|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1239-1316 |
6.41e-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: 116.92 E-value: 6.41e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 1239 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1316
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1056-1124 |
4.66e-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: 4.66e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 1056 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1124
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
667-743 |
2.02e-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: 106.91 E-value: 2.02e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 667 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 743
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1362-1418 |
2.98e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 74.07 E-value: 2.98e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 1362 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1418
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-483 |
5.53e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 338 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVLQvdgspssspraSAVSSLLcpsQEQAIEVLTRSSLEVELAAKER 417
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELE-----------SELEALL---NERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 418 EIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL--KGQADYEEVKKELNTLKS 483
Cdd:TIGR02168 902 ELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIED 965
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-478 |
1.02e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 143 EDLRKQVAPLLKsfQGEI----DALSKRSKEAEAAFLTVYKRLIDvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETL 218
Cdd:COG1196 196 GELERQLEPLER--QAEKaeryRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 219 EEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQKlqNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:COG1196 263 AELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 295 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvlq 374
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 375 vdgSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAK 454
Cdd:COG1196 413 ---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340
....*....|....*....|....
gi 1039770436 455 NSTLKQLEEKLKGQADYEEVKKEL 478
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAA 513
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1362-1419 |
1.05e-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: 1.05e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 1362 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1419
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1362-1417 |
6.60e-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: 6.60e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770436 1362 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1417
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
167-481 |
1.49e-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: 69.22 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 167 SKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 241
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 242 IREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTA 320
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 321 KAD-----------EIEMIMTDLERANQraEVAQREAETLREQLSSANhslQLASQIQKAPDVLQVDGSPSSSPRASAV- 388
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRQIE---ELQRQIEQATSSNEEVSKLLNELISELNk 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 389 ----SSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEek 464
Cdd:COG5185 453 vmreADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFM-- 530
|
330
....*....|....*..
gi 1039770436 465 lkgQADYEEVKKELNTL 481
Cdd:COG5185 531 ---RARGYAHILALENL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-484 |
7.84e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 275 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 351 EQ---LSSANHSLQLASQIQKA---------------------------PDVLQV----------DGSPSSSPRASAVSS 390
Cdd:COG4717 227 EEleqLENELEAAALEERLKEArlllliaaallallglggsllsliltiAGVLFLvlgllallflLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 391 LLCPSQEQAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQ 460
Cdd:COG4717 307 LQALPALEELEEEeleeLLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEE 386
|
330 340
....*....|....*....|....
gi 1039770436 461 LEEKLKGQADYEEVKKELNTLKSM 484
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQ 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-520 |
1.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 208 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 284
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 285 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 361
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 362 LASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSA 441
Cdd:TIGR02168 328 LESKLDELAEELA--------------------ELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 442 SQISQLEQQLNAKNSTLKQLEEKLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSEN 516
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
|
....
gi 1039770436 517 ATLR 520
Cdd:TIGR02168 464 EELR 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-483 |
1.90e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 143 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 219
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 220 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 297
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 298 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhslqlaSQIQKAPDVLQVDG 377
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 378 SPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVqrlqasltklrENSASqISQLEQQLNAKNST 457
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----------EEELS-LEDVQAELQRVEEE 966
|
330 340
....*....|....*....|....*..
gi 1039770436 458 LKQLEE-KLKGQADYEEVKKELNTLKS 483
Cdd:TIGR02169 967 IRALEPvNMLAIQEYEEVLKRLDELKE 993
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
143-478 |
2.90e-09 |
|
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: 61.63 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 143 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 216
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 217 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 277
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 278 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 351
Cdd:pfam05622 160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 352 QLSSANHSLQLAsQIQKApdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 431
Cdd:pfam05622 236 TLRETNEELRCA-QLQQA-------------------------ELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 432 SLTKLRE----NSASQISQLEQQLNAKNSTLKQLEEKLKG--------QADYEEVKKEL 478
Cdd:pfam05622 290 ENKMLRLgqegSYRERLTELQQLLEDANRRKNELETQNRLanqrilelQQQVEELQKAL 348
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-483 |
3.08e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 197 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 276
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 277 ETQMSTTSKLEEAEHKLQTLQTALEK----TRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 352
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 353 LSSANHSL------------QLASQIQKAPDV---LQVDGSPSSSPRASAVSSLLcpSQEQAIEVLTR---------SSL 408
Cdd:TIGR02169 334 LLAEIEELereieeerkrrdKLTEEYAELKEEledLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRL 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 409 EVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTLKS 483
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-438 |
3.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLTVYK 179
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 180 RLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiALE 259
Cdd:COG1196 324 EL---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 260 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRA 339
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 340 EVAQ--REAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKER 417
Cdd:COG1196 464 LLAEllEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340
....*....|....*....|.
gi 1039770436 418 EIAQLVEDVQRLQASLTKLRE 438
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIE 564
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-485 |
4.59e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918 388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDE---- 316
Cdd:PRK03918 534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEylel 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 317 -----ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLqlasqiqkapdvlqvdgspsssprasavssl 391
Cdd:PRK03918 608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------------------------------- 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 392 lcpSQEQAIEvltrssLEVELAAKEREIAQLVEDVQRLQasltKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADY 471
Cdd:PRK03918 657 ---SEEEYEE------LREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
410
....*....|....
gi 1039770436 472 EEVKKELNTLKSME 485
Cdd:PRK03918 724 EELREKVKKYKALL 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-484 |
7.11e-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: 59.78 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 251 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTkydeettakadEIEMI 328
Cdd:COG4942 17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQ-----------ELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 329 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLcPSQEQAIEvltrssl 408
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAE------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 409 evELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSM 484
Cdd:COG4942 154 --ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-353 |
7.96e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtPEDLR-KQVAPLLKSFQGE-----IDALSKRSKEAEaaflT 176
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKlKELAEQLKELEEKlkkynLEELEKKAEEYE----K 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 177 VYKRLIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlks 251
Cdd:PRK03918 530 LKEKLIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 252 qaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEET--------TAKAD 323
Cdd:PRK03918 600 -----FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSR 673
|
250 260 270
....*....|....*....|....*....|
gi 1039770436 324 EIEMIMTDLERANQRAEVAQREAETLREQL 353
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-479 |
8.36e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 270
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 271 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI-----------------MTDLE 333
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenqsykqeiknlesqINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 334 RANQRAEVAQREAETLREQLSSANHSLQ-----LASQIQKAPDVLQvDGSPSSSPRASAVSSL--LCPSQEQAIEVLTRS 406
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIKNNSEIK-DLTNQDSVKELIIKNLdnTRESLETQLKVLSRS 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 407 ---------SLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEKL---KGQADY 471
Cdd:TIGR04523 477 inkikqnleQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKEKESKISDLEDELnkdDFELKK 556
|
....*...
