|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1111-1188 |
6.44e-31 |
|
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: 116.54 E-value: 6.44e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 1111 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1188
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
928-996 |
4.60e-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: 108.45 E-value: 4.60e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 928 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 996
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
539-615 |
1.98e-27 |
|
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: 106.52 E-value: 1.98e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 539 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 615
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1234-1290 |
2.94e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 74.07 E-value: 2.94e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 1234 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1290
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-460 |
1.75e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.41 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 338 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQ 417
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES----K 909
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568937962 418 ISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEF 460
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1234-1291 |
1.02e-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: 66.88 E-value: 1.02e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 1234 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1291
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
236-452 |
2.66e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 236 KALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK---LQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAEleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 313 KYDEETTAKADEIEMIM---TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVE--LA 387
Cdd:COG1196 296 ELARLEQDIARLEERRReleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaeLA 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 388 AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKEL 452
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-447 |
4.46e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyEQTLKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 276 ---QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMimtdLERANQRAEVAQREAETLREQ 352
Cdd:COG1196 305 arlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 353 LSSANHSLQ--LASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 430
Cdd:COG1196 381 LEELAEELLeaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|....*..
gi 568937962 431 TLKQLEEKLKGQADYEE 447
Cdd:COG1196 461 LLELLAELLEEAALLEA 477
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1234-1289 |
6.14e-13 |
|
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: 64.58 E-value: 6.14e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 1234 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1289
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
143-517 |
5.74e-12 |
|
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: 70.10 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 143 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 216
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 217 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 277
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 278 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 351
Cdd:pfam05622 160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 352 QLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE----NSASQISQLEQQLNA 427
Cdd:pfam05622 236 TLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLgqegSYRERLTELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 428 KNSTLKQLEEKLKG--------QADYEEVKKELNtlksmefapSEGAGTQDST---KPLEVlLLEKNRSLQSENATLRIS 496
Cdd:pfam05622 316 ANRRKNELETQNRLanqrilelQQQVEELQKALQ---------EQGSKAEDSSllkQKLEE-HLEKLHEAQSELQKKKEQ 385
|
410 420
....*....|....*....|.
gi 568937962 497 NSDLSGPYSTNSISSPSPLQQ 517
Cdd:pfam05622 386 IEELEPKQDSNLAQKIDELQE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-716 |
6.49e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYNKE--FAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQNDFAEKERKLQETQ---MSTTS 284
Cdd:COG1196 216 RELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAEleAELEELRLELEELELELEEAQaeeYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 285 KLEEAEHKLQtlqtALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLAS 364
Cdd:COG1196 296 ELARLEQDIA----RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 365 QIQKApdvaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD 444
Cdd:COG1196 372 AELAE-----AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 445 YEEVKKELNTLKSMEFAPSEGAGTQDST--KPLEVLLLEKNRSLQSENATLRISNSDLSGPYST---NSISSPSPLQQSP 519
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALleAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaaLLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 520 DVN---GMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFghyvLGLSQGSVSEILARPKPWNKL---TV 593
Cdd:COG1196 527 AVLigvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF----LPLDKIRARAALAAALARGAIgaaVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 594 RGKEPFHKMKQFLSDEQNILALRSIQGRQRENPGQSLNRLFQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKRE 673
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568937962 674 LQVQKTAEPVQTSSTSSSGNSDDAIRSILQQARREMEAQQAAL 716
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-494 |
1.30e-11 |
|
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: 69.70 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 208 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 284
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 285 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQL----SSAN 357
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLeeleSKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 358 HSLQLASQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEE 437
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELE--SLEAELEELEAELEELESRLEELEEQLETLR----SKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937962 438 KLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 494
Cdd:TIGR02168 408 RLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-458 |
1.95e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918 388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDEETTA 320
Cdd:PRK03918 534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 321 KADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTRSSLEVELAAKEREIAQLVEDV 400
Cdd:PRK03918 608 KDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELSREL 675
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 401 QRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKgqaDYEEVKKELNTLKSM 458
Cdd:PRK03918 676 AGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
167-455 |
3.50e-11 |
|
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: 67.67 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 167 SKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 241
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 242 IREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTA 320
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 321 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-------PDVAI 374
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselnkVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 375 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK--GQADYEEV 448
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKdfMRARGYAH 537
|
....*..
gi 568937962 449 KKELNTL 455
Cdd:COG5185 538 ILALENL 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-457 |
5.34e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 143 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 219
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 220 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 297
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 298 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS-----ANHSLQLASQIQKAPDV 372
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkerDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 373 AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLEE-KLKGQADYEEVKKE 451
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKR 987
|
....*.
gi 568937962 452 LNTLKS 457
Cdd:TIGR02169 988 LDELKE 993
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-457 |
9.40e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 270
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 271 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQREAETLR 350
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 351 EQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNS 430
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIK-----KLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNLDN 461
|
250 260
....*....|....*....|....*..
gi 568937962 431 TLKQLEEKLKgqadyeEVKKELNTLKS 457
Cdd:TIGR04523 462 TRESLETQLK------VLSRSINKIKQ 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-401 |
1.37e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKR 180
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 181 LIDVpdpvpaldvGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAEti 256
Cdd:COG1196 297 LARL---------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeAEEELEEAEAELAEAEE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 257 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERAN 336
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE------EEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 337 QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQ 401
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-417 |
2.82e-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: 64.01 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 190 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 266
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 267 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 341
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 342 AQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 417
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
212-436 |
6.00e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 290
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 291 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkap 370
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE----- 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 371 dvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 436
Cdd:COG4913 381 --------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-456 |
6.36e-10 |
|
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: 64.32 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 197 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 276
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 277 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsa 356
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 357 nhslQLASQIQKApdvaieVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLE 436
Cdd:TIGR02169 326 ----KLEAEIDKL------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYR 391
|
250 260
....*....|....*....|
gi 568937962 437 EKLkgqadyEEVKKELNTLK 456
Cdd:TIGR02169 392 EKL------EKLKREINELK 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-457 |
7.31e-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: 63.89 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 270
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 271 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 348
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 349 lrEQLSSANHSLqLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLNAK 428
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKL 643
|
250 260 270
....*....|....*....|....*....|
gi 568937962 429 NSTLKQLEEKLKG-QADYEEVKKELNTLKS 457
Cdd:TIGR04523 644 KQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-368 |
1.21e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 275 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 568937962 351 EQLSSANHSLQLASQIQK 368
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-455 |
2.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtPEDLR-KQVAPLLKSFQGE-----IDALSKRSKEAEaaflT 176
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKlKELAEQLKELEEKlkkynLEELEKKAEEYE----K 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 177 VYKRLIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlks 251
Cdd:PRK03918 530 LKEKLIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 252 qaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTD 331
Cdd:PRK03918 600 -----FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLE 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 332 LERANQRAEVAQREAETLREQLSSanhslqlasqiqkapdvAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTK- 409
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKK-----------------TLEKLKEELEEREKAKKELEkLEKALERVEELREKVKKy 733
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 410 ---LRENSASQISQLEQQL-----NAKNS--TLKQLEEKLKGQADYEEVKKELNTL 455
Cdd:PRK03918 734 kalLKERALSKVGEIASEIfeeltEGKYSgvRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
121-440 |
2.80e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 60.31 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 121 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 197
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 198 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 277
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 278 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 357
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 358 HslqlasQIQKAPDVAIEVltrsslevelaakEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQLEE 437
Cdd:COG1340 216 K------EIVEAQEKADEL-------------HEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 568937962 438 KLK 440
Cdd:COG1340 275 KLK 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-465 |
7.93e-09 |
|
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: 59.39 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 303
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 304 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAiev 376
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 377 ltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKLKGQAdyEEVKKELNTLK 456
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTP 244
|
....*....
gi 568937962 457 SMEFAPSEG 465
Cdd:COG4942 245 AAGFAALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-458 |
9.19e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 157 QGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 236
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 237 ALKEKIREYEQTLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDE 316
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 317 ETTAKADEIEMIMT-----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVAIEVLT 378
Cdd:COG4717 243 ERLKEARLLLLIAAallallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 379 R--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEEVKK 450
Cdd:COG4717 323 EllAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKE 402
|
....*...
gi 568937962 451 ELNTLKSM 458
Cdd:COG4717 403 ELEELEEQ 410
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-457 |
9.62e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 227 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 299
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 300 LEKTRTELfdlktkydeettakadeiemimtdlERANQRAEVAQREAETLREQLssanhsLQLASQIQKAPDVAIEvltr 379
Cdd:COG4913 297 LEELRAEL-------------------------ARLEAELERLEARLDALREEL------DELEAQIRGNGGDRLE---- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 380 sSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLNAKNSTLKQLEEKL--------KGQAD 444
Cdd:COG4913 342 -QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALaeaeaalrDLRRE 420
|
250
....*....|...
