|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1215-1292 |
6.37e-31 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 116.54 E-value: 6.37e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 1215 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1292
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1032-1100 |
4.59e-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: 4.59e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 1032 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1100
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
643-719 |
1.99e-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: 1.99e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 643 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 719
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1338-1394 |
3.27e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 74.07 E-value: 3.27e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 1338 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1394
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-454 |
1.60e-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: 79.33 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 118 NRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaldvgQQ 196
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKE-LKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAEL-------------QE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 197 LEIKVQRLhdiETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQK--LQNDFAE 270
Cdd:TIGR02168 265 LEEKLEEL---RLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLdeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 271 KERKLQETQMSTTS---KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQR 344
Cdd:TIGR02168 342 LEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 345 EAETLREQLSSANhslqlasqiqkapdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA---SQIS 421
Cdd:TIGR02168 422 EIEELLKKLEEAE-----------------------LKELQAELEELEEELEELQEELERLEEALEELREELEeaeQALD 478
|
330 340 350
....*....|....*....|....*....|...
gi 601984298 422 QLEQQLNAKNSTLKQLEEKLKGQADYEEVKKEL 454
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-462 |
4.86e-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: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 338 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE--- 414
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRSele 897
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 415 -------NSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEF 462
Cdd:TIGR02168 898 elseelrELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1338-1395 |
1.20e-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: 1.20e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 1338 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1395
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-449 |
2.04e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyEQTLKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 276 ---QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQ 352
Cdd:COG1196 305 arlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 353 LSSANHSLQLASQIQKAPDVEQAIEvLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 432
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|....*..
gi 601984298 433 TLKQLEEKLKGQADYEE 449
Cdd:COG1196 461 LLELLAELLEEAALLEA 477
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1338-1393 |
7.10e-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: 7.10e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 1338 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1393
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-460 |
4.22e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918 388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDEETTA 320
Cdd:PRK03918 534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 321 KADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVE 400
Cdd:PRK03918 608 KDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSR 673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 401 DVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKgqaDYEEVKKELNTLKSM 460
Cdd:PRK03918 674 ELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-496 |
6.61e-12 |
|
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: 70.86 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 208 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 284
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 285 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 361
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 362 LASQIQKAPDVEQAIEVLTrSSLEVELAAKEREIAQLVEDVQ---RLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 438
Cdd:TIGR02168 328 LESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601984298 439 EKLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 496
Cdd:TIGR02168 407 ARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
167-455 |
1.01e-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: 69.60 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 167 SKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 241
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 242 IREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTA 320
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 321 KAD-----------EIEMIMTDLERANQraEVAQREAETLREQLS-SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 388
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRqIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 389 AAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQadYEEVKKELN 455
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ--LEGVRSKLD 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-459 |
1.30e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 143 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 219
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 220 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 297
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 298 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS-----ANHSLQLASQIQKAPDV 372
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkerDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 373 EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASltklRENSASqISQLEQQLNAKNSTLKQLEE-KLKGQADYEE 449
Cdd:TIGR02169 909 EAQIEKKRKrlSELKAKLEALEEELSEIEDPKGEDEEI----PEEELS-LEDVQAELQRVEEEIRALEPvNMLAIQEYEE 983
|
330
....*....|
gi 601984298 450 VKKELNTLKS 459
Cdd:TIGR02169 984 VLKRLDELKE 993
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-459 |
8.89e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 270
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 271 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQREAETLR 350
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 351 EQLSSanhslqLASQIQKAPDVEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAK 430
Cdd:TIGR04523 391 SQIND------LESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNL 459
|
250 260
....*....|....*....|....*....
gi 601984298 431 NSTLKQLEEKLKgqadyeEVKKELNTLKS 459
Cdd:TIGR04523 460 DNTRESLETQLK------VLSRSINKIKQ 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-459 |
1.00e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 197 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 276
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 277 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssA 356
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL--A 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 357 NHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKN 431
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreKLEKLKREINELK 405
|
250 260
....*....|....*....|....*....