gi 1039770436 472 EEVKKELN 479
Cdd:TIGR04523 557 ENLEKEID 564
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-520 |
1.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 104 KLKRELDATATVLANRQDESEQSRKRL---------IEQSREFKKNTPEDLRKQVapllksfqGEIDALSKRSKEaeaaf 174
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKrkleekireLEERIEELKKEIEELEEKV--------KELKELKEKAEE----- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 175 ltvYKRLIDVpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqae 254
Cdd:PRK03918 295 ---YIKLSEF------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 255 tiALEKEQKLQNDFAEKERKLQETQMSTTSK-LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMtDLE 333
Cdd:PRK03918 356 --ELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 334 RANQRAEVAQRE----------AETLREQLSSANHSLQLASQIQKAPDVL-QVDGSPSSSPRASAVSSLLcpsqEQAIEV 402
Cdd:PRK03918 433 KAKGKCPVCGRElteehrkellEEYTAELKRIEKELKEIEEKERKLRKELrELEKVLKKESELIKLKELA----EQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 403 ltRSSLEV----ELAAKEREIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKQLEEKLK---------GQA 469
Cdd:PRK03918 509 --EEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAellkeleelGFE 585
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 470 DYEEVKKELNTLKSM--EF-----APSEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 520
Cdd:PRK03918 586 SVEELEERLKELEPFynEYlelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-519 |
1.58e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 258
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 259 EKEQ------------------KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYdEE 317
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRL-EE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 318 TTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-NHSLQLASQIQKAPDVL----QVDGSPSSSPRASAVSSL 391
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELeKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 392 LCP------SQEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLNAK 454
Cdd:PRK03918 437 KCPvcgrelTEEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKY 515
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770436 455 NstLKQLEEKLKgqaDYEEVKKELNTLKsmefapSEGAGTQDSTKPLEVL------LLEKNRSLQSENATL 519
Cdd:PRK03918 516 N--LEELEKKAE---EYEKLKEKLIKLK------GEIKSLKKELEKLEELkkklaeLEKKLDELEEELAEL 575
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
143-335 |
6.66e-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: 56.22 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039770436 300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
121-353 |
9.27e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 121 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 197
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 198 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 277
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 278 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTK----------YDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqeLHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
....*.
gi 1039770436 348 TLREQL 353
Cdd:COG1340 227 ELHEEI 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-376 |
1.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 180
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 181 lidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 260
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 261 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039770436 338 RAEVAQREAETLreqlssANHSLQLASQIQKAPDVLQVD 376
Cdd:TIGR02168 500 NLEGFSEGVKAL------LKNQSGLSGILGVLSELISVD 532
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
202-344 |
1.17e-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: 54.55 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 202 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 271
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770436 272 E-RKLQEtqmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTdlERANQRAEVAQR 344
Cdd:COG1579 111 EiLELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
212-459 |
1.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 290
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 291 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-----QLASQ 365
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 366 IQKAPDVLQVdgspsssprasavssllCPSQEQAIEVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 445
Cdd:COG4913 386 RAEAAALLEA-----------------LEEELEALEE-ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
250
....*....|....
gi 1039770436 446 QLEQQLNAKNSTLK 459
Cdd:COG4913 448 ALAEALGLDEAELP 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-443 |
2.07e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 303
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 304 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVD 376
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 377 GSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 443
Cdd:COG4942 176 LEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-536 |
2.69e-07 |
|
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: 55.75 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 98 LCVAGAKLKRELDATATVLANRQDE---------SEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQ---------GE 159
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkereqqlQT 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 160 IDALSKRSKEAEAAFLTVYKRLIDVPDPV--------PALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 232 evtIKALKEKIREYEQTLKSQAETIALEKE------------QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQT- 298
Cdd:TIGR00618 558 ---RASLKEQMQEIQQSFSILTQCDNRSKEdipnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHl 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 299 -------ALEKTRTELFDLKTKYDEET---------------------TAKADEIEMIMTDLERANQRAEVAQREAETL- 349
Cdd:TIGR00618 635 qqcsqelALKLTALHALQLTLTQERVRehalsirvlpkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIe 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 350 -----REQLSSANHSLQ--------LASQIQK-----APDVLQVDGSPSSSPRASAVSSLLCPSQEQAIE------VLTR 405
Cdd:TIGR00618 715 eydreFNEIENASSSLGsdlaaredALNQSLKelmhqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiqffNRLR 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 406 SSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770436 474 VKKELNTLKSMEFAPSEGAgtqdSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRD 536
Cdd:TIGR00618 874 LSDKLNGINQIKIQFDGDA----LIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-355 |
2.70e-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: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 275 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 1039770436 355 S 355
Cdd:COG4913 430 S 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-483 |
3.46e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 143 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYN 222
Cdd:COG4717 74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 223 KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEK 302
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 303 TRTELFDLKtkyDEETTAKADEIEMIMT----------------------------------------------DLERAN 336
Cdd:COG4717 232 LENELEAAA---LEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllallflllarekaslgkEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 337 QRAEVAQREAETLREQLS--------SANHSLQLASQIQKAPDVL--------QVDGSPSSSPRASAVSSLLCPSQEQAI 400
Cdd:COG4717 309 ALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLreaeeleeELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 401 EVLTRS----SLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEK----------LK 466
Cdd:COG4717 389 AALEQAeeyqELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREElaeleaeleqLE 466
|
410
....*....|....*..
