEKEQKLQ-----NDFAEKERKlQETQMSTTSKLEEAEHKVQSLQTAlektRTELFDLKTKYDEETT 234
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrkiAGEVSRSEA-WDVARELLRRLREQRHLAEQLQQL----RMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 235 AKA-------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDVEQAIEVLTR 296
Cdd:PRK04863 535 AERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAWLAAQDALAR 614
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 297 SSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKLKG 358
Cdd:PRK04863 615 LREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
211-357 |
1.23e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 211 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 288
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 289 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
105-370 |
1.31e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 105 ALDLGQQLQLKVQRLHDIEtenqklrETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFA 184
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQ-------YRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 185 EKERKLQETQMST---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------- 252
Cdd:PRK04863 359 ELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdlta 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 253 -----RAEVAQREAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKL 327
Cdd:PRK04863 438 dnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRL 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 321400107 328 RE--NSASQISQLEQQLSAknstlkqLEEKLKGQADYEEVKKELN 370
Cdd:PRK04863 506 REqrHLAEQLQQLRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
112-427 |
1.55e-05 |
|
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: 49.97 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 112 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAkadeiemIMTDLERANQRAEVAQREAETLREQLSSA 271
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEIENASSSLGSDLAAREDAL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 272 NHSLQLASQIQK------APDVEQAIEVLT----------------------RSSLEVELAAKEREIAQLVED------- 316
Cdd:TIGR00618 742 NQSLKELMHQARtvlkarTEAHFNNNEEVTaalqtgaelshlaaeiqffnrlREEDTHLLKTLEAEIGQEIPSdedilnl 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 317 -----VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKp 391
Cdd:TIGR00618 822 qcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE- 899
|
330 340 350
....*....|....*....|....*....|....*.
gi 321400107 392 levLLLEKNRSLQSENAALRISNSDLSGSARRKGKD 427
Cdd:TIGR00618 900 ---ITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
108-445 |
1.67e-05 |
|
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: 49.44 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 LGQQLQLKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKNQAETIALEKEQkLQNDFAEKE 187
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 188 RK----------LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQ--RAE 255
Cdd:pfam10174 394 RKinvlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEQREREDRerLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 256 VAQ--REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLRENS 331
Cdd:pfam10174 470 LESlkKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 332 ---------ASQISQLEQQLSAKNstlkqlEEKLKGQAdyeEVKKELNILKSMEfapsegagTQDAAKPLEVLLLEKNRS 402
Cdd:pfam10174 548 eavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NEKNDKDKKIAELESLTL 610
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 321400107 403 LQSENAALRISN-SDLSGSARRKGKDQ-PESRRPGSLPAPPPSQL 445
Cdd:pfam10174 611 RQMKEQNKKVANiKHGQQEMKKKGAQLlEEARRREDNLADNSQQL 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
53-360 |
1.84e-05 |
|
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: 49.45 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 53 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 120
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 121 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 188
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 189 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 260
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 261 AETLREQLSSANHSL------------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKL 327
Cdd:pfam12128 421 ESELREQLEAGKLEFneeeyrlksrlgELKLRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKR 500
|
330 340 350
....*....|....*....|....*....|...
gi 321400107 328 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 360
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
66-371 |
2.02e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 66 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 145
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 146 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 225
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 226 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 305
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 306 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 366
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 321400107 367 KELNI 371
Cdd:PRK11281 282 QELEI 286
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-410 |
2.59e-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: 48.96 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRKRL------IEQSREFKKNTPEDLRKQVAPLLK---SFQG---EIDALSKRSKE 84
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLqntvheLEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGvlqEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 85 AEAAflNVYKRliDVPDPVPALDLG-------QQLQLKVQ-----------RLHDIETENQKLRETLEEYNKEFAE--VK 144
Cdd:pfam15921 199 ASGK--KIYEH--DSMSTMHFRSLGsaiskilRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQDRIEqlIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 145 NQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQETQMSTTSKLEEA----EHKVQSLQTALE 216
Cdd:pfam15921 275 EHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 217 KTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlssanhslqlasqiqkapDVEQAIev 293
Cdd:pfam15921 353 LANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------------------DTGNSI-- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 294 lTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSAsqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKEL-NIL 372
Cdd:pfam15921 413 -TIDHLRRELDDRNME-------VQRLEALLKAMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrKVV 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 321400107 373 KSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAL 410
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-368 |
2.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGE---IDALSKRSKEAEAAflNVYKRLI 97
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAkkkADEAKKKAEEKKKA--DEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 98 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 176 EQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--RANQ 252
Cdd:PTZ00121 1521 AKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaRIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 253 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 332
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
330 340 350
....*....|....*....|....*....|....*.