gi 601984298 432 STLKQL-EEKLKGQADYEEVKKELNTLKS 459
Cdd:TIGR02169 406 RELDRLqEELQRLSEELADLNAAIAGIEA 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
212-438 |
3.45e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 290
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 291 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 370
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 371 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 438
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-457 |
3.51e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtPEDLR-KQVAPLLKSFQGE-----IDALSKRSKEAEaaflT 176
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKlKELAEQLKELEEKlkkynLEELEKKAEEYE----K 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 177 VYKRLIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlks 251
Cdd:PRK03918 530 LKEKLIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 252 qaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTD 331
Cdd:PRK03918 600 -----FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLE 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 332 LERANQRAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAslt 410
Cdd:PRK03918 671 LSRELAGLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA--- 735
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 601984298 411 KLRENSASQISQLEQQL-----NAKNS--TLKQLEEKLKGQADYEEVKKELNTL 457
Cdd:PRK03918 736 LLKERALSKVGEIASEIfeeltEGKYSgvRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-419 |
4.41e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 190 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 266
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 267 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 341
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 342 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 419
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-368 |
9.26e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 275 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 601984298 351 EQLSSANHSLQLASQIQK 368
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-460 |
9.34e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 95 RWMLCvagAKLKRELDA-------TATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRS 167
Cdd:COG4717 44 RAMLL---ERLEKEADElfkpqgrKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 168 KEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQ 247
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 248 TLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEM 327
Cdd:COG4717 178 ELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 328 IMT--------DLERANQRAEVAqrEAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLE------------VE 387
Cdd:COG4717 254 IAAallallglGGSLLSLILTIA--GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeeeleellaalgLP 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 388 LAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 460
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-407 |
9.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSfQGEIDALSKRSKEAEAAFLTVYKRLi 182
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARL-EQDIARLEERRRELEERLEELEEEL- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 dvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiALEKEQ 262
Cdd:COG1196 326 --------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEI-EMIMTDLERANQRAEV 341
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeEEEALLELLAELLEEA 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 342 AQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 407
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-459 |
2.14e-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: 62.35 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 270
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 271 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 348
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 349 lrEQLSSANHSLqLASQIQKAPDVEQAIEvlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLN 428
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQKEK--EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKN 641
|
250 260 270
....*....|....*....|....*....|..
gi 601984298 429 AKNSTLKQLEEKLKG-QADYEEVKKELNTLKS 459
Cdd:TIGR04523 642 KLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-406 |
2.32e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKR 180
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 181 LIDVpdpvpaldvGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI 256
Cdd:COG1196 297 LARL---------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 257 -----ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtd 331
Cdd:COG1196 368 leaeaELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE----- 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601984298 332 lERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtRSSLEVELAAKEREiAQLVEDVQRLQ 406
Cdd:COG1196 443 -ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADY-EGFLEGVKAAL 514
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
121-442 |
2.41e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 60.31 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 121 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 197
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 198 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 277
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 278 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 357
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 358 HSLQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQL 437
Cdd:COG1340 216 KEIVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEI 272
|
....*
gi 601984298 438 EEKLK 442
Cdd:COG1340 273 FEKLK 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-384 |
2.81e-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: 62.38 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 180
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 181 lidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 260
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 261 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 601984298 338 RAEVAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 384
Cdd:TIGR02168 500 NLEGFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-460 |
4.23e-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: 60.55 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 251 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKtkydeettakaDEIEMI 328
Cdd:COG4942 17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALE-----------QELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 329 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKERE 394
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 395 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSM 460
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEAL 228
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
103-513 |
7.10e-09 |
|
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: 61.01 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YK 179
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 180 RLIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 259 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 337
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 338 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA 407
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDV 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 408 -SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLkGQAdyeevKKELNTLK-SMEFAPSEGAGTQDSTKPL----EVLL 481
Cdd:pfam12128 593 pEWAASEEELRERLDKAEEALQSAREKQAAAEEQL-VQA-----NGELEKASrEETFARTALKNARLDLRRLfdekQSEK 666
|
410 420 430
....*....|....*....|....*....|..