gi 568937962 445 YEEVKKELNTLKS 457
Cdd:COG4913 421 LRELEAEIASLER 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
257-453 |
1.32e-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: 57.24 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 257 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 336
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 337 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVAIEVLTRssleveLAAKEREIAQLVEDVQRLQASLTKLRENS 414
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILELMER------IEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568937962 415 ASQISQLEQQLNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 453
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-401 |
3.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 180
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 181 lidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 260
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 261 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937962 338 RAEVAQREAETLREQLSSANHSLQLASQIqkapdvaIEVLTRSSLEVELAAKEREIAQLVEDVQ 401
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGYEAAIEAALGGRLQAVVVENLN 556
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-578 |
6.05e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 361 QLASQIQKAPDV---------------AIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 423
Cdd:COG3883 96 YRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 424 QLNAKNSTLKQLEEKLK-GQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 502
Cdd:COG3883 176 QQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 503 PYSTNSISSPSPLQQSPDVNGMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSV 578
Cdd:COG3883 256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGG 331
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
236-438 |
8.64e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.95 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 236 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 298
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 299 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 362
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 363 ASQIQKAPDVAIEVLTRSS----LEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQL 435
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKklleLKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 568937962 436 EEK 438
Cdd:PHA02562 399 VKE 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
191-458 |
9.18e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 191 LDVGQQLEIKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA----ETIA--LEKEQ 262
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 338
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 339 AEVAQREAETLREQLSsanhslQLASQI-QKAPDVAIEVLtrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSASQ 417
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIgQEIPSDEDILN----LQCETLVQEEE------------QFLSRLEEKSATL 844
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568937962 418 IsQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 458
Cdd:TIGR00618 845 G-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
143-335 |
9.59e-08 |
|
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: 55.45 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 568937962 300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
216-435 |
1.21e-07 |
|
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: 53.76 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 216 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 287
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 288 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 361 QlasqiQKApDVAIEVLTR--SSLEVELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLNAKNSTLKQL 435
Cdd:pfam13851 137 Q-----QKT-GLKNLLLEKklQALGETLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-443 |
1.24e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 110 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRlid 183
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 184 vPDPVPALDvgQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIAlEKEQK 263
Cdd:PRK02224 383 -REEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 264 LQ-NDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 340
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 341 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVAIEVLTRS-SLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSAS 416
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLEriRTLLAAIADAED 606
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568937962 417 QISQLEQQ--------------LNAKNSTLKQLEEKLKGQA 443
Cdd:PRK02224 607 EIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-438 |
1.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALE--- 259
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLglg 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 260 ------------------------------KEQKLQNDFAE-----KERKLQETQMS------------TTSKLEEAEHK 292
Cdd:COG4717 266 gsllsliltiagvlflvlgllallflllarEKASLGKEAEElqalpALEELEEEELEellaalglppdlSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 293 LQTLQTALEKTRTELFDLKTKYDEE------TTAKADEIEMIMTDLERANQRAEvAQREAETLREQLSSANHSLQLASQI 366
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQeiaallAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937962 367 QKAPDVAIEVltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLNAKNSTLKQLEEK 438
Cdd:COG4717 425 LDEEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
204-507 |
1.28e-07 |
|
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: 56.98 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKSqAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 276 -QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 354
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 355 SANHSLQLASQIQKAPDVAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQLNA 427
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVKGI 1215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 428 KNSTLKQLEEKLKGQADyEEVKKELNTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGPYSTN 507
Cdd:TIGR01612 1216 NLSYGKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIIS 1293
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
202-349 |
1.41e-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: 54.16 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKEQklqnDFAEKERK 274
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 275 LQETqmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 349
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
103-439 |
1.53e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.39 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YK 179
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 180 RLIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 259 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 337
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 338 RAEVAQREAETLREQLSSANHSLqLASQIQKAPD--------VAIEVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA 405
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDweqsigkvISPELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDV 592
|
330 340 350
....*....|....*....|....*....|....*
gi 568937962 406 -SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 439
Cdd:pfam12128 593 pEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-442 |
1.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 281
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 282 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 357
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 358 HSLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA-KNSTLKQLE 436
Cdd:COG4913 763 VERELRENLEER---------IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYE 833
|
....*.
gi 568937962 437 EKLKGQ 442
Cdd:COG4913 834 ERFKEL 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-457 |
2.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 258
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 259 EKEQ------------------KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYD-- 315
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEel 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 316 -------EETTAKADEIEMIMTDL-----ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLE 383
Cdd:PRK03918 358 eerhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 384 VELAAKE--------------REIAQLVEDVQRLQASLTKLREN-------------------SASQISQLEQQLNAKNs 430
Cdd:PRK03918 438 CPVCGRElteehrkelleeytAELKRIEKELKEIEEKERKLRKElrelekvlkkeseliklkeLAEQLKELEEKLKKYN- 516
|
330 340
....*....|....*....|....*..
gi 568937962 431 tLKQLEEKLKgqaDYEEVKKELNTLKS 457
Cdd:PRK03918 517 -LEELEKKAE---EYEKLKEKLIKLKG 539
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
116-459 |
2.57e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 116 LANRQDESEQSRKRLIEQSREF-----KKNTPEDLRKQVAPLlksfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 190
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakaKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 191 LD-VGQQLEIKVQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAET 255
Cdd:PRK03918 417 LKkEIKELKKAIEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEkerkLRKELRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 256 IALEK--------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK03918 496 IKLKElaeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 311 KTKYDEETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRS 380
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 381 SLEVELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKS 457
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
..
gi 568937962 458 ME 459
Cdd:PRK03918 736 LL 737
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
114-642 |
2.70e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 55.47 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 114 TVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEAEAAFLTVYKRLIDVPDPv 188
Cdd:COG5022 868 TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTELIARLKKLLNNIDLEEG- 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 189 PALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKS--------QAETIALEK 260
Cdd:COG5022 946 PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalQESTKQLKE 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 261 EQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmiM 329
Cdd:COG5022 1021 LPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--V 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 330 TDLERANQRAEVAQREAETLREQ-------------LSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAqL 396
Cdd:COG5022 1099 KDLEVTNRNLVKPANVLQFIVAQmiklnllqeiskfLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAA-L 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 397 VEDVQRLQASLTKLRENSASQISQLEQQLNAK------NSTLKQLEEKLKGQA-DYEEVKKELNTLKSMEFAPSEGAGtQ 469
Cdd:COG5022 1178 SEKRLYQSALYDEKSKLSSSEVNDLKNELIALfskifsGWPRGDKLKKLISEGwVPTEYSTSLKGFNNLNKKFDTPAS-M 1256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 470 DSTKPLEVL-LLEKNRSLQSENATLriSNSDLSGPYSTNSISSPSPLqqSPDVNGMAPSPSQSESAGSISEGEEIDTAEI 548
Cdd:COG5022 1257 SNEKLLSLLnSIDNLLSSYKLEEEV--LPATINSLLQYINVGLFNAL--RTKASSLRWKSATEVNYNSEELDDWCREFEI 1332
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 549 ARqVKEQLI------------KHNIGQ--RIFGhYVLGLSQGSVSEILARPKPWNKLTvrgkepfHKMKQFLsdeQNILA 614
Cdd:COG5022 1333 SD-VDEELEeliqavkvlqllKDDLNKldELLD-ACYSLNPAEIQNLKSRYDPADKEN-------NLPKEIL---KKIEA 1400
|
570 580
....*....|....*....|....*....
gi 568937962 615 LRSIQGRQRENPG-QSLNRLFQEVPKRRN 642
Cdd:COG5022 1401 LLIKQELQLSLEGkDETEVHLSEIFSEEK 1429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-355 |
2.81e-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: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 275 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 568937962 355 S 355
Cdd:COG4913 430 S 430
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
190-455 |
4.13e-07 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 53.81 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 190 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 264
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 265 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 344
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 345 eaetLREQLSSANHSLQ-------------------LASQI---------QKAPDVAI------EVLTRSSLEVELAAKe 390
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinIGKQVftitittatTKTVDVTSigglinGIGNASDDEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 391 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 455
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
210-561 |
4.27e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 210 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 286 LEEAEHKLQTLQTALEKTRTELFDLKTKyDEETTAKADEIEmimTDLERANQRAEVAQREAETLR--EQLSSANhslqlA 363
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKK-AEEDKKKAEEAK---KAEEDEKKAAEALKKEAEEAKkaEELKKKE-----A 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 364 SQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQlEEKLKGQA 443
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEK 1791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 444 DYEEVKKELNTLKSMEFAPSEGA--GTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGPYSTNSISSPSplqqspdv 521
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFANIIEGGkeGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED-------- 1863
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568937962 522 nGMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNI 561
Cdd:PTZ00121 1864 -GNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
235-460 |
5.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 235 IKALKEKIREYEqTLKSQAETIALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY 314
Cdd:COG4717 48 LERLEKEADELF-KPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 315 D-EETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVAIEVLTRSSLevelaAKEREI 393
Cdd:COG4717 126 QlLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------ELEAELAELQEELEELLEQLSL-----ATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 394 AQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEF 460
Cdd:COG4717 195 QDLAEELEELQQ-----------RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-458 |
5.60e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 181 LIDVPDPVPALDVGQQLEIKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKS 251
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 252 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLk 311
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 312 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVAIEVLTRSSLEVELA---- 387
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQLAELEAELAelsa 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 388 ----------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELN 453
Cdd:COG3206 285 rytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVE 361
|
....*
gi 568937962 454 TLKSM 458
Cdd:COG3206 362 VAREL 366
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
202-459 |
8.13e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYE----------QTLKSQAETIaLEKEQKLQND 267
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDElnaqVKELREEAQELRekrdelnekvKELKEERDEL-NEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 268 FAEKERKLQETQMSTTS------KLEEAEHKLQTLQTALEKTRtELFD----LKTKYDEetTAKADEIEmimTDLERANQ 337
Cdd:COG1340 94 LDELRKELAELNKAGGSidklrkEIERLEWRQQTEVLSPEEEK-ELVEkikeLEKELEK--AKKALEKN---EKLKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 338 RAEVAQREAETLREQLSsanhslQLASQIQKAPDvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLREnsasQ 417
Cdd:COG1340 168 ELKELRKEAEEIHKKIK------ELAEEAQELHE-------------EMIELYKEADELRKEADELHKEIVEAQE----K 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568937962 418 ISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 459
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-440 |
8.95e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 186 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 264
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 265 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 341
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 342 AQREAEtLREQLSS--ANHSLQLASQIQKapdvaievltrssLEVELAAKEREIA---QLVEDVQRLQASLTKLRENSAS 416
Cdd:PRK11281 169 SQRLQQ-IRNLLKGgkVGGKALRPSQRVL-------------LQAEQALLNAQNDlqrKSLEGNTQLQDLLQKQRDYLTA 234
|
250 260 270
....*....|....*....|....*....|.