gi 321400107 333 SQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 368
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-378 |
3.56e-05 |
|
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: 48.66 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 119 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 192
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 193 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 266 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 338
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 321400107 339 EQQLSAKNSTLKQLEEKLKGQADyEEVKKElNILKSMEFA 378
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-353 |
3.58e-05 |
|
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: 48.59 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 205 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 276
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 277 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 352
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 321400107 353 E 353
Cdd:pfam07111 297 E 297
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1256-1341 |
3.89e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 1256 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1335
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 321400107 1336 RSGRAA 1341
Cdd:COG5576 121 EEADLA 126
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
110-364 |
4.06e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 189
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 190 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 256
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 257 AQREAETLREQLSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRL 320
Cdd:pfam01576 150 LSKERKLLEERIS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 321400107 321 QASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEE 364
Cdd:pfam01576 228 QAQIAELRaqlakkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-409 |
4.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLNVYKRL 96
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKA 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA--LKEKIREYEQT---------LK 165
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKAdeakkkaeeDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 166 NQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMT 245
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 246 DLERANQ---RAEVAQREAETLREQLSSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSSLEVE 302
Cdd:PTZ00121 1481 EAKKADEakkKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 303 LAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAD----YEEVKKELNILKSMEFA 378
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQL 1638
|
410 420 430
....*....|....*....|....*....|.
gi 321400107 379 PSEGAgtQDAAKPLEVLLLEKNRSLQSENAA 409
Cdd:PTZ00121 1639 KKKEA--EEKKKAEELKKAEEENKIKAAEEA 1667
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-410 |
5.20e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 208
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 209 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 279
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 280 QIQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 356
Cdd:TIGR00606 391 QIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 357 KG--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLLEKNRSLQSENAAL 410
Cdd:TIGR00606 471 DRilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
121-433 |
5.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 121 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKNQAETIALEKEQKLqndfAEKERKLQETQMSTTS 199
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 200 KLEEAEHKVQSLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 279
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 280 QIQKAPDVEQAIEVltRSSLEVELAAKEREI--AQLVEDVQRLQASLTKLRENSASQISQLEQqlsaknsTLKQLEEKLK 357
Cdd:PTZ00121 1174 DAKKAEAARKAEEV--RKAEELRKAEDARKAeaARKAEEERKAEEARKAEDAKKAEAVKKAEE-------AKKDAEEAKK 1244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 358 GqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRR 433
Cdd:PTZ00121 1245 A----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-430 |
5.65e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 254 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDV 317
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 318 QRLQASLTKLRENSASqISQLEQQLSAKNSTLKQlEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPleVLLL 397
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP--EDLS 282
|
250 260 270
....*....|....*....|....*....|...
gi 321400107 398 EKNRSLQSENAALRISNSDLSGSARRKGKDQPE 430
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
7.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 181 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-412 |
8.29e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKnqaetialEKEQKLQNDFAEKERK 189
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELE--------ELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 190 LQEtqmsttskLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4372 100 QEE--------LESLQEEAEELQEELEELQKERQDLE-QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 270 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 349
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321400107 350 KQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRI 412
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
8.29e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 321400107 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
758-944 |
8.75e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 758 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 833
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 834 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 913
Cdd:PHA03247 347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
|
170 180 190
....*....|....*....|....*....|.
gi 321400107 914 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 944
Cdd:PHA03247 409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
199-466 |
9.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 199 SKLEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL--- 275
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 276 -----QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 350
Cdd:COG3883 85 reelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 351 QLEEKLKG----QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGK 426
Cdd:COG3883 165 ELEAAKAEleaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 321400107 427 DQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 466
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
108-357 |
1.03e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 46.23 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 LGQQLQLkvqrLHDIETENQKLRETLEEYNKEfaevknqevTIKALKEKIREYEQTLKNQAETIAL------EKEQKLQN 181
Cdd:pfam04108 40 LSVQLAN----LEKVREGLEKVLNELKKDFKQ---------LLKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 182 DFAEkERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEA 261
Cdd:pfam04108 107 DFID-EDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 262 ETLREQLssANHsLQLASQIQKAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS- 333
Cdd:pfam04108 181 ASLLESL--TNH-YDQCVTAVKLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSa 257
|
250 260
....*....|....*....|....*.