gi 601984298 482 LEKNRSLQSENATLRISNSDLSGSARRKGRDQ 513
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-445 |
1.10e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 206 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERKLQETQMsttsK 285
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELEK----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQ 365
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA------ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 366 IQkapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 445
Cdd:COG4942 166 RA-----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-459 |
2.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 227 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 299
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 300 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLSSANHslqlasqiqkapdveQAIEvl 379
Cdd:COG4913 297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQIRGNGG---------------DRLE-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 380 trsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLNAKNSTLKQLEEKL--------KGQ 444
Cdd:COG4913 342 ---QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALaeaeaalrDLR 418
|
250
....*....|....*
gi 601984298 445 ADYEEVKKELNTLKS 459
Cdd:COG4913 419 RELRELEAEIASLER 433
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
216-437 |
2.16e-08 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 56.07 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 216 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 287
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 288 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 361 QlasqiQKAPD----VEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLNAKNSTLK 435
Cdd:pfam13851 137 Q-----QKTGLknllLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIK 198
|
..
gi 601984298 436 QL 437
Cdd:pfam13851 199 DL 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-459 |
2.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 258
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 259 EKEQ------------------KLQNDFAEKERKLQETQMSTT----------SKLEEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 311 KTKYDEETTAKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP-- 370
Cdd:PRK03918 358 EERHELYEEAKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 371 --------DVEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLNAKN 431
Cdd:PRK03918 438 cpvcgrelTEEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN 516
|
330 340
....*....|....*....|....*...
gi 601984298 432 stLKQLEEKLKgqaDYEEVKKELNTLKS 459
Cdd:PRK03918 517 --LEELEKKAE---EYEKLKEKLIKLKG 539
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
274-455 |
3.06e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 274 KLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLRE 351
Cdd:COG1579 11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 352 QLSSA--NHSLQ-LASQIQKApdvEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 426
Cdd:COG1579 81 QLGNVrnNKEYEaLQKEIESL---KRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 601984298 427 LNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 455
Cdd:COG1579 158 LEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
116-461 |
4.30e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 116 LANRQDESEQSRKRLIEQSREF-----KKNTPEDLRKQVAPLlksfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 190
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakaKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 191 LD-VGQQLEIKVQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAET 255
Cdd:PRK03918 417 LKkEIKELKKAIEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEkerkLRKELRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 256 IALEK--------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK03918 496 IKLKElaeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 311 KTKYDEETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLT 380
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 381 RSSLEVELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTL 457
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKY 733
|
....
gi 601984298 458 KSME 461
Cdd:PRK03918 734 KALL 737
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
143-335 |
7.42e-08 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 55.84 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 601984298 300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
236-440 |
9.03e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.95 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 236 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 298
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 299 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 362
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 363 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQL 437
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 601984298 438 EEK 440
Cdd:PHA02562 399 VKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-445 |
1.43e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 110 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRlid 183
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 184 vPDPVPALDvgQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIAlEKEQK 263
Cdd:PRK02224 383 -REEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 264 LQ-NDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 340
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 341 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 417
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 601984298 418 SQISQLEQQ--------------LNAKNSTLKQLEEKLKGQA 445
Cdd:PRK02224 606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-458 |
1.57e-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: 56.37 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 204 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 273
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 274 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 351 EQLSSANHSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASL 409
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 601984298 410 TklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 458
Cdd:pfam10174 432 S----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
141-506 |
2.64e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 141 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFltvykrlidvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEE 220
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTAL--------------------KNARLDLRRLFD---EKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 221 YNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQt 295
Cdd:pfam12128 672 ALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 296 lQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVE 373
Cdd:pfam12128 749 -LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIE 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 374 QAIEvltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEvkkE 453
Cdd:pfam12128 821 RAIS--------------------------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS---K 871
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 454 LNTLKsmEFAPSEGAGTQDSTKP--LEVLLLEKNR---SLQSENATLRISNSDLSGSA 506
Cdd:pfam12128 872 LATLK--EDANSEQAQGSIGERLaqLEDLKLKRDYlseSVKKYVEHFKNVIADHSGSG 927
|
|
| 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 601984298 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 275 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 601984298 355 S 355
Cdd:COG4913 430 S 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-444 |
2.89e-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: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 281
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 282 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 357
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 358 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA-KNSTLKQ 436
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPE 831
|
....*...