gi 1039770436 467 GQADYEEVKKELNTLKS 483
Cdd:COG4717 467 EDGELAELLQELEELKA 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-540 |
6.53e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 213 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLK-SQAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 287
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSdASRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 288 EAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 365
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 366 iqkapdvlqvdgspsssprasavssllcpsqeqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS--- 442
Cdd:TIGR02169 816 -----------------------------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiek 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 443 -------QISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsEGAGTQDSTkplevllLEKNRSLQS 514
Cdd:TIGR02169 855 eienlngKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLS 920
|
330 340
....*....|....*....|....*..
gi 1039770436 515 E-NATLRISNSDLSGSARRKGRDQPES 540
Cdd:TIGR02169 921 ElKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-482 |
7.70e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 204 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 273
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 274 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 351 EQLSSANHSLQ---------------LASQIQKAPDVLQVdgspsssprasavssllcpsQEQAIEVLTR--SSLEVELA 413
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMLDV--------------------KERKINVLQKkiENLQEQLR 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770436 414 AKEREIAQLVEDVQRLQASLTklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 482
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSS----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-483 |
8.03e-07 |
|
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: 53.87 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 270
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 271 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 348
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 349 lrEQLSSANHSLqLASQIQKAPDVLQvdgspsssprasavssllcpsQEQAIEVLTRsslevELAAKEREIAQLVEDVQR 428
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQ---------------------KEKEKKDLIK-----EIEEKEKKISSLEKELEK 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770436 429 LQASLTKLrensASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKS 483
Cdd:TIGR04523 622 AKKENEKL----SSIIKNIKSKKNKLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-374 |
8.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 281
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 282 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 357
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170
....*....|....*..
gi 1039770436 358 HSLQLASQIQKAPDVLQ 374
Cdd:COG4913 763 VERELRENLEERIDALR 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-353 |
1.46e-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: 53.14 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 177
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 178 YKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTLKSQA 253
Cdd:TIGR02168 816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 254 ETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 331
Cdd:TIGR02168 887 EALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
|
250 260
....*....|....*....|..
gi 1039770436 332 LERANQRAEVAQREAETLREQL 353
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
114-374 |
1.62e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.16 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 114 TVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEAEAAFLTVYKRLIDVPDPv 188
Cdd:COG5022 868 TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTELIARLKKLLNNIDLEEG- 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 189 PALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKS--------QAETIALEK 260
Cdd:COG5022 946 PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalQESTKQLKE 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 261 EQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmiM 329
Cdd:COG5022 1021 LPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--V 1098
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039770436 330 TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQ 374
Cdd:COG5022 1099 KDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLE 1143
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
867-1050 |
2.51e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 867 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 944
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 945 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 1024
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 1039770436 1025 NSPLPSSPIVPMAKPAKPSVPPLTPE 1050
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
208-528 |
2.89e-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: 52.28 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 208 ETENQKLRETLEEYNKEFA---EVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQM 280
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEklaqVLKENKEEEKEKKLQEEEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 281 STTSKLEEAEHKlqtlQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:pfam02463 289 KLLAKEEEELKS----ELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 360 LQLASQIQKAPDVLQVDGSPSSSPRASAvssllcpsQEQAIEVLTRSSLEVELAAKEREiaQLVEDVQRLQASLTKLREn 439
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKL--------KEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEILE- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 440 sASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATL 519
Cdd:pfam02463 434 -EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
....*....
gi 1039770436 520 RISNSDLSG 528
Cdd:pfam02463 513 LALIKDGVG 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-652 |
4.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 361 QLASQIQKAPDVLqvdgspsssPRASAVSSLLcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRE 438
Cdd:COG3883 96 YRSGGSVSYLDVL---------LGSESFSDFL--DRLSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 439 NSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKEL-NTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENA 517
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAE---EAAAEAQLAELeAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 518 TLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGK 597
Cdd:COG3883 242 AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770436 598 FALNSLLQRQLMQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGM 652
Cdd:COG3883 322 VVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYV 376
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-469 |
4.78e-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: 51.76 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 197 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 262
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 263 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 334
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 335 ANQRAE---VAQREAETLREQLSSANHSL-----QLASQIQKAPdvLQVDGSPsssprasaVSSLLCPSQEQAIEVLTRS 406
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSRLGELK--LRLNQAT--------ATPELLLQLENFDERIERA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770436 407 SLEVELAAKEreiaqlVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 469
Cdd:pfam12128 477 REEQEAANAE------VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
190-481 |
5.42e-06 |
|
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: 50.34 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 190 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 264
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 265 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 344
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 345 eaetLREQLSSANHSLQlaSQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSL----------EVELAA 414
Cdd:cd22654 155 ----LRTQIKTINDEIQ--EELTKILNRPIEVGDGSINIGKQVFTITITTATTKTVDVTSIGGLingignasddEVKEAA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 415 KerEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 481
Cdd:cd22654 229 N--KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
216-461 |
5.72e-06 |
|
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: 48.75 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 216 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 287
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 288 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 361 QLASQIQkapdvlqvdgspsssprasavSSLLcpsqEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENS 440
Cdd:pfam13851 137 QQKTGLK---------------------NLLL----EKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDA 178
|
250 260
....*....|....*....|..
gi 1039770436 441 ASQISQ-LEQQLNAKNSTLKQL 461
Cdd:pfam13851 179 LQAVTEkLEDVLESKNQLIKDL 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-483 |
5.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 227 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 299
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 300 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLssanhslqlasqiqkapdvLQVDGsp 379
Cdd:COG4913 297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQI-------------------RGNGG-- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 380 sssprasavssllcpsqeQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLN 452
Cdd:COG4913 338 ------------------DRLE-----QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLE 394
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039770436 453 AKNSTLKQLEEKL--------KGQADYEEVKKELNTLKS 483
Cdd:COG4913 395 ALEEELEALEEALaeaeaalrDLRRELRELEAEIASLER 433
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
103-537 |
7.48e-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: 50.99 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YK 179
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 180 RLIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 259 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 337
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 338 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVLQVDGSpsssprasavssLLCPsqeqaiEVLTRSSLEVEL----A 413
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIGK------------VISP------ELLHRTDLDPEVwdgsV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 414 AKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLkGQAdyeevKKELNTLK-SMEFAPSEG 491
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQSAREKQAAAEEQL-VQA-----NGELEKASrEETFARTAL 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1039770436 492 AGTQDSTKPL----EVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQ 537
Cdd:pfam12128 649 KNARLDLRRLfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-473 |
9.36e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 208 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 352
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 353 LSsaNHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQAS 432
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQ 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039770436 433 LTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-443 |
9.56e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 190 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 266
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 267 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 341
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 342 AQREAETLREQLSSANHSLQLASQiqkapdvlqvdgspsssprasavssllcpSQEQAIEVLTR--SSLEVELAAKEREI 419
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKA-----------------------------ERQKLLARLEKelAELAAELAELQQEA 222
|
250 260
....*....|....*....|....