gi 568937962 417 QISQLEQQL-------NAKNstLKQLEEKLK 440
Cdd:PRK11281 235 RIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
141-466 |
1.18e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 141 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFltvykrlidvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEE 220
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTAL--------------------KNARLDLRRLFD---EKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 221 YNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQt 295
Cdd:pfam12128 672 ALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 296 lQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapdva 373
Cdd:pfam12128 749 -LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA------------ 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 374 ievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQLEQQLNAKNSTLKQLEEKLKGQADYEEvkkELN 453
Cdd:pfam12128 814 ----------TQLSNIERAISELQQQLARLIAD-TKLR------RAKLEMERKASEKQQVRLSENLRGLRCEMS---KLA 873
|
330
....*....|...
gi 568937962 454 TLKsmEFAPSEGA 466
Cdd:pfam12128 874 TLK--EDANSEQA 884
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-456 |
1.35e-06 |
|
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: 53.29 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 273
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 274 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 351 EQLSSANHSLQ---------------LASQIQKAPDV------AIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASL 407
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMldvkerKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568937962 408 TklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 456
Cdd:pfam10174 432 S----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-353 |
2.06e-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: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 177
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 178 YKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTLKSQA 253
Cdd:TIGR02168 816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 254 ETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 331
Cdd:TIGR02168 887 EALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
|
250 260
....*....|....*....|..
gi 568937962 332 LERANQRAEVAQREAETLREQL 353
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-451 |
2.15e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLI 182
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEvtikALKEKIREyeqtLKSQAETIALEK 260
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKAD----EAKKKAEE----AKKKADEAKKAA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 261 EQKLQndfAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfDLKTKydeETTAKADEIEMImTDLERANQRAE 340
Cdd:PTZ00121 1507 EAKKK---ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD--ELKKA---EELKKAEEKKKA-EEAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 341 VAQREAETLR----------------------EQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVE 398
Cdd:PTZ00121 1578 MALRKAEEAKkaeearieevmklyeeekkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568937962 399 DVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 451
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
198-509 |
2.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 198 EIKVQRLHDIETENQKLRE-TLEEYNKEFAEVK-----------NQEVTIKALKEKIREYEQT---LKSQ------AETI 256
Cdd:PRK01156 383 SKNIERMSAFISEILKIQEiDPDAIKKELNEINvklqdisskvsSLNQRIRALRENLDELSRNmemLNGQsvcpvcGTTL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 257 ALEKEQKLQNDFAEKERKLQETQMST---TSKLEEAEHKLQTLQTALEKTRTElfDLKTKYDEETTAKADeIEMIMTDLE 333
Cdd:PRK01156 463 GEEKSNHIINHYNEKKSRLEEKIREIeieVKDIDEKIVDLKKRKEYLESEEIN--KSINEYNKIESARAD-LEDIKIKIN 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 334 RAnqraevaqREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVE-LAAKEREIAQLVEDV----QRLQASLT 408
Cdd:PRK01156 540 EL--------KDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIEtNRSRSNEIKKQLNDLesrlQEIEIGFP 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 409 KLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSmefAPSEGAGTQDSTKPLEVLLLEKNRSLQS 488
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLNNKYNEIQEN---KILIEKLRGKIDNYKK---QIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
330 340
....*....|....*....|.
gi 568937962 489 ENATLRISNSDLSGPYSTNSI 509
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEI 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-444 |
2.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykrli 182
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 dvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4913 688 ------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 KLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 341
Cdd:COG4913 750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 342 AQREAETL-------REQLSSANHS--LQLASQIQKAPDVAIEVLTR--SSLE---------VELAAKEREiaqlVEDVQ 401
Cdd:COG4913 822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIREIKERIDPlnDSLKripfgpgryLRLEARPRP----DPEVR 897
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568937962 402 RLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQAD 444
Cdd:COG4913 898 EFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEE 937
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
739-922 |
2.77e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 739 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 816
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 817 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 896
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 568937962 897 NSPLPSSPIVPMAKPAKPSVPPLTPE 922
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-713 |
2.78e-06 |
|
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: 52.15 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 197 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 262
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 334
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 335 ANQRAE---VAQREAETLREQLSSANHSL-----QLASQI------QKAPDVAIEVLTRSSLEVELAAKEREIAQL---- 396
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSRLgelklrLNQATATPELLLQLENFDERIERAREEQEAanae 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 397 VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQAdyeevkkelNTLksMEFAPSEGAGTQDST-KPL 475
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA---------GTL--LHFLRKEAPDWEQSIgKVI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 476 EVLLL-------EKNRSLQSENATLRISNSDLSGPYSTNSISSPSPLQQSPDVngmAPSPSQSESAgSISEGEEiDTAEI 548
Cdd:pfam12128 556 SPELLhrtdldpEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDK---AEEALQSARE-KQAAAEE-QLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 549 ARQVKEQLIKHNIGQRIFGHYVLGLSQGSVS-EILARPKpwNKLTVRGKEPFHKMKQFLSDEQNIL------ALRSIQGR 621
Cdd:pfam12128 631 NGELEKASREETFARTALKNARLDLRRLFDEkQSEKDKK--NKALAERKDSANERLNSLEAQLKQLdkkhqaWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 622 QRENPGQSLNRLfQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKRELqvqKTAEPVQTSSTSSSGNSDDAIRSI 701
Cdd:pfam12128 709 KREARTEKQAYW-QVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL---ASLGVDPDVIAKLKREIRTLERKI 784
|
570
....*....|..
gi 568937962 702 LQQARREMEAQQ 713
Cdd:pfam12128 785 ERIAVRRQEVLR 796
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-493 |
3.06e-06 |
|
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: 52.04 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 203 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKSQAETIALEKEQK----------LQND 267
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEIIQEQARNQnsmymrqlsdLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 348 TLREQlssanhslqlasqiQKAPDVAIEVLTRsslevELAAKEREiaqlvedVQRLQASLTKLRENSASQISQLEQQLNA 427
Cdd:pfam15921 402 RLWDR--------------DTGNSITIDHLRR-----ELDDRNME-------VQRLEALLKAMKSECQGQMERQMAAIQG 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 428 KNSTLKQ---LEEKLKGQADY-EEVKKELnTLKSMEFAPSEgagtqDSTKPLEVLLLEKNRSLQSENATL 493
Cdd:pfam15921 456 KNESLEKvssLTAQLESTKEMlRKVVEEL-TAKKMTLESSE-----RTVSDLTASLQEKERAIEATNAEI 519
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-453 |
4.13e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlKSQAETIALEKEQKLQNDFAEKERKLQETQMS 281
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN--LVQTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 282 T---TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 344
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 345 EAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElaakeREIAQlvedvQRLQASLTKLRE--NSASQISQLE 422
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS-----RSEAW-----DVARELLRRLREqrHLAEQLQQLR 519
|
250 260 270
....*....|....*....|....*....|.
gi 568937962 423 QQLNAknstlkqLEEKLKGQADYEEVKKELN 453
Cdd:PRK04863 520 MRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-459 |
4.31e-06 |
|
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: 51.65 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 104 KLKRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykrlid 183
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL-------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 184 vpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEKeQK 263
Cdd:pfam05483 445 -------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN-KE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 264 LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIMTDL 332
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 333 ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKA---------PDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRl 403
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK- 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937962 404 QASLTKLRENS-----------ASQISQLEQQLNA----KNSTLKQLEEKLKGQAD--YEEVKKELNTLKSME 459
Cdd:pfam05483 662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-454 |
5.13e-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: 51.51 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 210 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 286
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 287 EEAEhKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI 366
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 367 QKAPDVAIE---------VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 437
Cdd:pfam02463 330 LKKEKEEIEelekelkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250
....*....|....*..