gi 601984298 437 LEEKLKGQ 444
Cdd:COG4913 832 YEERFKEL 839
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-460 |
3.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 181 LIDVPDPVPALDVGQQLEIKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKS 251
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 252 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLk 311
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 312 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA-- 389
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAel 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 390 ------------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKE 453
Cdd:COG3206 283 sarytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLERE 359
|
....*..
gi 601984298 454 LNTLKSM 460
Cdd:COG3206 360 VEVAREL 366
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
99-495 |
3.92e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 55.08 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 99 CVAGAKLKRELDATATVLANRQDESEQSRKRlieQSREFKKNTPEDLRKQVAPLLKSFQ------GEIDALSKRSKEAEA 172
Cdd:COG5022 830 KKLRETEEVEFSLKAEVLIQKFGRSLKAKKR---FSLLKKETIYLQSAQRVELAERQLQelkidvKSISSLKLVNLELES 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 173 ---------------------AFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHdieTENQKLRETLEEYNKEFAEVKNQ 231
Cdd:COG5022 907 eiielkkslssdlienlefktELIARLKKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTIL 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 232 EVTIKALKEKIREYEQTLKS--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHK 292
Cdd:COG5022 984 VREGNKANSELKNFKKELAElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQ 1063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 293 LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQ----LASQIQK 368
Cdd:COG5022 1064 ARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskfLSQLVNT 1141
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 369 APDVEQAIEV-------LTRSSLEVELAAKEREIAqLVEDVQRLQASLTKLRENSASQISQLEQQLNAK------NSTLK 435
Cdd:COG5022 1142 LEPVFQKLSVlqleldgLFWEANLEALPSPPPFAA-LSEKRLYQSALYDEKSKLSSSEVNDLKNELIALfskifsGWPRG 1220
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984298 436 QLEEKLKGQA-DYEEVKKELNTLKSMEFAPSEGAGtQDSTKPLEVL-LLEKNRSLQSENATL 495
Cdd:COG5022 1221 DKLKKLISEGwVPTEYSTSLKGFNNLNKKFDTPAS-MSNEKLLSLLnSIDNLLSSYKLEEEV 1281
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
190-457 |
5.56e-07 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 53.42 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 190 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 264
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 265 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 344
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 345 eaetLREQLSSANHSLQ----------------------LASQIQKAPDVEQAIEVLTRSSL----------EVELAAKe 392
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinigkQVFTITITTATTKTVDVTSIGGLingignasddEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601984298 393 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 457
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-456 |
6.22e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 210 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 286
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 287 EEAEhKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 364
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 365 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250
....*....|....
gi 601984298 443 GQADYEEVKKELNT 456
Cdd:pfam02463 413 LARQLEDLLKEEKK 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-442 |
7.67e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DVGQQLEIKVQ-----RLHDIETENQKLRETLEEY--NKEFAevknqEVTIKALKEKIREYEQTlksQAETIALEKE-QK 263
Cdd:PRK02224 191 QLKAQIEEKEEkdlheRLNGLESELAELDEEIERYeeQREQA-----RETRDEADEVLEEHEER---REELETLEAEiED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 264 LQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTE----------LFDLKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PRK02224 263 LRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 334 RANQRAEVAQREAETLREQLSSANhslqlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL- 412
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELR---------EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDAp 404
|
250 260 270
....*....|....*....|....*....|..
gi 601984298 413 --RENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:PRK02224 405 vdLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-449 |
7.87e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 111 ATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpA 190
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEI-----EDLRETIAETER----EREELAEEVRDLRERLEELEEERDDLLAEA-G 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 191 LDVGQQlEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlksqaetialEKEQKLQNDFAE 270
Cdd:PRK02224 304 LDDADA-EAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 271 KERKLQETQMSTT---SKLEEAEHKLQTLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:PRK02224 368 LESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 348 TLRE--QLSSANHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQL 423
Cdd:PRK02224 447 ALLEagKCPECGQPVEGSPHVETIEEDRERVEELEaeLEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELI 525
|
330 340
....*....|....*....|....*.