gi 321400107 334 --QISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:pfam04108 258 lqLIAEIQSRLPEYLAALKEFEERWE 283
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
109-355 |
1.14e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 109 GQQLQLKVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQaETIALEKEQKLQ 180
Cdd:COG3096 342 ALRQQEKIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 181 NdFAEKERKLQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQ 252
Cdd:COG3096 421 A-LEKARALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 253 RAE-----------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRL 320
Cdd:COG3096 496 TARellrryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEEL 569
|
250 260 270
....*....|....*....|....*....|....*
gi 321400107 321 QASLTKLREnsasQISQLEQQLSAKNSTLKQLEEK 355
Cdd:COG3096 570 EEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-373 |
1.35e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 54 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLNVYKRLIDVPDPVPAL----DLG 109
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 110 QQLQLKVQ----RLHDIETENQKLRETLEEYNK--EFAEVKNQEVTIKALKEK--IREYEQTLKNQAETIA--------L 173
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKYKndIENKKQILSNIDAEINkyhaiikkL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 174 EKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEILKIQEID 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 254 AEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT---------------------------RSSLEV 301
Cdd:PRK01156 404 PDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynekKSRLEE 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 302 ELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILK 373
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-266 |
1.42e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 60 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKR--LIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLR------- 130
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 131 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 204
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321400107 205 EHKVQSLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
58-405 |
1.44e-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: 46.22 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAaflnvykrlIDVPDPVPALDLgQQLQLKVQRLHD----IETENQKLR 130
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGKKY-LLLQKQLEQLQEenfrLETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 131 ETLEEYNKEFAE--VKNQEVT-----IKALKEKIREYEQTLK--NQAETIALEKEQKLQ--NDFAEKERKLQETQ---MS 196
Cdd:pfam05622 87 IKCEELEKEVLElqHRNEELTslaeeAQALKDEMDILRESSDkvKKLEATVETYKKKLEdlGDLRRQVKLLEERNaeyMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---REQLSSANH 273
Cdd:pfam05622 167 RTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRDTLRETNE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 274 SL-----------------------------------------------------QLASQIQKAPDVEQAIE--VLTRSS 298
Cdd:pfam05622 243 ELrcaqlqqaelsqadallspssdpgdnlaaeimpaeireklirlqhenkmlrlgQEGSYRERLTELQQLLEdaNRRKNE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 299 LEVEL-AAKER--EIAQLVEDVQR----------------------------LQASLTKLRE-----------NSASQIS 336
Cdd:pfam05622 323 LETQNrLANQRilELQQQVEELQKalqeqgskaedssllkqkleehleklheAQSELQKKKEqieelepkqdsNLAQKID 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 337 QLEQQLSAKNSTLKQLEEKLKgqadyEEVKKELNILKSMEfaPSEGAGTQDAAKPLEVLLLEKNRSLQS 405
Cdd:pfam05622 403 ELQEALRKKDEDMKAMEERYK-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-376 |
1.44e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 13 KRFD-LQQLQRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSK 80
Cdd:TIGR00606 173 QKFDeIFSATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 81 RSKEAEAAFLNVYKrlidVPDPVPALDlgqqlQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalKEKIREY 160
Cdd:TIGR00606 253 RLKEIEHNLSKIMK----LDNEIKALK-----SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 161 EQTLKN-QAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKVQSLQTALEK----TRTELFDLKTKYDEETTA 235
Cdd:TIGR00606 318 ERELVDcQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 236 K----------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LA 304
Cdd:TIGR00606 393 KnfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLE 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321400107 305 AKEREIAQLVEDVQRLQASLTKLRENSASQiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 376
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELSKAEKNSLTE-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-374 |
1.58e-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: 46.55 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 110 QQLQLKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEK 186
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 187 ERKLQETQMSTT----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 258
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 259 REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 335
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 321400107 336 SQLE---QQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKS 374
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-376 |
1.73e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 107 DLGQQLQ---------------------LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:pfam15921 500 DLTASLQekeraieatnaeitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 166 NQAET---IALEKEQkLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQtaLEKTR-----TELFDLKTKYDEETT 234
Cdd:pfam15921 580 QHGRTagaMQVEKAQ-LEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLE--LEKVKlvnagSERLRAVKDIKQERD 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 235 AKADEIEMIMTDLERANQRAEVAQR-------EAET----LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 303
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRnfrnkseEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321400107 304 AAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLEEKLKGqadyeevkkELNILKSME 376
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAG---------ELEVLRSQE 799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-390 |
1.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 125 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 201 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEmimTDLERANQRAEVAQREAEtlrEQLSSANHSLQLASQ 280
Cdd:PTZ00121 1642 EAEEKKKAEELK---------------KAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 281 IQKAPDVEQAIEVLTRSSLEVELAAKEREI----AQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEK 355
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAV 1780
|
250 260 270
....*....|....*....|....*....|....*
gi 321400107 356 LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAK 390
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
221-373 |
2.07e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 297
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 298 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 373
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-376 |
2.39e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 122 IETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIRE-----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEI--SRMRElerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 197 TTSKLEEAEHKVQSLQTALEKTRtelfdlktkydeettakADEIEMI-MTDLERANQRAEVAQREAETLREQLssanhsl 275
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEER-----------------AREMERVrLEEQERQQQVERLRQQEEERKRKKL------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 276 qlasQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQlvedVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ--LE 353
Cdd:pfam17380 478 ----ELEKEKRDRKRAEEQRRKILEKELEERKQAMIE----EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqeME 549
|
250 260
....*....|....*....|...
gi 321400107 354 EKLKGQADYEEVKKELNILKSME 376
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAME 572
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-376 |
2.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 119 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQAETIALEKEQKlqndfAEKERKLQEtqmstt 198
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 199 skLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 278
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 279 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEK 352
|
250
....*....|....*....
gi 321400107 358 GQADYEEVKKELNILKSME 376
Cdd:PRK03918 353 RLEELEERHELYEEAKAKK 371
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-368 |
3.08e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 49 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpALDLGQQLQLKVQRLHDIETENQK 128
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 129 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKNQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKV 208
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 209 QSLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLSSANHSLQLASQIQK 283
Cdd:TIGR00618 331 AAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 284 APDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQLSAKNSTLKQLEEKLK 357
Cdd:TIGR00618 404 ILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHL 483
|
330
....*....|.