gi 568937962 438 KLKGQADYEEVKKELNT 454
Cdd:pfam02463 410 LLELARQLEDLLKEEKK 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
208-459 |
5.62e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 208 ETENQKLRETLEEYNKEFAEVKnqevtikalkEKIREYEqtlkSQAETiALEKEQKLQNDFAEKERKLQETQmsttsKLE 287
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELD----------EEIERYE----EQREQ-ARETRDEADEVLEEHEERREELE-----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 288 EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQ 367
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 368 KAPDVAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLNAKNSTLKQLEEKLKGQADY- 445
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNAEDFl 414
|
250
....*....|....
gi 568937962 446 EEVKKELNTLKSME 459
Cdd:PRK02224 415 EELREERDELRERE 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-447 |
7.31e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 111 ATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpA 190
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEI-----EDLRETIAETER----EREELAEEVRDLRERLEELEEERDDLLAEA-G 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 191 LDVGQQlEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlksqaetialEKEQKLQNDFAE 270
Cdd:PRK02224 304 LDDADA-EAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 271 KERKLQETQMSTT---SKLEEAEHKLQTLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:PRK02224 368 LESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 348 TLREQ---------LSSANHSLQLASQIQKAPDVAIEvltRSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQI 418
Cdd:PRK02224 447 ALLEAgkcpecgqpVEGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLE 522
|
330 340
....*....|....*....|....*....
gi 568937962 419 SQLEQQLNAKNSTLKQLEEKLKGQADYEE 447
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEA 551
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-421 |
7.37e-06 |
|
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: 50.84 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 104 KLKREL-DATATVLANRQDESEQSRKRLIEQSrefkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:TIGR02169 215 ALLKEKrEYEGYELLKEKEALERQKEAIERQL--------ASLEEE----LEKLTEEISELEKRLEEIE-------QLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKvQRLHDIETENQKLRETLEEYNKE-----------FAEVKNQEVTIKALKEKIREY------ 245
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-EKIGELEAEIASLERSIAEKEREledaeerlaklEAEIDKLLAEIEELEREIEEErkrrdk 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 246 -----------EQTLKSQAETIA----------------LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLqtlqT 298
Cdd:TIGR02169 355 lteeyaelkeeLEDLRAELEEVDkefaetrdelkdyrekLEKLKREINELKRELDRLQEELQRLSEELADLNAAI----A 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 299 ALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhslqlaSQIQKapdvaievlT 378
Cdd:TIGR02169 431 GIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY----------DRVEK---------E 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568937962 379 RSSLEVELAAKEREiAQLVEDVQRLQASLTKLRENSAS----QISQL 421
Cdd:TIGR02169 485 LSKLQRELAEAEAQ-ARASEERVRGGRAVEEVLKASIQgvhgTVAQL 530
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-502 |
7.77e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 213 KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTL--KSQAETIALEKEQKLQN---DFAEKERKLQETQMSTT---- 283
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEeelKLLAKEEEELKSELLKLerrk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 284 ----SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:pfam02463 310 vddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-EELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 360 LQLASQIQKAPDVaiEVLTRSSLEVELAAKEREIAQLvedvqrlqASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 439
Cdd:pfam02463 389 AAKLKEEELELKS--EEEKEAQLLLELARQLEDLLKE--------EKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937962 440 KGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 502
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-493 |
9.17e-06 |
|
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: 50.43 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 295 TlqtalektrtelfdlktkydeETTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVA 373
Cdd:TIGR00606 312 R---------------------TVREKERELVDCQRELEKLNKeRRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 374 IEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLrenSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 451
Cdd:TIGR00606 371 QSLATRLELDGfeRGPFSERQIKNFHTLVIERQEDEAKT---AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568937962 452 LNTLK--SMEFAPSEGAGTQDSTKPlevlLLEKNRSLQSENATL 493
Cdd:TIGR00606 448 ILEKKqeELKFVIKELQQLEGSSDR----ILELDQELRKAEREL 487
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
212-459 |
1.07e-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: 50.50 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMSTTS------- 284
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKlrsrvdl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 285 KLEEAEHkLQTLQTALEKTRTELFDLK---TKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ 361
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKlqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 362 LASQIQKAPDVAIEVLTRSSLEVEL-------AAKER---------EIAQLVEDVQRLQASLTKLRENsasqISQLEQQL 425
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELekvklvnAGSERlravkdikqERDQLLNEVKTSRNELNSLSED----YEVLKRNF 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 568937962 426 NAKNSTLKQLEEKLKGQ--ADYEEVKKELNTLKSME 459
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQlkSAQSELEQTRNTLKSME 719
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
135-473 |
1.16e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 135 REFKKNTpEDLRKQVAPLLksfqgeIDALSKRSKEAEAAFLTVYKRlidvpdpvpalDVGQQLEIKVQrlhdIETENqkL 214
Cdd:pfam05483 229 EEYKKEI-NDKEKQVSLLL------IQITEKENKMKDLTFLLEESR-----------DKANQLEEKTK----LQDEN--L 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI-ALEKEQKLQNDFAEKER---------------KLQET 278
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcQLTEEKEAQMEELNKAKaahsfvvtefeattcSLEEL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 279 QMSTTSKLEEAEHKLQTLQTALEKTRTELFDLkTKYDEETTAKADEIEMIMTDleraNQRAEVAQREAETLREQLSSANH 358
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVELEELKKILAE----DEKLLDEKKQFEKIAEELKGKEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 359 SLQ--LASQIQKAPDVAIEV-LTRSS----------LEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQL 425
Cdd:pfam05483 440 ELIflLQAREKEIHDLEIQLtAIKTSeehylkevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568937962 426 NAKNSTLKQLEEKLKGQADYEEvkKELNTLKSMEFAPSEGAGTQDSTK 473
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEE--KEMNLRDELESVREEFIQKGDEVK 565
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-450 |
1.45e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEeTTAKADEIEMI----MTDLERANQRAEVAQREAEtlREQLSSA 356
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLaeysWDEIDVASAEREIAELEAE--LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 357 NHSL-QLASQIQKapdvaievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQ- 434
Cdd:COG4913 684 SDDLaALEEQLEE-------------LEAELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLe 746
|
170 180
....*....|....*....|
gi 568937962 435 ----LEEKLKGQADYEEVKK 450
Cdd:COG4913 747 lralLEERFAAALGDAVERE 766
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-457 |
1.85e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKSQaETIALEKEQKLQND--FAEK 271
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 272 ERKLQETQMSTT----SKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQraeva 342
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEkqkkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEElENELNLLEKEKLNI----- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 343 QREAETLREQLSSANHSL-QLASQIQKAPDVAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 417
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISelkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568937962 418 ISQLE---QQLNAKNSTLKQLEEKLKgqadyeEVKKELNTLKS 457
Cdd:TIGR04523 266 KKQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
203-312 |
2.17e-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: 48.09 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 568937962 277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
127-438 |
2.22e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 127 RKRLIEQSREFKKntpeDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaldvgQQLEiK 200
Cdd:COG3096 280 RRELSERALELRR----ELFGARRQLaeeqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL------RQQE-K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 201 VQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKE 272
Cdd:COG3096 349 IERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 273 RKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE---- 340
Cdd:COG3096 427 ALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARellr 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 341 -------VAQReAETLREQLSSANhslQLASQIQKAPDVAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTKLRE 412
Cdd:COG3096 503 ryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAEAVE 578
|
330 340
....*....|....*....|....*.
gi 568937962 413 nsasQISQLEQQLNAKNSTLKQLEEK 438
Cdd:COG3096 579 ----QRSELRQQLEQLRARIKELAAR 600
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
157-457 |
2.32e-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: 49.05 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 157 QGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL-----DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 232 evtIKALKEKIREYEQTLKSQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELF 308
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 309 DLKtkydEETTAKADEieMIMTDLERANQRAEVAQREAETLReqlssanhslqLASQIQKAPDVAIEVLTRSSLEVELAA 388
Cdd:pfam10174 500 DLK----EHASSLASS--GLKKDSKLKSLEIAVEQKKEECSK-----------LENQLKKAHNAEEAVRTNPEINDRIRL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 389 KEREIAQLVEDVQRLQASLTKL------RENSAS----QISQLE---------QQLNAKNSTLKQLEEKLKGQADYEEVK 449
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLlgilreVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
....*...
gi 568937962 450 KELNTLKS 457
Cdd:pfam10174 643 RREDNLAD 650
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
306-456 |
2.36e-05 |
|
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: 48.70 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 306 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKAPDVAIEVLTRSSL 382
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILEELDELLESEEKNRE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937962 383 EVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 456
Cdd:pfam06160 122 EVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
289-585 |
2.58e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 289 AEHKLQTLQTALEKTRTELFDLKTKYDeettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI-- 366
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 367 QKAPDVAIEVLTRSSLEVELAAKEreiaqLVEDVQRLQAsLTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYE 446
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSES-----FSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAK---LAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 447 EVKKELNTLKS-MEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGPYSTNSISSPSPLQQSPDVNGMA 525
Cdd:COG3883 161 ALKAELEAAKAeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 526 PSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARP 585
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
211-436 |
2.62e-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: 48.98 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 211 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 290 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlaS 364
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--A 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 365 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---------ASLTKLRENSASQISQL-EQQLNAKNSTLKQ 434
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQedradlqatVELLQVRVQSLTHMLALqEEELTRKIQPSDS 295
|
..