gi 601984298 424 EQQLNAKNSTLKQLEEKLKGQADYEE 449
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEA 551
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
193-454 |
9.68e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 193 VGQQLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam05483 132 VSLKLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 259 EKEQKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKA 322
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 323 DEIEMIMTDLERANQRAEVAQReaeTLREQLSSANHSL-QLASqiQKAPDVEQAIEVLTRSSLEV-ELAAKEREIAQLVE 400
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQK---ALEEDLQIATKTIcQLTE--EKEAQMEELNKAKAAHSFVVtEFEATTCSLEELLR 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 401 -DVQRLqasltklrENSASQISQLEQQLNAKNSTLKQLEE-KLKGQADYEEVKKEL 454
Cdd:pfam05483 367 tEQQRL--------EKNEDQLKIITMELQKKSSELEEMTKfKNNKEVELEELKKIL 414
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-461 |
9.76e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 104 KLKRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykrlid 183
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL-------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 184 vpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEKeQK 263
Cdd:pfam05483 445 -------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN-KE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 264 LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIMTDL 332
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 333 ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRl 405
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK- 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601984298 406 QASLTKLRENS-----------ASQISQLEQQLNA----KNSTLKQLEEKLKGQAD--YEEVKKELNTLKSME 461
Cdd:pfam05483 662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-484 |
1.03e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRA 339
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 340 EVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA- 417
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEeLQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQa 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601984298 418 -------SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEK 484
Cdd:COG4372 176 lseaeaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-446 |
1.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykrli 182
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 dvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4913 688 ------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 341
Cdd:COG4913 750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 342 AQREAETL-------REQLSSANHS--LQLASQIQKAP-DVEQAIEVLTRSSLEVE--------LAAKEREiaqlVEDVQ 403
Cdd:COG4913 822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIrEIKERIDPLNDSLKRIPfgpgrylrLEARPRP----DPEVR 897
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 601984298 404 RLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQAD 446
Cdd:COG4913 898 EFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEE 937
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-442 |
1.45e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 186 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 264
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 265 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 341
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 342 AQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAAKEREIA---QLVEDVQRLQASLTKLRENSAS 418
Cdd:PRK11281 169 SQRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQALLNAQNDlqrKSLEGNTQLQDLLQKQRDYLTA 234
|
250 260 270
....*....|....*....|....*....|.
gi 601984298 419 QISQLEQQL-------NAKNstLKQLEEKLK 442
Cdd:PRK11281 235 RIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-353 |
1.60e-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: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 177
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 178 YKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTLKSQA 253
Cdd:TIGR02168 816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 254 ETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 331
Cdd:TIGR02168 887 EALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
|
250 260
....*....|....*....|..
gi 601984298 332 LERANQRAEVAQREAETLREQL 353
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-513 |
1.66e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 373
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 374 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKLKG-Q 444
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLESlQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 445 ADYEEVKKELNTLKsmefapsegagTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQ 513
Cdd:COG4372 164 EELAALEQELQALS-----------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-453 |
2.44e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLI 182
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI---- 256
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkade 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 257 ---ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PTZ00121 1515 akkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 334 --RANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTK 411
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 601984298 412 LRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 453
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-504 |
2.46e-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: 52.67 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 213 KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTL--KSQAETIALEKEQKLQN---DFAEKERKLQETQMSTT---- 283
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEeelKLLAKEEEELKSELLKLerrk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 284 ----SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImTDLERANQRAEVAQREAETLREQLSSANHS 359
Cdd:pfam02463 310 vddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-EELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 360 LQLASQIQKAPDVEQAIEVltrsSLEVELAAKEREIAQLvedvqrlqASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 439
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEA----QLLLELARQLEDLLKE--------EKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601984298 440 KLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-628 |
2.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 361 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 425
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 426 QLNAKNSTLKQLEEKlkgQADYEEVKKEL-NTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELeAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 505 SARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGKFALNSLLQRQL 584
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 601984298 585 MQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGM 628
Cdd:COG3883 333 GSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYV 376
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
843-1026 |
2.49e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 843 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 920
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 921 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 1000
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 601984298 1001 NSPLPSSPIVPMAKPAKPSVPPLTPE 1026
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
199-412 |
2.52e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 199 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 275 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlERANQRAEvA 342
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EIMDEFNE-Q 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 343 QREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 412
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
259-515 |
2.60e-06 |
|
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: 52.05 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 259 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 339 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVElAAKER--EIAQLVED 401
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVK-NSKSElaRIPELEKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 402 VQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefapsegAGTQDSTKPL 477
Cdd:pfam05557 206 LERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL-------AQDTGLNLRS 277
|
250 260 270
....*....|....*....|....*....|....*...