gi 1039770436 420 AQLVEDVQRLQASLTKLRENSASQ 443
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-480 |
1.02e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 210 ENQKLRETLEeyNKEFAEVKNQEVTIKALKEKIREYEqtlksqaetiALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam02463 174 ALKKLIEETE--NLAELIIDLEELKLQELKLKEQAKK----------ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 290 EHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqRAEVAQREAETLREQLSSANHSLQLASQIQKa 369
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKLERRKVDDEEKLK- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 370 pdVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 449
Cdd:pfam02463 318 --ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270
....*....|....*....|....*....|.
gi 1039770436 450 QLNAKNSTLKQLEEKLKGQADYEEVKKELNT 480
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
274-479 |
1.16e-05 |
|
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: 48.38 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 274 KLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLRE 351
Cdd:COG1579 11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 352 QLSSA--NHSLQ-LASQIQkapdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDV 426
Cdd:COG1579 81 QLGNVrnNKEYEaLQKEIE---------------------------SLKRRISDLEDEILELmeRIEELEEELAELEAEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770436 427 QRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 479
Cdd:COG1579 134 AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-464 |
1.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 263 KLQNDFAE------------------KERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL---FDLKTKYDEETTAK 321
Cdd:COG4717 266 GSLLSLILtiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 322 ADEIEMIMTDLERANQRAEVAQREAE----------TLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSL 391
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEiaallaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770436 392 LCPSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLNAKNSTLKQLEEK 464
Cdd:COG4717 426 DEEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-485 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 104 KLKRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykrlid 183
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL-------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 184 vpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKSQAE 254
Cdd:pfam05483 445 -------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 255 TIALEKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELF----DLKTKYDE-ETTAKADEIEMI 328
Cdd:pfam05483 512 TLELKKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEYEVL 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 329 mtdleRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSL---LCPSQEQAIEVLTR 405
Cdd:pfam05483 584 -----KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLeleLASAKQKFEEIIDN 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 406 SSLEVELAAKEREiaQLVEDVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD--YEEVKKELNTLKS 483
Cdd:pfam05483 659 YQKEIEDKKISEE--KLLEEVEKAKAIA----DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDkiIEERDSELGLYKN 732
|
..
gi 1039770436 484 ME 485
Cdd:pfam05483 733 KE 734
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-484 |
1.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 181 LIDVPDPVPALDVGQQLEIKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKS 251
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 252 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLk 311
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 312 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVLQVDGSPSSsprasavssl 391
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQLAE---------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 392 lcpsQEQAIEVLTRSSLE-----VELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKl 465
Cdd:COG3206 275 ----LEAELAELSARYTPnhpdvIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL- 349
|
330
....*....|....*....
gi 1039770436 466 kgQADYEEVKKELNTLKSM 484
Cdd:COG3206 350 --EAELRRLEREVEVAREL 366
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
236-464 |
1.75e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 236 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 298
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 299 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSLqla 363
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSL--- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 364 SQIQKAPDVLQVdgspsssprasavssLLCPSQEQAIEVLTrssLEVELAAKEREIAQLVEDVQRLQASLTKL---RENS 440
Cdd:PHA02562 316 EKLDTAIDELEE---------------IMDEFNEQSKKLLE---LKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDN 377
|
250 260
....*....|....*....|....
gi 1039770436 441 ASQISQLEQQLNAKNSTLKQLEEK 464
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
212-477 |
1.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYE----------QTLKSQAETIALEKE-------------------- 261
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLEELEEERDdllaeaglddadaeavearr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 262 QKLQNDFAEKERKLQETQMSTTSKLEEAE-----------------HKLQTLQTALEKTRTELFDLKTK---YDEETTAK 321
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAEslredaddleeraeelrEEAAELESELEEAREAVEDRREEieeLEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 322 ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVLQvDGSpsssprasavssllCPSQEQAI 400
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtARERVEEAEALLE-AGK--------------CPECGQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 401 E----VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE--NSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEV 474
Cdd:PRK02224 462 EgsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
...