gi 568937962 435 LE 436
Cdd:pfam07111 296 LE 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-331 |
3.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrli 182
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 dvPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQ 262
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 263 KLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-461 |
3.40e-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: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KSQAETIALE-KEQKLQNDFAEKERKLQE 277
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 278 TQMSTTSKleeaEHKLQTLQTALEKTRTEL------FDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam10174 329 LKESLTAK----EQRAAILQTEVDALRLRLeekesfLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 348 TLREQLSSANhslqlaSQIQKAPDVAIEVLTRSS--------LEVELAAKEREIAQLVE-----DVQRLQ--ASLTKLRE 412
Cdd:pfam10174 405 NLQEQLRDKD------KQLAGLKERVKSLQTDSSntdtalttLEEALSEKERIIERLKEqrereDRERLEelESLKKENK 478
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568937962 413 NSASQISQLEQQLNAKNSTLKQLEEKLKGQADyEEVKKElNTLKSMEFA 461
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1234-1319 |
4.14e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 1234 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1313
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 568937962 1314 RSSRAA 1319
Cdd:COG5576 121 EEADLA 126
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-322 |
4.84e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 116 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL 191
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDF 268
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568937962 269 AEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 322
Cdd:COG3206 337 AQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
199-410 |
6.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 199 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 275 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlERANQRAEvA 342
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EIMDEFNE-Q 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 343 QREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 410
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
121-452 |
6.40e-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: 47.66 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 121 DESEQSRKRLIEQSREFK-KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvPALDVGQQLEI 199
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR------------EALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 200 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEK--------EQKLQNDFAEK 271
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqriHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 272 ERKLQETQ--MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADE--IEMIMTDLERANQRAEVAQREAE 347
Cdd:TIGR00618 324 AKLLMKRAahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 348 TLREQLSSAN--HSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasqisqLEQQL 425
Cdd:TIGR00618 404 ILQREQATIDtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE--------REQQL 475
|
330 340
....*....|....*....|....*..
gi 568937962 426 NAKNSTLKQLEEKLKGQADYEEVKKEL 452
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
301-457 |
6.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 301 EKTRTELFDLKTKYDEETTAKAdEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLT-- 378
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLRE-ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQee 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 379 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEKLKgQADYEEVKKELNTL 455
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEreeELKELEEQLESLQEELAALEQELQ-ALSEAEAEQALDEL 188
|
..
gi 568937962 456 KS 457
Cdd:COG4372 189 LK 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-459 |
8.32e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKlqndfAEKERKLQEtqmstt 283
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 284 skLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 364 SQIQKapdVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLNAKNSTLKQLEEKLKGQA 443
Cdd:PRK03918 286 KELKE---KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLE 355
|
250
....*....|....*.
gi 568937962 444 DYEEVKKELNTLKSME 459
Cdd:PRK03918 356 ELEERHELYEEAKAKK 371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-437 |
9.48e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 207 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 286
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 287 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 349
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 350 REQLSSANHSLQLASQIQKApdvaIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKN 429
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ----LAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTV 385
|
....*...
gi 568937962 430 STLKQLEE 437
Cdd:COG3206 386 GNVRVIDP 393
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
226-442 |
1.57e-04 |
|
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: 44.98 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 226 AEVKNQEVTIKALKEKIREYEQTL----KSQAETIALEKEQKLQNDFAEKERKLQE------TQMSTTSKLEEAEHKLQT 295
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALslldKIDASKQRAAAYQKALDDAPAELRELRQelaalqAKAEAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 296 LQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaie 375
Cdd:pfam12795 83 LEQRLLQTSAQLQELQNQLAQLN----SQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQ-------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 376 vltRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 442
Cdd:pfam12795 151 ---RWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
701-946 |
1.58e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 701 ILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEA 780
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 781 QDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQG 860
Cdd:PRK10263 363 VPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 861 PSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLtpeqyevYMYQEVD 933
Cdd:PRK10263 442 VAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL-------YYFEEVE 513
|
250
....*....|...
gi 568937962 934 tiELTRQVKEKLA 946
Cdd:PRK10263 514 --EKRAREREQLA 524
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
249-451 |
1.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 249 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 327
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 328 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvaievltrsslEVELAAKEREIAQLVEDVQRLQASL 407
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-----------------------EEELEKKEKELEQKQQELEKKEEEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568937962 408 TKLREnsaSQISQLEQ--QLN---AKNSTLKQLEEKLKGQA-----DYEEVKKE 451
Cdd:PRK12704 134 EELIE---EQLQELERisGLTaeeAKEILLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-447 |
1.69e-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: 46.32 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 208 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 352
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 353 LSsaNHSLQLASQIQKAPDVAI------------------EVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--- 411
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAKSLSKlknkheamisdleerlkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaql 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568937962 412 ----ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 447
Cdd:pfam01576 239 akkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-456 |
1.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKEQ 262
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 343 QREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI---- 418
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAleeq 729
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568937962 419 ------SQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 456
Cdd:COG1196 730 leaereELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
106-500 |
1.85e-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: 45.89 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 106 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 174
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 175 ----LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 242
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 243 REYEQTLKSQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKLQTLQTALEKTRTELfdlktkYDEETTAKA 322
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 323 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVAIEVLTRSSLEVELAAKEREIAQLVEDVQ 401
Cdd:pfam05557 271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 402 RLQASLTKLRENSASQISQLEQQLNAKNSTlKQLEEKLKGQADY-EEVKKELNTLK-SMEFAPSEGAGTQDSTKPLEVLL 479
Cdd:pfam05557 346 RRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLEREL 424
|
410 420 430
....*....|....*....|....*....|....*.
gi 568937962 480 LEKNR---------------SLQSENATLRISNSDL 500
Cdd:pfam05557 425 QALRQqesladpsyskeevdSLRRKLETLELERQRL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-351 |
2.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 145 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 215
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 216 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 289
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937962 290 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 351
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-456 |
2.12e-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: 46.19 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 108 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLR----------KQVAPLLKSFQGEIDALSKRSKE---AEAAF 174
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELVDCQRELEKLNKERRLlnqEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 175 LTVYKRLIDVPDPVPALDVGQQLEIKVQRLH------------DIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKE 240
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfsERQIKNfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 241 K-IREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQ--ETQMSTTSKLEEAEHK-LQTLQTALEKTRTElfdlkTKY 314
Cdd:TIGR00606 426 EqADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQqlEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 315 DEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLT--------RSSLEVEL 386
Cdd:TIGR00606 501 KEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTsllgyfpnKKQLEDWL 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 387 AAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 456
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
113-495 |
2.90e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 113 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 192
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 271
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 272 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 345
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 346 AETLREQLSSanhslqLASQiqkapdvaievltRSSLEVELAAKEREIAQLveDVQRLQASLtKLRENSASQISQLEQQL 425
Cdd:pfam07888 253 VEGLGEELSS------MAAQ-------------RDRTQAELHQARLQAAQL--TLQLADASL-ALREGRARWAQERETLQ 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937962 426 NA----KNSTLKQLEEKLKGQADYEEVKKELNTLKsmefapSEGAGTQDSTKpleVLLLEKNRSLQSENATLRI 495
Cdd:pfam07888 311 QSaeadKDRIEKLSAELQRLEERLQEERMEREKLE------VELGREKDCNR---VQLSESRRELQELKASLRV 375
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
202-307 |
3.62e-04 |
|
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: 43.36 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 265
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568937962 266 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 307
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
108-444 |
3.83e-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: 45.17 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 108 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP 185
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 186 DPVPalDVGQQLEIKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 259 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 325
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 326 EMIMTDLERANQRAEVAQREAETlreqlssanHSLQLASQIQKAPDvaievlTRSSLEVELAAKEREIAQLV---EDVQR 402
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKET---------RALSLARALEEALE------AKEELERTNKQLRAEMEDLVsskDDVGK 678
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568937962 403 LQASLTKLREnsasqisQLEQQLNAKNSTLKQLEEKLKGQAD 444
Cdd:pfam01576 679 NVHELERSKR-------ALEQQVEEMKTQLEELEDELQATED 713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-459 |
4.08e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 118 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDVPDPVPALDVGQQL 197
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA--EEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 198 EIKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALK----EKIREYEQTLKSQAETIALEKEQKLQN-DF 268
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEvrkaEELRKAEDARKAEAARKAEEerkaEEARKAEDAKKAEAVKKAEEAKKDAEEaKK 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 269 AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ--RAEVAQREA 346
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 347 ETLREQLSSANHSlqlASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 426
Cdd:PTZ00121 1325 EEAKKKADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350
....*....|....*....|....*....|...