gi 321400107 358 gqaDYEEVKKE 368
Cdd:TIGR00618 484 ---QETRKKAV 491
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
3.70e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 112 LQ-LKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKNQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 181 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 321400107 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
21-272 |
4.26e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 21 QRELDATATVLANRQD-----ESEQSRKRLIEQSREFKKNTPEDLRKQVAPL--LKSFQGEIDALSKR-SKEAEAAflnv 92
Cdd:pfam17380 326 QAEMDRQAAIYAEQERmamerERELERIRQEERKRELERIRQEEIAMEISRMreLERLQMERQQKNERvRQELEAA---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 93 ykRLIDVPDPVPALDLGQQLQLKVQ-RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaeTI 171
Cdd:pfam17380 402 --RKVKILEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK--KL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 172 ALEKEQKLQNDFAEKERKLQETQM-STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTAKADEIE-------- 241
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELeERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREaEEERRKQQEMEerrriqeq 557
|
250 260 270
....*....|....*....|....*....|.
gi 321400107 242 MIMTDLERAnqRAEVAQREAETLREQLSSAN 272
Cdd:pfam17380 558 MRKATEERS--RLEAMEREREMMRQIVESEK 586
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-358 |
4.49e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKkntpeDLRKQVApllkSFQGEIDALSKRSKEAEAAF--LNVY 93
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD-----SLKSQLA----DYQQALDVQQTRAIQYQQAVqaLEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 94 KRLIDVPD--PVPALDLGQQLQLKVQRLHDIETEN-QKLR---ETLEEYNKEFA-------EVKNQEVTIKAlKEKIREY 160
Cdd:COG3096 426 RALCGLPDltPENAEDYLAAFRAKEQQATEEVLELeQKLSvadAARRQFEKAYElvckiagEVERSQAWQTA-RELLRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 161 EQtLKNQAEtialeKEQKLQNDFAEKERKLQEtqmsttskleeaEHKVQSLQTALEKTrtelfdLKTKYDEettakADEI 240
Cdd:COG3096 505 RS-QQALAQ-----RLQQLRAQLAELEQRLRQ------------QQNAERLLEEFCQR------IGQQLDA-----AEEL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 241 EMImtdLERANQRAEVAQREAETLREQLSSANHSL-QLASQI----QKAPDVEQAIEVLTR----------SSLEV---- 301
Cdd:COG3096 556 EEL---LAELEAQLEELEEQAAEAVEQRSELRQQLeQLRARIkelaARAPAWLAAQDALERlreqsgealaDSQEVtaam 632
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 302 -ELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLSAKNSTLKQLEEKLKG 358
Cdd:COG3096 633 qQLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
68-270 |
6.07e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 68 LKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE----V 143
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALN--RRIQLLEEELERTEERLAEALEKLEEAEKAADEsergR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 144 KNQEVTIKALKEKIREYEQTLKnQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRT 220
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 321400107 221 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
122-353 |
6.34e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 122 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAE-------------TIALEKEQKLQNDFA 184
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKAQFERDLQARDEQGEekrrqlvkqvrelEAELEDERKQRAQAV 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 185 EKERKLQ------ETQMSTTSK-LEEAEHKVQSLQTALEKTRTELFDLKTKYDE------ETTAKADEIEMIMTDLERAN 251
Cdd:pfam01576 770 AAKKKLEldlkelEAQIDAANKgREEAVKQLKKLQAQMKDLQRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 252 QRAEVAQREAETLREQLSSanhslQLASQIQKapdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-- 329
Cdd:pfam01576 850 AASERARRQAQQERDELAD-----EIASGASG------------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDrl 912
|
250 260
....*....|....*....|....*
gi 321400107 330 -NSASQISQLEQQLSAKNSTLKQLE 353
Cdd:pfam01576 913 rKSTLQVEQLTTELAAERSTSQKSE 937
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-354 |
7.48e-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: 44.12 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 28 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpald 107
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 lgQQLQLKVQRLHDIETENQklRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalEKEQKLQNDFAEKE 187
Cdd:pfam07888 100 --EEKYKELSASSEELSEEK--DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 188 RKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 262 ETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 322
Cdd:pfam07888 254 EGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350
....*....|....*....|....*....|...