gi 1039770436 475 KKE 477
Cdd:PRK02224 542 LRE 544
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
203-312 |
2.10e-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: 48.48 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 1039770436 277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-356 |
2.26e-05 |
|
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: 47.61 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 203 RLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQKLQnDFAEKERKLQETQMS- 281
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIK-RLELEIE-EVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 282 TTSK-LEEAEHKLQTL---QTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSA 356
Cdd:COG1579 86 RNNKeYEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-331 |
2.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrli 182
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 dvPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQ 262
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 263 KLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-469 |
2.96e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 110 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRlid 183
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 184 vPDPVPALDvgQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIAlEKEQK 263
Cdd:PRK02224 383 -REEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 264 LQ-NDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 340
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 341 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVLQvDGSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEvELAAKEREI 419
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAA-EAEEEAEEAREEVAEL---NSKLAELKERIESLE-RIRTLLAAI 601
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039770436 420 AQLVEDVQRLQASltklRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 469
Cdd:PRK02224 602 ADAEDEIERLREK----REALAELNDERRERLAEKRERKRELEAEFDEAR 647
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-519 |
3.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 295 TlqtalektrtelfdlktkydeETTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-------NHSLQLASQI 366
Cdd:TIGR00606 312 R---------------------TVREKERELVDCQRELEKLNKeRRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 367 QKAPDVLQVDGSPSSSPRASAVSSLLCPSQE-QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 445
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 446 QLEQQLNAKNSTLKQLEEKLKG--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 519
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
193-468 |
3.85e-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: 48.56 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 193 VGQQLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam05483 132 VSLKLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 259 EKEQKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKA 322
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 323 DEIEMIMTDLERANQRAEVAQReaeTLREQLSSANHSLQLASQIQKApdvlQVDGSPSSSPRASAVSSLLcPSQEQAIEV 402
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQK---ALEEDLQIATKTICQLTEEKEA----QMEELNKAKAAHSFVVTEF-EATTCSLEE 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770436 403 LTRSSLEvELAAKEREIAQLVEDVQRLQASL---TKLRENSASQISQLEQQLNAKNSTL---KQLE---EKLKGQ 468
Cdd:pfam05483 364 LLRTEQQ-RLEKNEDQLKIITMELQKKSSELeemTKFKNNKEVELEELKKILAEDEKLLdekKQFEkiaEELKGK 437
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-322 |
4.18e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 116 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL 191
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDF 268
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039770436 269 AEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 322
Cdd:COG3206 337 AQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1362-1447 |
4.26e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 1362 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1441
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 1039770436 1442 RSSRAA 1447
Cdd:COG5576 121 EEADLA 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-371 |
4.34e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykrli 182
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 dvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4913 688 ------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 263 KLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 341
Cdd:COG4913 750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039770436 342 AQREAETL-------REQLSSANHS--LQLASQIQKAPD 371
Cdd:COG4913 822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIR 860
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-491 |
6.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLI 182
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI---- 256
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkade 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 257 ---ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PTZ00121 1515 akkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 334 --RANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASA--VSSLLCPSQEQAIEVLTRSSLE 409
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkAEELKKAEEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 410 VELAAKEREIAQLVEDVQRLQASLTKLRENS--ASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFA 487
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
....
gi 1039770436 488 PSEG 491
Cdd:PTZ00121 1751 KDEE 1754
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
235-486 |
1.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 235 IKALKEKIREYEqTLKSQAETIALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY 314
Cdd:COG4717 48 LERLEKEADELF-KPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 315 D-EETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKApdvlqvdgspsssprasavssllc 393
Cdd:COG4717 126 QlLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------ELEAELAEL------------------------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 394 psQEQAIEVLTRSSLevelaAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 473
Cdd:COG4717 176 --QEELEELLEQLSL-----ATEEELQDLAEELEELQQ-----------RLAELEEELEEAQEELEELEEELEQLENELE 237
|
250
....*....|...
gi 1039770436 474 VKKELNTLKSMEF 486
Cdd:COG4717 238 AAALEERLKEARL 250
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
829-1074 |
1.29e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 829 ILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEA 908
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 909 QDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQG 988
Cdd:PRK10263 363 VPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 989 PSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLtpeqyevYMYQEVD 1061
Cdd:PRK10263 442 VAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL-------YYFEEVE 513
|
250
....*....|...
gi 1039770436 1062 tiELTRQVKEKLA 1074
Cdd:PRK10263 514 --EKRAREREQLA 524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-366 |
1.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 145 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 215
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 216 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 289
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 290 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMI---MTDLERANQRAEVAQREAETLREQLSSAN--HSLQLAS 364
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELkaeLRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
..
gi 1039770436 365 QI 366
Cdd:COG4717 523 EY 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-508 |
1.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRA 339
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 340 EVAQREAETLREQLSSANHSLQlasQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVlTRSSLEVELAAKEREI 419
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELE---ELQKERQDLE--------------------QQRKQLEA-QIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 420 AQLVEDVQRLQASLTKLRENSA--------SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEG 491
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQalseaeaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250
....*....|....*..
gi 1039770436 492 AGTQDSTKPLEVLLLEK 508
Cdd:COG4372 233 LALSALLDALELEEDKE 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
216-476 |
2.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 216 ETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKER------------KLQETQMSTT 283
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDnradeateeafgKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 284 SKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDEETTAKADEIEMIMTDLERAnQRAEVAQREAETLREQLSSANHSL 360
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 361 QLASQIQKAPDVLQVDgSPSSSPRASAVSSLLCPSQEQAIEVLTRssleVELAAKEREIAQLVEDVqRLQASLTKLRENS 440
Cdd:PTZ00121 1188 RKAEELRKAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKDAEEAKKAEEE-RNNEEIRKFEEAR 1261
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039770436 441 ASQISQLEQQLNA----KNSTLKQLEEKLKGQA--DYEEVKK 476
Cdd:PTZ00121 1262 MAHFARRQAAIKAeearKADELKKAEEKKKADEakKAEEKKK 1303
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-466 |
2.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 186 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 264
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 265 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 341
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 342 AQREAEtLREQLSSanhslqlaSQIQKAPdvlqvdgspsssprasavsslLCPSQEQAievltrssLEVELAAKEREIA- 420
Cdd:PRK11281 169 SQRLQQ-IRNLLKG--------GKVGGKA---------------------LRPSQRVL--------LQAEQALLNAQNDl 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770436 421 --QLVEDVQRLQASLTKLRENSASQISQLEQQL-------NAKNstLKQLEEKLK 466
Cdd:PRK11281 211 qrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
211-462 |
2.20e-04 |
|
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: 45.90 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 211 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 290 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlas 364
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 365 qiqkapdvlqvdgspsssPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSAS 442
Cdd:pfam07111 215 ------------------AQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLT 276
|
250 260
....*....|....*....|.
gi 1039770436 443 QISQL-EQQLNAKNSTLKQLE 462
Cdd:pfam07111 277 HMLALqEEELTRKIQPSDSLE 297
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
195-358 |
2.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ-EVTIKALKEKIREYEQtLKSQAETIALEKE--QKLQNDFAEK 271
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEErDELNEKLNELREELDE-LRKELAELNKAGGsiDKLRKEIERL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 272 ERKLQETQMSTT------SKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTaKADEIEMIMTDL-ERANQ-RAEVAQ 343
Cdd:COG1340 122 EWRQQTEVLSPEeekelvEKIKELEKELEKAKKALEKNE-KLKELRAELKELRK-EAEEIHKKIKELaEEAQElHEEMIE 199
|
170
....*....|....*..