gi 568937962 427 AKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 459
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
157-441 |
4.45e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 157 QGEIDALSKRSKEAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 232
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 233 vtiKALKEKIREYEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQ 297
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 298 TALEKTRTeLFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APD- 371
Cdd:PRK04863 527 QRLRQQQR-AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAw 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 372 -VAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQLEEKLKG 441
Cdd:PRK04863 606 lAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-317 |
4.71e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDv 193
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE- 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 194 gQQLEIKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKS----QAETIALEKEQKLQNDFA 269
Cdd:TIGR02169 896 -AQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568937962 270 EKERKLQETQMSTTSKLEEAEHKLQTLQ---TALEKTRTELFDLKTKYDEE 317
Cdd:TIGR02169 965 EEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
114-502 |
4.83e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 114 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDvpdpvpaldv 193
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 194 gqqleikvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKER 273
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 274 KLQETQMSTTSKLEEAEHKLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 341
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 342 AQREAETLREQLSSANHslQLASQIQKAPDVAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRLQA 405
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQREAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRMDL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 406 SLTKLREnSASQISQLEQQLN-----------------AKNSTLKQLEEKLKGQA-DYEEVKKELNTLK---SMEFAPSE 464
Cdd:PRK10929 284 IASQQRQ-AASQTLQVRQALNtlreqsqwlgvsnalgeALRAQVARLPEMPKPQQlDTEMAQLRVQRLRyedLLNKQPQL 362
|
410 420 430
....*....|....*....|....*....|....*....
gi 568937962 465 GAGTQDSTKPLEVlllEKNRSLQSENATLR-ISNSDLSG 502
Cdd:PRK10929 363 RQIRQADGQPLTA---EQNRILDAQLRTQReLLNSLLSG 398
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
196-494 |
4.88e-04 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 43.82 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 196 QLEIKVQRLhDIET-ENQKLRETlEEYNKEfaevknqevtIKALKEKIREYEQTLKSQAETIA---LEKEQKLQNDFAEK 271
Cdd:pfam14915 5 QDEIAMLRL-EIDTiKNQNQEKE-KKYLED----------IEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 272 ERklqetqmsTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLRE 351
Cdd:pfam14915 73 TM--------LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 352 QLSSanhslQLASQIQKapdvaIEVLTRsslevELAAKEREIAQLVEDVQRLQASltkLRENSaSQISQLEQQLNAKNST 431
Cdd:pfam14915 134 KMNF-----DVSNLRDE-----NEILSQ-----QLSKAESKANSLENELHRTRDA---LREKT-LLLESVQRDLSQAQCQ 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937962 432 LKQLEEKLkgQADYEEVKKELNTLKSMEfapsegagtqdstkplevlllEKNRSLQSENATLR 494
Cdd:pfam14915 195 KKELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
193-333 |
5.05e-04 |
|
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: 42.38 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 193 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlksQAETialekEQKLQNDFAEKE 272
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 273 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 333
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
214-440 |
5.18e-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: 44.30 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 214 LRETLEEYNKEFAEVknqevtIKALKEKIREYEQTLKSQAETIAL------EKEQKLQNDFAEkERKLQETQMSTTSKLE 287
Cdd:pfam04108 54 LEKVLNELKKDFKQL------LKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLLDFID-EDSVEILRDALKELID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 288 EAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEAETLREQLssANH---SLQLAS 364
Cdd:pfam04108 127 ELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EMASLLESL--TNHydqCVTAVK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 365 QIQKAPDVAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLE 436
Cdd:pfam04108 200 LTEGGRAEMLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALKEFE 279
|
....
gi 568937962 437 EKLK 440
Cdd:pfam04108 280 ERWE 283
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-493 |
5.22e-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: 44.65 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKireyeqtlKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR--------KKQMEKDNSELELKMEKVFQGTDEQL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 276 QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 356 ANHSLQLASQIQKAPDVAIEVLTR-----SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 430
Cdd:TIGR00606 382 FERGPFSERQIKNFHTLVIERQEDeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 431 TLKQLEEKLKG--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 493
Cdd:TIGR00606 462 ELQQLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
218-436 |
5.68e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 218 LEEYNKEFAEVKNQEVTIKALKEKIReyeQTLK--SQAETIALEKEQKLQNDFAEKERKLQETQmsttskleeaehkLQT 295
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKLI---ASLKegSGVEGLDSSTALTLELEELRQERDLLREE-------------IQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLasqiqkapdvaie 375
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRR------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 376 vlTRSSLEVELAAKEREIaqlvedvQRLQASLTkLRENSASQISQLEQQLNA------------------KNSTLKQLE 436
Cdd:pfam09787 133 --SKATLQSRIKDREAEI-------EKLRNQLT-SKSQSSSSQSELENRLHQltetliqkqtmlealsteKNSLVLQLE 201
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
722-922 |
6.13e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 722 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 801
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 802 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 881
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568937962 882 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 922
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
197-459 |
6.14e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 197 LEIKVQRLHDIETENQKLRETLEEynKEFAEVKNQEVTIKALKEK------IREYEQTL--KSQAETIALEKEQKLQNDF 268
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEE--KESFLNKKTKQLQDLTEEKstlageIRDLKDMLdvKERKINVLQKKIENLQEQL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 269 AEKERKLQETQMSTTSkLEE----AEHKLQTLQTAL-EKTRTeLFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ 343
Cdd:pfam10174 411 RDKDKQLAGLKERVKS-LQTdssnTDTALTTLEEALsEKERI-IERLKEQREREDRERLEELESLKKENKDLKEKVSALQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 344 REaetLREQLSSANHSLQLASQIqkAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQISQL 421
Cdd:pfam10174 489 PE---LTEKESSLIDLKEHASSL--ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLL 563
|
250 260 270
....*....|....*....|....*....|....*...
gi 568937962 422 EQQLNAKNstlkqlEEKLKGQAdyeEVKKELNTLKSME 459
Cdd:pfam10174 564 EQEVARYK------EESGKAQA---EVERLLGILREVE 592
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
202-426 |
6.62e-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: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKsQAETIALEKEQKL-----QNDFAEKERK-L 275
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAE---VAALNRRIQLLEEELE-RTEERLAEALEKLeeaekAADESERGRKvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 276 QETQMSTTSKLEEAEHKL-QTLQTALEKTRtelfdlktKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLkEAKEIAEEADR--------KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 355 SANHSLQ-LASQIQKAPD------VAIEVLTRSSLEVELAAK--EREIAQLVEDVQRLQASLTKLRENSASQISQLEQQL 425
Cdd:pfam00261 152 VVGNNLKsLEASEEKASEredkyeEQIRFLTEKLKEAETRAEfaERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTL 231
|
.
gi 568937962 426 N 426
Cdd:pfam00261 232 A 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
216-473 |
8.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 216 ETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKER------------KLQETQMSTT 283
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDnradeateeafgKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 284 SKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDEETTAKADEIEMIMTDLERAnQRAEVAQREAETLREQLSSANHSL 360
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 361 QLASQIQKAPDV-AIEVL-----TRSSLEVELAAKEREIAQL--VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 432
Cdd:PTZ00121 1188 RKAEELRKAEDArKAEAArkaeeERKAEEARKAEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568937962 433 KQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTK 473
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
196-444 |
9.01e-04 |
|
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: 43.74 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 196 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 273
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 346
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 347 ETLREQLSSANHSLQLASQ----IQK--APDVAIEVLTRSSLEVELAAK-----------ERE-----------IAQLVE 398
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLekesIQQsfSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568937962 399 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 444
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
122-439 |
9.49e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 122 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlTVYKRLIDVPDPVPALDVGQQLEI 199
Cdd:PRK04778 133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVEAREILDQLEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 200 KV------------------------------------------------QRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:PRK04778 206 ELaaleqimeeipellkelqtelpdqlqelkagyrelveegyhldhldieKEIQDLKEQIDENLALLEELDLDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 232 EvtikaLKEKIRE-YEQtlksqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK04778 286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 311 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQLASQIQKAPDVAIevltrSSLEVELA 387
Cdd:PRK04778 330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYDEITERIAEQEIAY-----SELQEELE 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 388 AKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLnaknSTLKQLEEKL 439
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-459 |
9.67e-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: 43.88 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 125 QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKrlidvpdpvpaldvgqqLE 198
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEHNLSKIMK-----------------LD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 199 IKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----KIREYEQTL-KSQAETIALEKEQKLQNdfaeKER 273
Cdd:TIGR00606 269 NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrTVREKERELvDCQRELEKLNKERRLLN----QEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 274 KLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDEETTAK----------ADEIEMIMTDLERANQRA 339
Cdd:TIGR00606 343 TELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnfhtlvierqEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 340 EVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLRENSASQiS 419
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK-FVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSLTE-T 498
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568937962 420 QLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 459
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-456 |
9.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 382 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 439
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 568937962 440 KG-QADYEEVKKELNTLK 456
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
203-547 |
1.06e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 282
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 283 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQRAEvAQREAETLREqlSSANHS 359
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKPK-LKKKEKKKKK--SSADKS 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 360 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 439
Cdd:PTZ00108 1190 KKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 440 KGQADYEE---VKKELNTLKSMEFAPSEGAGTQDST------KPLEVLLLEKNRSLQSENATLRISNSDlsgpysTNSIS 510
Cdd:PTZ00108 1270 KPKNAPKRvsaVQYSPPPPSKRPDGESNGGSKPSSPtkkkvkKRLEGSLAALKKKKKSEKKTARKKKSK------TRVKQ 1343
|
330 340 350
....*....|....*....|....*....|....*..