gi 321400107 323 SLTKLRensaSQISQLEQQLS-AKNSTLKQLEE 354
Cdd:pfam07888 333 RLQEER----MEREKLEVELGrEKDCNRVQLSE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
23-373 |
7.87e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 23 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvaplLKSFQGEidalSKRSKEAEAA-------FLNVYKR 95
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND-----LYHNHQR----TVREKERELVdcqreleKLNKERR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 96 LIDVPDPVPALDLGqQLQLKVQRLH------DIETENQKLRETLEEYNKEF---AEVKN-QEVTIKALKEKIREYEQTLK 165
Cdd:TIGR00606 337 LLNQEKTELLVEQG-RLQLQADRHQehirarDSLIQSLATRLELDGFERGPfseRQIKNfHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 166 NQAETIALEKEQ--KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQT-------------ALEKTRTELFDL----- 225
Cdd:TIGR00606 416 DLQSKERLKQEQadEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdrileldqELRKAERELSKAeknsl 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 226 -KTKYDEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSS 298
Cdd:TIGR00606 496 tETLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQ 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321400107 299 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 373
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
22-394 |
7.97e-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: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 22 RELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF--- 89
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqst 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 90 ---LNVYKRLIDVPDP--VPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKIR 158
Cdd:pfam05557 131 nseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 159 EYEQTLKNQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKVQSLQTALEKTRTELfdlktkYDEETTAKAD 238
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQDT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 239 EIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVEDV 317
Cdd:pfam05557 272 GLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRRL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 318 QRLQASLTKLRENSASQISQLEQQLSAKNSTlKQLEEKLKGQADY-EEVKKELNILK-SMEFAPSEGAGTQDAAKPLEV 394
Cdd:pfam05557 345 QRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
125-222 |
8.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETiaLEKeqklqndfaeKERKLQETQMSTTSKLEEA 204
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLEL--LEK----------REEELEKKEKELEQKQQEL 126
|
90
....*....|....*...
gi 321400107 205 EHKVQSLQTALEKTRTEL 222
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL 144
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
698-939 |
9.06e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 698 TAEPAQPSSASGSGNSDDAIRSILQQA---RREMEAQQAALDPA---------LKQAPLSQSDITILTPKLlSTSPMPTv 765
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAaparppvrrLARPAVSRSTESFALPPD-QPERPPQ- 2910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 766 ssyPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAAdcaqgvlrqvknevGRSGAWKDHWWSAVQPERRN 845
Cdd:PHA03247 2911 ---PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG--------------EPSGAVPQPWLGALVPGRVA 2973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 846 A--------ASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETP 917
Cdd:PHA03247 2974 VprfrvpqpAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE 3053
|
250 260
....*....|....*....|..
gi 321400107 918 QNSPLPSSPIVPMSKPTKPSVP 939
Cdd:PHA03247 3054 ALDPLPPEPHDPFAHEPDPATP 3075
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
63-228 |
1.04e-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: 42.60 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 63 QVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLKVQRLhdiETENQKLRETLEEYNKEFAE 142
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------EDLEKEIKRL---ELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 143 VKNQ-EVT-----IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttsklEEAEHKVQSLQTALE 216
Cdd:COG1579 85 VRNNkEYEalqkeIESLKRRISDLEDEILE-----LMERIEELEEELAELEAELAELE-------AELEEKKAELDEELA 152
|
170
....*....|..
gi 321400107 217 KTRTELFDLKTK 228
Cdd:COG1579 153 ELEAELEELEAE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-267 |
1.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 43 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 120
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 121 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 197
Cdd:PTZ00121 1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321400107 198 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:PTZ00121 1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
133-353 |
1.12e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 133 LEEYNKEFAEVKNQEVTIKALKEKIreyeqtlknqaetIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKVQSLQ 212
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKL-------------IASLKEGSGVEGL--------DSSTALTLELEELRQERDLLR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 213 TALEKTRTELFDLKTKydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIE 292
Cdd:pfam09787 61 EEIQKLRGQIQQLRTE---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 293 VLTR--SSLEVELaakEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQL------------------SAKN 346
Cdd:pfam09787 118 RLQEelRYLEEEL---RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLhqltetliqkqtmlealsTEKN 194
|
....*..
gi 321400107 347 STLKQLE 353
Cdd:pfam09787 195 SLVLQLE 201
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
252-411 |
1.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 252 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 317
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 318 QRLQASLTKLRENS------------------ASQISQLEQQLSAKNS----------TLKQLEEKLKG----------- 358
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 359 QADYEEVKKELNILKSMEFAPSEGA------GTQDAAKplevlLLEKNRSLqseNAALR 411
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSEVVqrrphfSYEDAVG-----LLGENSDL---NEKLR 990
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
107-356 |
1.24e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 107 DLGQQLQLKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQtlKNQAEtiaLEKEQKLQNDFAE 185
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQ--KYEDE---LNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 186 KERKLQETQMSTTskleEAEHKVQSLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 264
Cdd:pfam00038 108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 265 REQLSS-ANHSLQLASQIQKApDVEQAIEVLTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 340
Cdd:pfam00038 176 RAQYEEiAAKNREEAEEWYQS-KLEELQQAAARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
|
250 260
....*....|....*....|
gi 321400107 341 QLSAK----NSTLKQLEEKL 356
Cdd:pfam00038 253 RYELQladyQELISELEAEL 272
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-376 |
1.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLNVYKRLIDVPDP 102
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 103 VPALDLGQQLQLKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKNQAETIALE 174
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 175 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTE----------LFDLKTKYDE-----ETTAKADE 239
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeakkaeekkkADEAKKKAEEakkadEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 240 I----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV----ELAAKEREIA 311
Cdd:PTZ00121 1327 AkkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDK 1404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321400107 312 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSME 376
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
117-222 |
1.63e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 117 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIREyeqtLKNQAEtIALEKEQKLQND 182
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKD----LKWEHE-VLEQRFEKVERE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 321400107 183 FAEKERK----LQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 222
Cdd:pfam13851 122 RDELYDKfeaaIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
700-968 |
1.65e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.15 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 700 EPAQPSSASGSGNSDDairsILQQARREMEAQQAALDPALKQAPLSQ---SDITILTPKLLSTSPMPTVSSYPPLAiSLK 776
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEpvaVAAAATTATQSWAAPVEPVTQTPPVA-SVD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 777 KPSAAPEAGASALPNPPAlkKEAQDAPglDPQGAADCAQGVLRQVknevgrsgAWKDHWWSAVQPERRNAASSEEAKAEE 856
Cdd:PRK10263 351 VPPAQPTVAWQPVPGPQT--GEPVIAP--APEGYPQQSQYAQPAV--------QYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 857 TGGGKEKGSGGSGGGSQPRAER----SQLQGPSSSEYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSK 932
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQpvagNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVE 497
|
250 260 270
....*....|....*....|....*....|....*.