gi 1039770436 344 --REAETLREQLSSANH 358
Cdd:COG1340 200 lyKEADELRKEADELHK 216
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
259-539 |
2.60e-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: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 259 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 339 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVLQVdgspssspRASAVSSLlcpsqEQAIEVLTRSSLEVElAA 414
Cdd:pfam05557 127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAE--------AEQRIKEL-----EFEIQSQEQDSEIVK-NS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 415 KER--EIAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefap 488
Cdd:pfam05557 193 KSElaRIPELEKELERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL---- 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039770436 489 segAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPE 539
Cdd:pfam05557 268 ---AQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
202-307 |
2.63e-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: 43.74 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 202 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 265
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039770436 266 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 307
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
388-539 |
2.66e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 388 VSSLLCPSQEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQLEE 463
Cdd:PRK11281 21 CLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQAPA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770436 464 KLKgqadyeEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSarrkgRDQPE 539
Cdd:PRK11281 95 KLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL-----QTQPE 159
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
153-355 |
2.87e-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: 44.25 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 153 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 228
Cdd:pfam00261 17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 229 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam00261 91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039770436 306 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-537 |
2.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPDVLQ 374
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 375 VdgspsssprasavssllcpSQEQAIEVLT-RSSLEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQ 450
Cdd:COG4372 84 E-------------------LNEQLQAAQAeLAQAQEELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 451 LNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsegagTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGS 529
Cdd:COG4372 145 IAEREEELKELEEQLESlQEELAALEQELQALS-----------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
....*...
gi 1039770436 530 ARRKGRDQ 537
Cdd:COG4372 214 RELAEELL 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-463 |
3.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 207 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 286
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 287 EEAEHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHslQLASQI 366
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--QLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 367 QKAPDVLQVDgspsSSPRASAVSSLlcpsqEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQ 446
Cdd:COG3206 312 QRILASLEAE----LEALQAREASL-----QAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEE 376
|
250
....*....|....*..
gi 1039770436 447 LEQQLNAKNSTLKQLEE 463
Cdd:COG3206 377 ARLAEALTVGNVRVIDP 393
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
193-333 |
3.67e-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: 42.76 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 193 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlksQAETialekEQKLQNDFAEKE 272
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 273 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 333
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
113-356 |
4.21e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 113 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 192
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 271
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 272 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 345
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250
....*....|.
gi 1039770436 346 AETLREQLSSA 356
Cdd:pfam07888 253 VEGLGEELSSM 263
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
850-1050 |
5.77e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 850 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 929
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 930 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 1009
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039770436 1010 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 1050
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
141-530 |
6.14e-04 |
|
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: 44.83 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 141 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFltvykrlidvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEE 220
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTAL--------------------KNARLDLRRLFD---EKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 221 YNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQt 295
Cdd:pfam12128 672 ALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 296 lQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapdvl 373
Cdd:pfam12128 749 -LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA------------ 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 374 qvdgspsssprasavssllcpsqeqaievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQLEQQLNA 453
Cdd:pfam12128 814 ------------------------------------TQLSNIERAISELQQQLARLIAD-TKLR------RAKLEMERKA 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 454 KNSTLKQLEEKLKGQADYEEvkkELNTLKsmEFAPSEGAGTQDSTKP--LEVLLLEKNR---SLQSENATLRISNSDLSG 528
Cdd:pfam12128 851 SEKQQVRLSENLRGLRCEMS---KLATLK--EDANSEQAQGSIGERLaqLEDLKLKRDYlseSVKKYVEHFKNVIADHSG 925
|
..
gi 1039770436 529 SA 530
Cdd:pfam12128 926 SG 927
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-313 |
7.28e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 148 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldvgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 227
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 228 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 304
Cdd:COG1579 85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155
|
....*....
gi 1039770436 305 TELFDLKTK 313
Cdd:COG1579 156 AELEELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-479 |
8.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 195 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREY---------------------------- 245
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklkknkdkinklnsdlskinseiknd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 246 -EQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTA 320
Cdd:TIGR04523 116 kEQKNKLEVELNKLEKQkkenKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID-KIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 321 KADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ-IQKAPDVLQvdgspSSSPRASAVSSllcpSQEQA 399
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeINEKTTEIS-----NTQTQLNQLKD----EQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 400 IEVLTRSSLEVELAakEREIAQLVEDVQRLQASLTKLR----------------------ENSASQISQLEQQLNAKNST 457
Cdd:TIGR04523 266 KKQLSEKQKELEQN--NKKIKELEKQLNQLKSEISDLNnqkeqdwnkelkselknqekklEEIQNQISQNNKIISQLNEQ 343
|
330 340
....*....|....*....|...
gi 1039770436 458 LKQLEEKLKG-QADYEEVKKELN 479
Cdd:TIGR04523 344 ISQLKKELTNsESENSEKQRELE 366
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
212-302 |
9.68e-04 |
|
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: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 212 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 280
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 1039770436 281 STTSKLEEAEHKLQTLQTALEK 302
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
212-355 |
9.80e-04 |
|
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: 42.95 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 212 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 286
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770436 287 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 355
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-482 |
1.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 408 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 465
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 1039770436 466 KG-QADYEEVKKELNTLK 482
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
226-496 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKLQTLQTALEK 302
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 303 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVLQvdgspsss 382
Cdd:COG4372 85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK------QLEAQIAELQSEIA-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 383 prasavssllcpSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLNAKNSTLKQLE 462
Cdd:COG4372 147 ------------EREEELK-----ELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
250 260 270
....*....|....*....|....*....|....