gi 568937962 511 SPSPLQQSPdvngmAPSPSQSESAGSISEGEEIDTAE 547
Cdd:PTZ00108 1344 ASASQSSRL-----LRRPRKKKSDSSSEDDDDSEVDD 1375
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1253-1287 |
1.07e-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: 37.88 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|....*
gi 568937962 1253 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1287
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
119-457 |
1.09e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 119 RQDESEQSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRLIDVPdPVP 189
Cdd:pfam05667 241 RKRKRTKLLKRIAEQLRSAALAGTEatsGASRSAQDLAELLSsfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAAT-SSP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 190 ALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ-KLQNDF 268
Cdd:pfam05667 320 PTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTlDLLPDA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 269 AEKERKLQetqmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqraevaqreaet 348
Cdd:pfam05667 400 EENIAKLQ-------ALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKE-------------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 349 LREQlssanhslqlasqIQKAPDvaievltrsslevELAAKEREIAQLVEDVQRLQasltklRENSASQISQ--LEQQLN 426
Cdd:pfam05667 459 LREK-------------IKEVAE-------------EAKQKEELYKQLVAEYERLP------KDVSRSAYTRriLEIVKN 506
|
330 340 350
....*....|....*....|....*....|.
gi 568937962 427 AKnstlKQLEEKLKGQADYEEVKKELNTLKS 457
Cdd:pfam05667 507 IK----KQKEEITKILSDTKSLQKEINSLTG 533
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
212-302 |
1.13e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 40.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 280
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 568937962 281 STTSKLEEAEHKLQTLQTALEK 302
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
204-490 |
1.19e-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: 43.56 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQETQM 280
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 281 STTSKLEE--AEHKL-----QTLQTALEKTRtelfdlKTKYDEETTAKA-----DEIEMIMTDLERANQRAEVAQREAE- 347
Cdd:pfam05483 142 ENKDLIKEnnATRHLcnllkETCARSAEKTK------KYEYEREETRQVymdlnNNIEKMILAFEELRVQAENARLEMHf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 348 TLREQLSSANHslqLASQIQKapdvaievltrsslevELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQ 423
Cdd:pfam05483 216 KLKEDHEKIQH---LEEEYKK----------------EINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEE 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 424 QLNAKNSTLKQLEEKLKG-QADYEEVKKELNtlKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSEN 490
Cdd:pfam05483 276 KTKLQDENLKELIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
113-506 |
1.23e-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: 43.50 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 113 ATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ---VAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRL 181
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLlgtIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 182 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREyeqtLKSQAETIALEKE 261
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----------IQHLKSKTNE----LKSEKLQIGTNLQ 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 262 QKLQndFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 331
Cdd:TIGR00606 882 RRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 332 LERANQraEVAQREAETLREQLSSANHSLQLASQIQK---------APDVAIEVLTRSSLEVELAAKEREiAQLVEDVQR 402
Cdd:TIGR00606 960 IENKIQ--DGKDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmRQDIDTQKIQERWLQDNLTLRKRE-NELKEVEEE 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 403 LQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT-LKSMEFAPSEgagtqdstkplevlll 480
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIKHFKKeLREPQFRDAE---------------- 1100
|
410 420
....*....|....*....|....*.
gi 568937962 481 EKNRSLQSENATLRISNSDLSGPYST 506
Cdd:TIGR00606 1101 EKYREMMIVMRTTELVNKDLDIYYKT 1126
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
212-355 |
1.28e-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: 42.56 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 286
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937962 287 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 355
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
296-456 |
1.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIE 375
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 376 VL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsQISQLEQQLNAK-----NSTLKQLEEKLKgqaDYE 446
Cdd:COG4717 127 LLplyqELEALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELleqlsLATEEELQDLAE---ELE 202
|
170
....*....|
gi 568937962 447 EVKKELNTLK 456
Cdd:COG4717 203 ELQQRLAELE 212
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
227-395 |
2.05e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 227 EVKNQEVTIKALKEKIREYEQTLksqaetiALEKEQKLQndfaekerkLQETQMSTTSKLEEAEH---KLQTLQTALEKT 303
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLL-------SLERQGNQD---------LQDSVANLRASLSAAEAersRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 304 RTELfdlkTKYDEETTAKADEIEMIMtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsSLE 383
Cdd:PRK09039 111 GAAA----EGRAGELAQELDSEKQVS---ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGR-RLN 182
|
170
....*....|..
gi 568937962 384 VELAAKEREIAQ 395
Cdd:PRK09039 183 VALAQRVQELNR 194
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
262-449 |
2.12e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 262 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYDEETTAKAdeiemimtdleranqR 338
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrkLRETQNTLNQLNKQIDELNASIA---------------K 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 339 AEVAQREAET-LREQLSSA----NHS-LQL-----ASQ-----------IQKAPDVAIEVLTRSSleVELAAKEREIaql 396
Cdd:PRK11637 115 LEQQQAAQERlLAAQLDAAfrqgEHTgLQLilsgeESQrgerilayfgyLNQARQETIAELKQTR--EELAAQKAEL--- 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568937962 397 vEDVQRLQASLtkLRENSASQiSQLEQQLNAKNSTLKQLEEKL-KGQADYEEVK 449
Cdd:PRK11637 190 -EEKQSQQKTL--LYEQQAQQ-QKLEQARNERKKTLTGLESSLqKDQQQLSELR 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
200-456 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 200 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKLQTLQT------ALEKTRTELFDLKTKYDEETTA---------- 320
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 321 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEV---ELAAKERE 392
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS--------LKSSRDAkqqTLQELEQE 1041
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 393 IAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTLK 456
Cdd:COG3096 1042 LEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQVVQAK 1114
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
323-456 |
2.29e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; 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. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.
Pssm-ID: 214017 [Multi-domain] Cd Length: 161 Bit Score: 40.45 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 323 DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVltrssLEVELAAKEREIAQLVEDVQR 402
Cdd:cd12924 1 DNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKI-----FEEQCQTQERYSKEYIEKFKR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 403 L--QASLTKLRENSASQISQLEQQLNAKnstlKQLEEKLKGQ-ADYEEVKKELNTLK 456
Cdd:cd12924 76 EgnEKEIQRIMHNYEKLKSRISEIVDSR----RRLEEDLKKQaAEYREIDKRMNSIK 128
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
320-444 |
2.41e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 320 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaievlTRSSLEVELAAKEREIAQLved 399
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ----------LIATLEGQLAELEAELAAL--- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568937962 400 vqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 444
Cdd:COG3524 241 -------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-441 |
2.41e-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: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 212 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 290
Cdd:COG3096 495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 291 HKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSSA-NHSLQLASQI 366
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSGEAlADSQEVTAAM 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 367 QkapdvaievltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLNAKNSTLKQLEEKLKG 441
Cdd:COG3096 633 Q-----------------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
204-457 |
2.90e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 204 LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEkirEYEQTLKSQAETIA----------------LEKEQKLQND 267
Cdd:PTZ00440 723 LNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKN---EFILHLYENDKDLPdgkntyeeflqykdtiLNKENKISND 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 268 FAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEET-TAKADEIEM-----------IMTDLERA 335
Cdd:PTZ00440 800 INILKENKKNNQ----DLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDeNLNLKELEKefnennqivdnIIKDIENM 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 336 NQRAEVAQreaeTLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVE----LAAKEREI--AQLVEDVQRLQASLtk 409
Cdd:PTZ00440 876 NKNINIIK----TLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniIQKNEKLNllNNLNKEKEKIEKQL-- 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 410 lrenSASQISQLEQQLNAKNSTLKQLEEKLKG------------QADYEEVKKELNTLKS 457
Cdd:PTZ00440 950 ----SDTKINNLKMQIEKTLEYYDKSKENINGndgthlekldkeKDEWEHFKSEIDKLNV 1005
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
117-362 |
3.15e-03 |
|
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: 42.05 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 196
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 197 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 265
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 266 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 342
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 568937962 343 QREAETLREQLSSANHSLQL 362
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
100-449 |
3.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 100 VAGAKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRKQvapllksfQGEIDALSKRSKEAEAAFLTVyk 179
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREEL-EQAREELEQLEEELEQA--------RSELEQLEEELEELNEQLQAA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 180 rlidvpdpvpaldvGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAETIale 259
Cdd:COG4372 93 --------------QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 260 keQKLQNDFAEKERKLQETQMST-TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:COG4372 153 --KELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 339 AEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 418
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
330 340 350
....*....|....*....|....*....|.