gi 321400107 933 PTKPSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 968
Cdd:PRK10263 498 ETKPARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
107-434 |
1.79e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 107 DLGQQLQ-LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKNQAETIALEKEQKLQNDFAE 185
Cdd:PTZ00108 1035 DLVKELKkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEK 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 186 KERKLQETQmSTTSK---LEEaehkVQSLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVA 257
Cdd:PTZ00108 1114 KEKELEKLK-NTTPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKK 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 258 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 337
Cdd:PTZ00108 1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 338 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmeFAPSEGAGTQDA-AKPLEVLLLEKNRSLQSENAALRISNSD 416
Cdd:PTZ00108 1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKvKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
|
330
....*....|....*...
gi 321400107 417 lSGSARRKGKDQPESRRP 434
Cdd:PTZ00108 1339 -TRVKQASASQSSRLLRR 1355
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
125-273 |
1.98e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.02 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 204
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 205 EHKVQSLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 273
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1325-1398 |
2.11e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 2.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 1325 GQAGASDSPSARSGRAAPSSEGD-----SCDGVEATEGPGSADTEEPKSQGEAEREEVPRPAEQTEPPPSGTPGPDDAR 1398
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSgpapsSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
141-359 |
2.12e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETialekeqklqNDFAEKERKLQEtqmsttsKLEEAEHKVQSLQTALEKTRT 220
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQK-------ALDDAPAELRELRQELAALQA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 221 ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA---------ETLREQLSSANHSLQ-LASQIQKAPDVEQA 290
Cdd:pfam12795 66 KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSqlielqtrpERAQQQLSEARQRLQqIRNRLNGPAPPGEP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 291 IEVLTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQ 359
Cdd:pfam12795 146 LSEAQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-232 |
2.22e-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: 42.75 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLA---------NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKE 84
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 85 AEAAFLNVYKRLIDVPDPVpaLDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKER--DELEAQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321400107 165 KN----QAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEE 232
Cdd:TIGR02169 941 GEdeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-409 |
2.39e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 119 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKNQAETIALEKE--QKLQNDFAEKERKLQEtQM 195
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEE-EI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 196 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSL 275
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER----EETRQVYMDL---NNNIEKMILAFEELRVQ--AENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 276 QLASQIQKAPDVEQAIEvltrSSLEVELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLSAKNSTLKQ 351
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLE----EEYKKEINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKE 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 321400107 352 LEEKLKG-QADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 409
Cdd:pfam05483 287 LIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
17-288 |
2.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATA----TVLANRQDESEQSRKRLIEQSREFKKNTPE-DLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLN 91
Cdd:PRK04863 874 LSALNRLLPRLNlladETLADRVEEIREQLDEAEEAKRFVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRD 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 92 VYKRLIDVP------------DPVPALDLGQQLQLKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKEKIR 158
Cdd:PRK04863 954 AKQQAFALTevvqrrahfsyeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKSSYD 1030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 159 EYEQTLKnqaetialEKEQKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKVQSLQTALEKTRTELfdlktkydeet 233
Cdd:PRK04863 1031 AKRQMLQ--------ELKQELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC----------- 1086
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 321400107 234 takadEIEMimtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 288
Cdd:PRK04863 1087 -----EAEM-----DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-369 |
2.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 115 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 178 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKVQSLQT------ALEKTRTELFDLKTKYDEETTA---------- 235
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 236 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 305
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 306 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 369
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-209 |
2.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 12 WKRFDLQQLQRELDATATVLAN-------------RQDESEQSRKRLIEQSREFKKN--TPEDLRKQVAPLLKSFQGEID 76
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERldassddlaaleeQLEELEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 77 ALSKRSKEAEAAFLNvyKRLIDVPDPVPALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEF-AEVKNQEVTIKALk 154
Cdd:COG4913 738 AAEDLARLELRALLE--ERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWpAETADLDADLESL- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 321400107 155 ekiREYEQTLKNQAETIALEKEQKLqndfaeKERKLQETQMSTT---SKLEEAEHKVQ 209
Cdd:COG4913 815 ---PEYLALLDRLEEDGLPEYEERF------KELLNENSIEFVAdllSKLRRAIREIK 863
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
115-353 |
3.05e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 115 KVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIreyeqtlkNQAEtialekeqklqnDFAEKER--KLQ 191
Cdd:pfam06160 33 KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELL--------FEAE------------ELNDKYRfkKAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 192 ETQMSTTSKLEEAEHKVQSLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevAQREA--- 261
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------ANRFSygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 262 --ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLRE------ 329
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELKEgyreme 224
|
250 260 270
....*....|....*....|....*....|...