gi 1039770436 463 EKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQD 496
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1381-1415 |
1.17e-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: 1.17e-03
10 20 30
....*....|....*....|....*....|....*
gi 1039770436 1381 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1415
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
103-354 |
1.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDeSEQSRkRLIEQSREFKKNTpEDLRKQV--AP-LLKSFQGEIDALSKRSKEaeaafltvyk 179
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQD-LEQTL-ALLDKIDRQKEET-EQLKQQLaqAPaKLRQAQAELEALKDDNDE---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 180 rliDVPDPVPALDVgQQLEikvQRLHDIETENQKLRETLEEYNKEFA---------------------EVKNQEVTIKAL 238
Cdd:PRK11281 113 ---ETRETLSTLSL-RQLE---SRLAQTLDQLQNAQNDLAEYNSQLVslqtqperaqaalyansqrlqQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 239 KEKIREYEQTLKsQAETIALEkeqkLQNDFAEKE----RKLQETQMS----TTSKLEEAEHKLQTLQTALEKTRTELFdl 310
Cdd:PRK11281 186 GKALRPSQRVLL-QAEQALLN----AQNDLQRKSlegnTQLQDLLQKqrdyLTARIQRLEHQLQLLQEAINSKRLTLS-- 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039770436 311 ktkydEETTAKADEIEmimtDLERANQRAEVAQrEAETLReQLS 354
Cdd:PRK11281 259 -----EKTVQEAQSQD----EAARIQANPLVAQ-ELEINL-QLS 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-258 |
1.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAA--FLTV 177
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsreLAGLRAELEELEKRREEIKKTleKLKE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 178 YKRLID-----VPDPVPALDVGQQLEIKVQRLHDIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKEKIR------- 243
Cdd:PRK03918 702 ELEEREkakkeLEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENKVKlfvvyqg 781
|
170
....*....|....*.
gi 1039770436 244 -EYEQTLKSQAETIAL 258
Cdd:PRK03918 782 kERPLTFLSGGERIAL 797
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
196-470 |
1.83e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 196 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 273
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 346
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 347 ETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQ--AIEVLTRSSLEVELAAKEREIAQLVE 424
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQmeAQHDKTVNEQYSLLTSQNTFIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039770436 425 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 470
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
117-362 |
1.93e-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: 42.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 196
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 197 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 265
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 266 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 342
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 1039770436 343 QREAETLREQLSSANHSLQL 362
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
127-464 |
1.97e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 127 RKRLIEQSREFKKntpeDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaldvgQQLEiK 200
Cdd:COG3096 280 RRELSERALELRR----ELFGARRQLaeeqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL------RQQE-K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 201 VQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKE 272
Cdd:COG3096 349 IERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 273 RKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLERAnQRAEVAQREA 346
Cdd:COG3096 427 ALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERS-QAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 347 ETLREQLSSANHSLQLASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLT----RSSLEVELAAK-EREIAQ 421
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLR--------------------QQQNAERLLEefcqRIGQQLDAAEElEELLAE 561
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039770436 422 LVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEK 464
Cdd:COG3096 562 LEAQLEELEEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
121-477 |
3.04e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 121 DESEQSRKRLIEQSREFK-KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvPALDVGQQLEI 199
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR------------EALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 200 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERKLQETQ 279
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 280 mSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttakadeiemimtdlERANQRAEVAQREAETLREQLSSANHS 359
Cdd:TIGR00618 318 -SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---------------IHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 360 LQLASQIQKAPDVLQVdgspssspRASAVSSLLCPSQEQAIEVLTRSSLEVELA-AKEREIAQLVEDVQRLQASLTKLRE 438
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQS--------LCKELDILQREQATIDTRTSAFRDLQGQLAhAKKQQELQQRYAELCAAAITCTAQC 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039770436 439 NSASQISQLE--QQLNAKNSTLKQLEEKLKgqaDYEEVKKE 477
Cdd:TIGR00618 454 EKLEKIHLQEsaQSLKEREQQLQTKEQIHL---QETRKKAV 491
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
406-524 |
3.49e-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: 39.97 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 406 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 485
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039770436 486 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 524
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-277 |
4.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
|
170
....*....|....*
gi 1039770436 263 KLQNDFAEKERKLQE 277
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
207-338 |
4.27e-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: 39.90 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 207 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 282
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039770436 283 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 338
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-482 |
4.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKEQ 262
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 343 QREAETLREQLSSANHSLQLASQIQKAPDVLQVDGspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQL 422
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL-----------------AERLAEEELELEEALLAEEEEERELAEA 712
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770436 423 VEDVQRLQASLTKLRENSASQISQ-LEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 482
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
199-377 |
4.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 199 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 275 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttakadeiEMIMTDLERANQRAEVA 342
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL--------EEIMDEFNEQSKKLLEL 342
|
170 180 190
....*....|....*....|....*....|....*
gi 1039770436 343 QREAETLREQLSSANHSlqlASQIQKAPDVLQVDG 377
Cdd:PHA02562 343 KNKISTNKQSLITLVDK---AKKVKAAIEELQAEF 374
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
219-306 |
4.46e-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: 39.10 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 219 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 293
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 1039770436 294 QTLQTALEKTRTE 306
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
197-553 |
6.21e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 197 LEIKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKSQAETIALEKEQkLQNDFAEKERK-- 274
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKin 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 275 --------LQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLktkydEETTAKADEIemimtdLERANQRAEvaqREA 346
Cdd:pfam10174 398 vlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-----EEALSEKERI------IERLKEQRE---RED 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 347 ETLREQLSSANHSLQLASQiqkAPDVLQVDgspsssprASAVSSLLCPSQEQAiEVLTRSSLEVELAAKEREIA--QLVE 424
Cdd:pfam10174 464 RERLEELESLKKENKDLKE---KVSALQPE--------LTEKESSLIDLKEHA-SSLASSGLKKDSKLKSLEIAveQKKE 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 425 DVQRLQASLTKLRENS---------ASQISQLEQQLNAKNstlkqlEEKLKGQAdyeEVKKELNTLKSMEfapsegagTQ 495
Cdd:pfam10174 532 ECSKLENQLKKAHNAEeavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NE 594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770436 496 DSTKPLEVLLLEKNRSLQSENATLRISN-SDLSGSARRKGRDQPESRRPGPLPASPPPQ 553