gi 568937962 419 SQLEQQLNAKNSTLKQLEEKLKGQADYEEVK 449
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-489 |
3.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 263 KlqndfAEKERKLQETQmsttSKLEEAEHKLQTLQTALE-KTRTElfdlKTKYDEETTAKADEIEmimtDLERANQRAEV 341
Cdd:PTZ00121 1406 K-----ADELKKAAAAK----KKADEAKKKAEEKKKADEaKKKAE----EAKKADEAKKKAEEAK----KAEEAKKKAEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 342 AqREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQL 421
Cdd:PTZ00121 1469 A-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937962 422 EQQLNA----KNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSE 489
Cdd:PTZ00121 1543 EEKKKAdelkKAEELKKAEEKKKAeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
191-378 |
4.11e-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: 40.49 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 191 LDVGQQLEIK-VQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAEtialekeqKLQNDFA 269
Cdd:pfam17078 33 LEIAQQKESKfLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLE--------NSSASET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 270 EKERKLQETQMS----TTSKLEEAEH---KLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:pfam17078 105 TLEAELERLQIQydalVDSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNI 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 568937962 343 QREAET-LREQLSSANHSLQLASQIQKAPDVAIEVLT 378
Cdd:pfam17078 185 YVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
380-498 |
4.17e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.59 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 380 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 459
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 568937962 460 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 498
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-456 |
4.43e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 139 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLTVYKRLIDVPDPVPAL----DVG 194
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 195 QQLEIKVQ----RLHDIETENQKLRETLEEYNK--------------EFAEVKNQEVT----IKALKEKIREYEQTLKSq 252
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiindpvyknrnyinDYFKYKNDIENkkqiLSNIDAEINKYHAIIKK- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 253 aetiaLEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALE----------KTRTELFDLKTKYDEETTAKA 322
Cdd:PRK01156 331 -----LSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIEslkkkieeysKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 323 DEI----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAP----DVAIEVLTR---------SSLEVE 385
Cdd:PRK01156 405 DAIkkelNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgtTLGEEKSNHiinhynekkSRLEEK 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937962 386 LAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLK 456
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
319-454 |
4.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 319 TAKADEIEmimtdlERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVE 398
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKL---------RNEFEKELRERRNELQKLEK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568937962 399 DVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT 454
Cdd:PRK12704 90 RLLQKEENL----DRKLELLEKREEELEKKEKELEQKQQELEKkEEELEELIEEQLQ 142
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
219-306 |
5.72e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 219 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 293
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 568937962 294 QTLQTALEKTRTE 306
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
207-338 |
5.85e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.51 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 207 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 282
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937962 283 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 338
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
199-453 |
6.25e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 199 IKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAL--------EKEQKLQNDFAE 270
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDHLNLvqtalrqqEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 271 KERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKY-------DEETT------------AKADEI-EMIMT 330
Cdd:COG3096 359 LTERLEEQEEV----VEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqalDVQQTraiqyqqavqalEKARALcGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 331 DLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASltkl 410
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQAL---- 510
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568937962 411 rensASQISQLEQQLnaknstlKQLEEKLKGQADYEEVKKELN 453
Cdd:COG3096 511 ----AQRLQQLRAQL-------AELEQRLRQQQNAERLLEEFC 542
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
239-437 |
6.29e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 239 KEKIREYEQTLKSQAETIA----LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAL------EKTRTELF 308
Cdd:PRK04863 279 NERRVHLEEALELRRELYTsrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqekiERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 309 DLKTKYDE--ETTAKADEIemimtdLERANQRAEVAQREAETLREQLSSANHSLQL----ASQIQKApdvaievltrssl 382
Cdd:PRK04863 359 ELEERLEEqnEVVEEADEQ------QEENEARAEAAEEEVDELKSQLADYQQALDVqqtrAIQYQQA------------- 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 383 eVELAAKEREIAQL----VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 437
Cdd:PRK04863 420 -VQALERAKQLCGLpdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
373-502 |
6.40e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 373 AIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQLEEKLKgqadyeEV 448
Cdd:PRK11281 32 NGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQAPAKLR------QA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568937962 449 KKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 502
Cdd:PRK11281 100 QAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
202-363 |
6.41e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 202 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 266
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 267 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 334
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 568937962 335 ANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
306-456 |
6.81e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 306 ELFD-LKTKYDEETTAKADEIEMIMTDLERANqraevaqreaETLReqLSSANHSL-QLASQIQkapdvAIEVLTRSSLE 383
Cdd:PRK04778 64 EKFEeWRQKWDEIVTNSLPDIEEQLFEAEELN----------DKFR--FRKAKHEInEIESLLD-----LIEEDIEQILE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937962 384 -----VELAAKER-EIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 456
Cdd:PRK04778 127 elqelLESEEKNReEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESGDYVEAREILDQLE 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-457 |
7.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhslqlasqiqkapdvaie 375
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 376 vltrssLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT 454
Cdd:COG4372 64 ------LEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQEELEElQKERQDLEQQRKQ 133
|
...
gi 568937962 455 LKS 457
Cdd:COG4372 134 LEA 136
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-277 |
7.90e-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: 39.91 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
|
170
....*....|....*
gi 568937962 263 KLQNDFAEKERKLQE 277
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
192-457 |
7.91e-03 |
|
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: 40.71 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKSQAETIALEK-------EQKL 264
Cdd:COG5185 97 KILQEYVNSLIKLPNYEWSADILISLLYLYKSE----IVALKDELIKVEKLDEIADIEASYGEVETGIIkdifgklTQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 265 -QNDFAEKERKLQETQMSTTSKLEEAEH-----------------KLQTLQTALEKTRTE----LFDLKTKYDEETTAKA 322
Cdd:COG5185 173 nQNLKKLEIFGLTLGLLKGISELKKAEPsgtvnsikesetgnlgsESTLLEKAKEIINIEealkGFQDPESELEDLAQTS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 323 DEIEMIMTD-----LERANQRAEVAQR---EAETLREQLSSANHSLQLASQ---IQKAPDVAIEVLTRSSLEVELAAKER 391
Cdd:COG5185 253 DKLEKLVEQntdlrLEKLGENAESSKRlneNANNLIKQFENTKEKIAEYTKsidIKKATESLEEQLAAAEAEQELEESKR 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937962 392 EIAqlvEDVQRLQASLTKLREnsasqisQLEQQLNAKNSTLKQLEeklkGQADYEEVKKELNTLKS 457
Cdd:COG5185 333 ETE---TGIQNLTAEIEQGQE-------SLTENLEAIKEEIENIV----GEVELSKSSEELDSFKD 384
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
190-453 |
9.52e-03 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 40.19 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 190 ALDVGQQLEIKVQRLHDIETENQKLRETLEeYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAEtialekeqKLQNDFA 269
Cdd:cd23695 160 LLDENEEIEYKNSLLMPIYQDLKSLIKHLK-YTELFKLLKEYQDAKAIIIEDFRESSEEGAEKLE--------KLEKAFA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 270 EKERKLQEtqmsttsKLEEAEHKLQTLQTALEktrtELFDLKTKYDEETT-AKADEIeMIMTDLERANQRAEVAQREAET 348
Cdd:cd23695 231 TLLKNYKE-------ELEEPEKQLEFMQKRLL----DLYNLLRLWGQYITiVKMPDS-VVRDIMNKTQARPEVAKLNSKQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 349 LREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASL-----TKLRENSASQISQ--- 420
Cdd:cd23695 299 ELEDAKNRKRDTEENEFDDDYESADEGETSDEEDEIEEENFQLQKEKKKEEELNAEFNIaknslYKFSPQNDKNVVDdrd 378
|
250 260 270
....*....|....*....|....*....|....*....
gi 568937962 421 ------LEQQLnakNSTLKQLEEKLKGqADYEEVKKELN 453
Cdd:cd23695 379 fysgvdLENVF---PRALLNNLNDFTG-LDFQNVKEILN 413
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
259-500 |
9.58e-03 |
|
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: 40.49 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 259 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 339 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVAIEVLTR-SSLEVELAAKERE-------------IAQLVEDV 400
Cdd:pfam05557 127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDseivknskselarIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 401 QRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefapsegAGTQDSTKPLE 476
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL-------AQDTGLNLRSP 278
|
250 260
....*....|....*....|....
gi 568937962 477 VLLLEKNRSLQSENATLRISNSDL 500
Cdd:pfam05557 279 EDLSRRIEQLQQREIVLKEENSSL 302
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
120-452 |
9.63e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 120 QDESEQSRKRLIEQSREFKKNTPE-----------DLRKQVAPLLKsfqgEIDALSKRSKEAEAAF--LTVYKRLIDVPD 186
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQeavleetqeriNRARKAAPLAA----HIKAVTQIEQQAQRIHteLQSKMRSRAKLL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 187 PVPALDVGQQLEIKVQrlhdietenQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAE--TIALEKEQKL 264
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQ---------RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkTTLTQKLQSL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 265 QNDFaEKERKLQETQMSTTSKLE---------EAEHKLQ-----TLQTALEKTRT-------ELFDLKTKYDEETTAKAD 323
Cdd:TIGR00618 399 CKEL-DILQREQATIDTRTSAFRdlqgqlahaKKQQELQqryaeLCAAAITCTAQceklekiHLQESAQSLKEREQQLQT 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 324 EIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVL----TRSSLEVELAAKEREIAQLVED 399
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqTYAQLETSEEDVYHQLTSERKQ 557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568937962 400 VQRLQASLTKLREnSASQISQLEQQLNAKNSTLKQLEEKLK--GQADYEEVKKEL 452
Cdd:TIGR00618 558 RASLKEQMQEIQQ-SFSILTQCDNRSKEDIPNLQNITVRLQdlTEKLSEAEDMLA 611
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
200-452 |
9.73e-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: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 200 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQ 279
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 280 MSTTSKLEEAEHKLQTL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 346
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937962 347 ETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 426
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260
....*....|....*....|....*.
gi 568937962 427 AKNSTLKQLEEKLKGQADYEEVKKEL 452
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKI 496
|
|
| |