gi 321400107 330 ---------NSASQISQLEQQLSAKNSTLKQLE 353
Cdd:pfam06160 225 eegyalehlNVDKEIQQLEEQLEENLALLENLE 257
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1316-1405 |
3.08e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 1316 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEVPRPAEQTEPPPSG 1390
Cdd:PRK12678 55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
|
90
....*....|....*
gi 321400107 1391 TPGPDDARDDDHEGG 1405
Cdd:PRK12678 135 EAARRGAARKAGEGG 149
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
40-376 |
3.12e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 40 QSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQGEIdaLSKRSKEAEAAFLNVYKRLIDVPDPVPALD-----LGQQ 111
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKqqsSIEEQRRLLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQqqkttLTQK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 112 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS- 270
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSe 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 271 ANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelaakerEIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 350
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
330 340
....*....|....*....|....*.
gi 321400107 351 QLEEKLKGQADYEEVKKELNILKSME 376
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQ 652
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
108-361 |
3.32e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 LGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKNQAETIALEKeQKLQNDFAE 185
Cdd:pfam15964 361 LKSELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 186 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR------ 259
Cdd:pfam15964 436 AQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarar 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 260 -EAETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQ 312
Cdd:pfam15964 516 eECLKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAK 595
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 321400107 313 LVEDVQRLQASLTKLRENSASQISQLEQQlsakNSTLKQLEEKLKGQAD 361
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
127-324 |
3.40e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 205
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 206 HKVQSLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 279
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 321400107 280 -----QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 324
Cdd:COG1842 169 rmeekIEEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
29-344 |
3.45e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 29 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpaldl 108
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 109 gqqlqlkvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKER 188
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 189 KLQETQMSTTSKLEEAEHKVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 256
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 257 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 320
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
|
330 340
....*....|....*....|....
gi 321400107 321 QASLTKLREnSASQISQLEQQLSA 344
Cdd:PRK10929 282 DLIASQQRQ-AASQTLQVRQALNT 304
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
112-291 |
3.57e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 112 LQLKVQR---LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQ---TLKNQAETIALEKEQ---KLQND 182
Cdd:pfam17078 20 LQLTVQSqnlLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDqlsELKNSYEELTESNKQlkkRLENS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 183 FAEKERKLQETQMSTT-------SKLEEAEH---KVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ 252
Cdd:pfam17078 100 SASETTLEAELERLQIqydalvdSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 321400107 253 RAEVAQREAET-LREQLSSANHSLQLASQIQKAPDVEQAI 291
Cdd:pfam17078 180 NLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
112-222 |
3.82e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 112 LQLKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVTI-KALKEKIREYEQT---LKNQAETIALE-KEQKLQNDFAEK 186
Cdd:pfam15294 131 LHMEIERLKE---ENEKLKERLKTLESQATQALDEKSKLeKALKDLQKEQGAKkdvKSNLKEISDLEeKMAALKSDLEKT 207
|
90 100 110
....*....|....*....|....*....|....*.
gi 321400107 187 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 222
Cdd:pfam15294 208 LNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-244 |
3.93e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.78 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 5 VGSMFQYWKRFDLQQLQRELDATATVlANRQDESEQSRKRLIEQSREFKKntpedLRKQVAPLLKSFQGEIDALSKRSke 84
Cdd:COG0610 690 LRALFPEGVDFSAFDPTEKLEALDEA-VERFLGDEEARKEFKKLFKELSR-----LYNLLSPDDEFGDLELEKYRDDV-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 85 aeAAFLNVYKRLIDVPDPVPAldlgQQLQLKVQRLHD--IETENQKLRETLEE---YNKEFAE--------VKNQEVTIK 151
Cdd:COG0610 762 --SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQnpvQYRKFSElleeiieeYNNGALDAD 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 152 ALKEKIREYEQTLKNQAETIA---LEKEQK-----LQNDFAEKERKLQETQMSTTSKlEEAEHKVQSLQTALEKTRTELF 223
Cdd:COG0610 836 EVLEELEELAKEVKEEEERAEeegLNEEELafydaLAENLGDEKLKELAKELDDLLK-KNVTVDWRKRESVRAKLRDAIK 914
|
250 260
....*....|....*....|.