Cdd:pfam10174 595 KNDKDKKIAELESLTLRQMKEQNKKVANiKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
202-363 |
6.24e-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: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 202 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 266
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 267 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 334
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 1039770436 335 ANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
192-483 |
6.37e-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: 41.10 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKSQAETIALEKE--QKLQNDFA 269
Cdd:COG5185 97 KILQEYVNSLIKLPNYEWSADILISLLYLYKSE----IVALKDELIKVEKLDEIADIEASYGEVETGIIKdiFGKLTQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 270 EKERKLQETQMSTTSKL--EEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAdEIEMIMTDLERANQRAEVAQREAE 347
Cdd:COG5185 173 NQNLKKLEIFGLTLGLLkgISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKE-IINIEEALKGFQDPESELEDLAQT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 348 TLR-EQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRA----------SAVSSLLCPSQEQAIEVLTRSSLEVELAAKE 416
Cdd:COG5185 252 SDKlEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQfentkekiaeYTKSIDIKKATESLEEQLAAAEAEQELEESK 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770436 417 REIAqlvEDVQRLQASLTKLREnsasqisQLEQQLNAKNSTLKQLEeklkGQADYEEVKKELNTLKS 483
Cdd:COG5185 332 RETE---TGIQNLTAEIEQGQE-------SLTENLEAIKEEIENIV----GEVELSKSSEELDSFKD 384
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-522 |
7.01e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKireyeqtlKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR--------KKQMEKDNSELELKMEKVFQGTDEQL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 276 QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 356 ANHSLQLASQIQKAPDVL---QVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSS-----LEVELAAKEREIAQLVEDVQ 427
Cdd:TIGR00606 382 FERGPFSERQIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 428 RLQASltklrENSASQISQLEQQLNAKNSTLKQLEEklkgQADYEEVKKELNTLKsmefapSEGAGTQDSTKPLEVLLLE 507
Cdd:TIGR00606 462 ELQQL-----EGSSDRILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQ------NEKADLDRKLRKLDQEMEQ 526
|
330
....*....|....*
gi 1039770436 508 KNRSLQSENATLRIS 522
Cdd:TIGR00606 527 LNHHTTTRTQMEMLT 541
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
157-467 |
7.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 157 QGEIDALSKRSKEAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 232
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 233 vtiKALKEKIREYEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQ 297
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 298 TALEKTRTeLFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDV 372
Cdd:PRK04863 527 QRLRQQQR-AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAW 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 373 LQVDgspssspraSAVSSLlcpsQEQAIEVLTRSslevelaakeREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 452
Cdd:PRK04863 606 LAAQ---------DALARL----REQSGEEFEDS----------QDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
330 340
....*....|....*....|..
gi 1039770436 453 -------AKNSTLKQLEEKLKG 467
Cdd:PRK04863 663 rlsqpggSEDPRLNALAERFGG 684
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
405-482 |
7.95e-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: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 405 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVK---KELNTL 481
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESL 101
|
.
gi 1039770436 482 K 482
Cdd:COG1579 102 K 102
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
210-358 |
8.39e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 210 ENQKLRETLEEYNKEfaevKNQEvtIKALKEKIREYEQTLKSQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 289
Cdd:pfam12072 61 EIHKLRAEAERELKE----RRNE--LQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 290 EHKLQTLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 358
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-476 |
8.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEeTTAKADEIEMImTDLERANQRAEVAQREAETLREQLSsanhsl 360
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRL-AEYSWDEIDVASAEREIAELEAELE------ 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 361 qlasQIQKAPDVLQVdgspsssprasavssllcpsQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREns 440
Cdd:COG4913 679 ----RLDASSDDLAA--------------------LEEQLE-----ELEAELEELEEELDELKGEIGRLEKELEQAEE-- 727
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039770436 441 asQISQLEQQLNAKNSTLKQ-----LEEKLKGQADYEEVKK 476
Cdd:COG4913 728 --ELDELQDRLEAAEDLARLelralLEERFAAALGDAVERE 766
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
207-485 |
8.68e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 207 IETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKEQKLqndfaekerKLQETQMSTTsk 285
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEaTNAEITKLRSRVDL---------KLQELQHLKN-- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 286 leEAEHkLQTLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 365
Cdd:pfam15921 539 --EGDH-LRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 366 IQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEV----LTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 441
Cdd:pfam15921 612 LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039770436 442 SQISQLEQQLNAKNSTLKQLEeklkgqadyeevkkelNTLKSME 485
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTR----------------NTLKSME 719
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
196-313 |
8.86e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.01 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 196 QLEIKVQRLHDIETENQKLRE----------TLEEYN--------KEFAEVKNQevtIKALKEKI-REYEQTLKSQAETI 256
Cdd:pfam04849 165 QLDALQEKLRGLEEENLKLRSeashlktetdTYEEKEqqlmsdcvEQLSEANQQ---MAELSEELaRKMEENLRQQEEIT 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770436 257 AL-----EKEQKLQNDFAEKERKLQ------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTK 313
Cdd:pfam04849 242 SLlaqivDLQHKCKELGIENEELQQhlqaskEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
106-450 |
9.00e-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: 40.88 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 106 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 174
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 175 ----LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 242
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 243 REYEQTLKSQAETIALEKEQKlqNDFA---EKERKLQETQMSTTSKLEEAEHKLQ------------------------T 295
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV--EDLKrklEREEKYREEAATLELEKEKLEQELQswvklaqdtglnlrspedlsrrieQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 296 LQT-----------------ALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS--- 355
Cdd:pfam05557 288 LQQreivlkeenssltssarQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydk 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 356 ----ANHSLQLASQIQKAPDVLQ--------VDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLV 423
Cdd:pfam05557 368 eltmSNYSPQLLERIEEAEDMTQkmqahneeMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLR 447
|
410 420
....*....|....*....|....*..
gi 1039770436 424 EDVQRLQASLTKLRENSASQISQLEQQ 450
Cdd:pfam05557 448 RKLETLELERQRLREQKNELEMELERR 474
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
203-542 |
9.38e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 282
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 283 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKadEIEMIMTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAK--EQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSK 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 360 LQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 439
Cdd:PTZ00108 1191 KASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGK 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770436 440 SASQISqleqqlnaKNSTLKQLEEKLKGQADYEEvkkelntlksmEFAPSEGAGTQDST-KPLEVLLLEKNRSLQSENAT 518
Cdd:PTZ00108 1271 PKNAPK--------RVSAVQYSPPPPSKRPDGES-----------NGGSKPSSPTKKKVkKRLEGSLAALKKKKKSEKKT 1331
|
330 340
....*....|....*....|....*..
gi 1039770436 519 LRISNSD---LSGSARRKGRDQPESRR 542
Cdd:PTZ00108 1332 ARKKKSKtrvKQASASQSSRLLRRPRK 1358
|
|
| |