gi 601984298 478 EVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPE 515
Cdd:pfam05557 278 PEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-459 |
2.86e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQ-----------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:COG4717 266 GSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 332 LERANQ-RAEVAQREAETLREQLSSANHSL----------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVE 400
Cdd:COG4717 346 IEELQElLREAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984298 401 DVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEklkgQADYEEVKKELNTLKS 459
Cdd:COG4717 426 DEEELEEELEELEEELEEleeELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-495 |
3.75e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 203 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKSQAETIALEKEQK----------LQND 267
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEIIQEQARNQnsmymrqlsdLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 348 TLREQlssanhslqlasqiqkapDVEQAIevlTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSASQISQLEQQL 427
Cdd:pfam15921 402 RLWDR------------------DTGNSI---TIDHLRRELDDRNME-------VQRLEALLKAMKSECQGQMERQMAAI 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984298 428 NAKNSTLKQ---LEEKLKGQADY-EEVKKELnTLKSMEFAPSEgagtqDSTKPLEVLLLEKNRSLQSENATL 495
Cdd:pfam15921 454 QGKNESLEKvssLTAQLESTKEMlRKVVEEL-TAKKMTLESSE-----RTVSDLTASLQEKERAIEATNAEI 519
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-461 |
3.97e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQL-----QAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 275 LQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4372 103 LESLQ-EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 355 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 434
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260
....*....|....*....|....*..
gi 601984298 435 KQLEEKLKGQADYEEVKKELNTLKSME 461
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEAL 288
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-459 |
4.82e-06 |
|
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: 51.56 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKSQaETIALEKEQKLQND--FAEK 271
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 272 ERKLQETQMSTT----SKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQraeva 342
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEkqkkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEElENELNLLEKEKLNI----- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 343 QREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 419
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 601984298 420 ISQLE---QQLNAKNSTLKQLEEKLKgqadyeEVKKELNTLKS 459
Cdd:TIGR04523 266 KKQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-445 |
5.03e-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: 51.38 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 197 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 262
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 334
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 335 ANQRAE---VAQREAETLREQLSSANHSL-----QLAS-------QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL- 398
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSrlgelklRLNQATATPELLLQLENFDERIERAREEQEAANAe 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 601984298 399 VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 445
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
211-438 |
6.56e-06 |
|
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: 50.91 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 211 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 290 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 361
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 362 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLNAKNSTLKQL 437
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 601984298 438 E 438
Cdd:pfam07111 297 E 297
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
226-472 |
7.76e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKLQTLQTALEK 302
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 303 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEqaievltRS 382
Cdd:COG4372 85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE-------LK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 383 SLEVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEF 462
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250
....*....|
gi 601984298 463 APSEGAGTQD 472
Cdd:COG4372 232 GLALSALLDA 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
204-501 |
8.31e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 204 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKSqAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 276 -QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 354
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 355 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQL 427
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601984298 428 NAKNSTLKQLEEKLKGQADyEEVKKELNTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSD 501
Cdd:TIGR01612 1214 GINLSYGKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
201-512 |
8.63e-06 |
|
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: 50.74 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 201 VQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQM 280
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 361 QLASQIQK------APDVEQAIEVLT----------------------RSSLEVELAAKEREIAQLVED----------- 401
Cdd:TIGR00618 746 KELMHQARtvlkarTEAHFNNNEEVTaalqtgaelshlaaeiqffnrlREEDTHLLKTLEAEIGQEIPSdedilnlqcet 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 402 -VQRLQASLTKLRENSASQIsQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAgtqdSTKPLEVL 480
Cdd:TIGR00618 826 lVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDA----LIKFLHEI 900
|
330 340 350
....*....|....*....|....*....|..
gi 601984298 481 LLEKNRSLQSENATLRISNSDLSGSARRKGRD 512
Cdd:TIGR00618 901 TLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-461 |
1.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 204 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKlqndfAEKERKLQEtqmstt 283
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 284 skLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 363
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 364 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQqlnaKNSTLKQLEEKLK 442
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEE----KEERLEELKKKLK 348
|
250 260
....*....|....*....|...