gi 321400107 224 DLKTKYDEETTAKAdeIEMIM 244
Cdd:COG0610 915 RLLRKYGYPKQDEA--VEEVY 933
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-367 |
3.95e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlrkQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRL 96
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE---ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlknqaetiALEKE 176
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT------------NLQRR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 177 QKLQNDFAEKERKLQETqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 246
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 247 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 312
Cdd:TIGR00606 960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 321400107 313 LvedvqrlqasLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKK 367
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIK 1085
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-361 |
4.63e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 235 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 314
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 321400107 315 edvqrlqasLTKLRENSAsQISQLEQQLSAKNSTLKQLEEKLKGQAD 361
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
299-370 |
4.79e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 299 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LSAKNSTLKQLEEKL 356
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*
gi 321400107 357 KG-QADYEEVKKELN 370
Cdd:COG4913 695 EElEAELEELEEELD 709
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
108-248 |
4.96e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 39.29 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 108 LGQQLQLKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlknQAETialekEQKLQNDFAEKE 187
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 188 RKlqetqmsttsklEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 248
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-369 |
5.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 67 LLKSFQGEIDALSKRSKEAEA-------------AFLNVYKRLIDVPDPVPAL-DLGQQLQLKVQRLHDIETENQKLRET 132
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELrQLNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 133 L----------------------EEYNKEFAEVKNQEVTIKALKEKIREYEQTLkNQAETIAlekeQKLQNDfaekerkl 190
Cdd:PRK04863 867 LeqakeglsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIV----SVLQSD-------- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 191 qetqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKT--------KYDEETTAKADEIEMImtdlERANQRAEVAQREAE 262
Cdd:PRK04863 934 -------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLN----EKLRQRLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 263 TLREQLSSANHSLQLASQIQkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRL----------QASLTK------ 326
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVL--------------ASLKSSYDAKRQMLQELKQELQDLgvpadsgaeeRARARRdelhar 1068
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 321400107 327 LRENSaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 369
Cdd:PRK04863 1069 LSANR-SRRNQLEKQLTFCEAEMDNLTKKLrKLERDYHEMREQV 1111
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
277-373 |
5.88e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 277 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKL 356
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
|
90 100
....*....|....*....|.
gi 321400107 357 K--GQADYEEVKK--ELNILK 373
Cdd:COG2433 451 SeaRSEERREIRKdrEISRLD 471
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
141-310 |
5.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKVQSLQTALEKtRT 220
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 221 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 297
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 321400107 298 SLEVELAAKEREI 310
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
6.27e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 127 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKE-----QKLQNDFAEKERK-LQETQMSTTS 199
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEAIL--QADQALTEKEkeieaERAKAEAAEQERKlLEEQQRELEQ 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321400107 200 KLEEAEHkvqSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 270
Cdd:cd16269 227 KLEDQER---SYEEHLRQ-------LKEKMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
17-356 |
7.33e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 17 LQQLQRELDATATVLANRQDESEQSRKRlIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlNVYK 94
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREE-VEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 95 RLIDVPDPV-----------------------PAL------DLGQQL--------QLKVQ-----------RLHDIETEN 126
Cdd:PRK04778 186 ELTESGDYVeareildqleeelaaleqimeeiPELlkelqtELPDQLqelkagyrELVEEgyhldhldiekEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 127 QKLRETLEEYNKEFAEVKNQEvtikaLKEKIRE-YEQtlknqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAE 205
Cdd:PRK04778 266 DENLALLEELDLDEAEEKNEE-----IQERIDQlYDI----------LEREVKARK---------------------YVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 206 HKVQSLQTALEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQ 282
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EIT 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321400107 283 KAPDvEQAIevlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLsaknSTLKQLEEKL 356
Cdd:PRK04778 369 ERIA-EQEI---AYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-433 |
8.75e-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: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 115 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 195 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 262 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 341
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 342 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAlRISNSDlsgsa 421
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEE----- 541
|
330
....*....|..
gi 321400107 422 RRKGKDQPESRR 433
Cdd:pfam17380 542 RRKQQEMEERRR 553
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1275-1309 |
8.81e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 35.57 E-value: 8.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 321400107 1275 QQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSR 1309
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-381 |
9.20e-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: 40.87 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 125 ENQK--LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaetialekeqkLQNDFAEKE--RKLQETQMS-TTS 199
Cdd:pfam15921 102 EKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ-----------LQNTVHELEaaKCLKEDMLEdSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 200 KLEEAEHKVQSLQTALEKTRTELFDL-----KTKYDEET----------TAKADEIEMIMTDLERANQRAEVAQREAETL 264
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFeeasgKKIYEHDSmstmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321400107 265 ReqlSSANHSLQLASQiQKAPDVEQAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 344
Cdd:pfam15921 251 K---SESQNKIELLLQ-QHQDRIEQLI-----SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270
....*....|....*....|....*....|....*...
gi 321400107 345 KNSTLKQLEEKLK-GQADYEEVKKELNilKSMEFAPSE 381
Cdd:pfam15921 322 LESTVSQLRSELReAKRMYEDKIEELE--KQLVLANSE 357
|
|
| |