gi 601984298 443 G-QADYEEVK---KELNTLKSME 461
Cdd:PRK03918 349 ElEKRLEELEerhELYEEAKAKK 371
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-495 |
1.57e-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: 50.05 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 295 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLASQ 365
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 366 IQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:TIGR00606 392 IKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 443 G--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 495
Cdd:TIGR00606 472 RilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-439 |
1.64e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 207 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 286
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 287 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 349
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 350 REQLSsanhslQLASQIQKAPDVEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNA 429
Cdd:COG3206 316 ASLEA------ELEALQAREASLQAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEAL 383
|
250
....*....|
gi 601984298 430 KNSTLKQLEE 439
Cdd:COG3206 384 TVGNVRVIDP 393
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
154-459 |
1.74e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 154 KSFQGEIDAlSKRSKEAEAAFLTVYKRLIDVpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV 233
Cdd:TIGR01612 1496 KGCKDEADK-NAKAIEKNKELFEQYKKDVTE-----LLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 234 TIKALK-EKIR---EYEQTLKSQAETIALEKE-QKLQNDFAE------------KERKLQETQMSTTS------KLEEAE 290
Cdd:TIGR01612 1570 KIKEIKkEKFRiedDAAKNDKSNKAAIDIQLSlENFENKFLKisdikkkindclKETESIEKKISSFSidsqdtELKENG 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 291 HKLQTLQTALEKTRTE---LFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQRE-----AETLREQLSSANHSLQl 362
Cdd:TIGR01612 1650 DNLNSLQEFLESLKDQkknIEDKKKELDELDS----EIEKIEIDVDQHKKNYEIGIIEkikeiAIANKEEIESIKELIE- 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 363 asqiqkaPDVEQAIEVLTRSSLE-----VELAAKEREIAQLVEDVQRLQASLTK-LRENSASQISQLE---QQLNAKNST 433
Cdd:TIGR01612 1725 -------PTIENLISSFNTNDLEgidpnEKLEEYNTEIGDIYEEFIELYNIIAGcLETVSKEPITYDEiknTRINAQNEF 1797
|
330 340 350
....*....|....*....|....*....|.
gi 601984298 434 LKQLEEKLKGQA-----DYEEVKKELNTLKS 459
Cdd:TIGR01612 1798 LKIIEIEKKSKSylddiEAKEFDRIINHFKK 1828
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-463 |
1.94e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 204 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KSQAETIALE-KEQKLQNDFAEKERKLQE 277
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 278 TQMSTTSKleeaEHKLQTLQTALEKTRTEL------FDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam10174 329 LKESLTAK----EQRAAILQTEVDALRLRLeekesfLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 348 TLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVE-----DVQRLQ--ASLTKLRENSASQI 420
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEqrereDRERLEelESLKKENKDLKEKV 484
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 601984298 421 SQLEQQLNAKNSTLKQLEEKLKGQADyEEVKKElNTLKSMEFA 463
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-455 |
2.00e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlKSQAETIALEKEQKLQNDFAEKERKLQETQMS 281
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN--LVQTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 282 T---TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 344
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 345 EAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVElaakeREIAQlvedvQRLQASLTKLRE--NSASQISQ 422
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEVS-----RSEAW-----DVARELLRRLREqrHLAEQLQQ 517
|
250 260 270
....*....|....*....|....*....|...
gi 601984298 423 LEQQLNAknstlkqLEEKLKGQADYEEVKKELN 455
Cdd:PRK04863 518 LRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
127-440 |
2.00e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 127 RKRLIEQSREFKKntpeDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaldvgQQLEiK 200
Cdd:COG3096 280 RRELSERALELRR----ELFGARRQLaeeqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL------RQQE-K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 201 VQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKE 272
Cdd:COG3096 349 IERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 273 RKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE---- 340
Cdd:COG3096 427 ALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARellr 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 341 -------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTKL 412
Cdd:COG3096 503 ryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAEA 576
|
330 340
....*....|....*....|....*...
gi 601984298 413 REnsasQISQLEQQLNAKNSTLKQLEEK 440
Cdd:COG3096 577 VE----QRSELRQQLEQLRARIKELAAR 600
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
203-312 |
2.09e-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: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 601984298 277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
202-344 |
2.67e-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: 47.23 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 202 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 271
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601984298 272 E-RKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTdlERANQRAEVAQR 344
Cdd:COG1579 111 EiLELMERIEELEEELAELEAELAELEAELEEKKAEL-------DEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
116-490 |
3.01e-05 |
|
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: 48.53 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 116 LANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAafltvYKRLIDV----PDPVPAL 191
Cdd:pfam05622 63 LLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLEL----QHRNEELTSLAEEAQA-----LKDEMDIlresSDKVKKL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DvgQQLEIKVQRLHDIETENQKLReTLEEYNKEFAEVKNQevtikaLKEKIREYeQTLKSQAETIalekEQKLQndfaEK 271
Cdd:pfam05622 134 E--ATVETYKKKLEDLGDLRRQVK-LLEERNAEYMQRTLQ------LEEELKKA-NALRGQLETY----KRQVQ----EL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 272 ERKLQEtQMSTTSKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD---------------- 331
Cdd:pfam05622 196 HGKLSE-ESKKADKLEfeykKLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADallspssdpgdnlaae 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 332 ------------LERANQRAEVAQREAE-----TLREQLSSANHSL-----QLASQIQKAPDVEQAIEVLTRSSLEV--- 386
Cdd:pfam05622 275 impaeireklirLQHENKMLRLGQEGSYrerltELQQLLEDANRRKneletQNRLANQRILELQQQVEELQKALQEQgsk 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 387 --ELAAKEREIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLNAKNSTLKQLEEKLKgqadyEEVKKE 453
Cdd:pfam05622 355 aeDSSLLKQKLEEHLEKLHEAQSELQKKKEqieelepkqdsNLAQKIDELQEALRKKDEDMKAMEERYK-----KYVEKA 429
|
410 420 430
....*....|....*....|....*....|....*..
gi 601984298 454 LNTLKSMEfaPSEGAGTQDSTKPLEVLLLEKNRSLQS 490
Cdd:pfam05622 430 KSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-331 |
3.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrli 182
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 dvPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQ 262
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 263 KLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
157-443 |
3.76e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 157 QGEIDALSKRSKEAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 232
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 233 vtiKALKEKIREYEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQ 297
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 298 TALEKTRTeLFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDV 372
Cdd:PRK04863 527 QRLRQQQR-AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAW 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 373 EQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQLEEKLKG 443
Cdd:PRK04863 606 LAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
306-458 |
4.08e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 306 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 382
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 383 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 458
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-322 |
4.15e-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: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 116 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL 191
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDF 268
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 601984298 269 AEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 322
Cdd:COG3206 337 AQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1338-1423 |
4.53e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 1338 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1417
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 601984298 1418 RSSRAA 1423
Cdd:COG5576 121 EEADLA 126
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-458 |
5.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKEQ 262
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 343 QREAETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 415
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 601984298 416 SASQISQ-LEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 458
Cdd:COG1196 730 LEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
212-461 |
5.75e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMSTTSKLEEAEH 291
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKLRSRVDL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 292 KLQTLQtALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQ------------RAEVAQREAETLREQLSSA 356
Cdd:pfam15921 529 KLQELQ-HLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 357 NHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER---------EIAQLVEDVQRLQASLTKLRENsasqISQLEQQL 427
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlravkdikqERDQLLNEVKTSRNELNSLSED----YEVLKRNF 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 601984298 428 NAKNSTLKQLEEKLKGQ--ADYEEVKKELNTLKSME 461
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQlkSAQSELEQTRNTLKSME 719
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-449 |
5.91e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 208 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 352
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 353 LSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--- 413
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaql 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 601984298 414 ----ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 449
Cdd:pfam01576 239 akkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
198-349 |
6.39e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 198 EIKVQRLHDIETENQKLRETLE-EYNKEFAEVKNQEvtikalkEKIREYEQTLKSQAETIALEKEQ---------KLQND 267
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEElekkekeleQKQQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 268 FAEKERKLQETQMSTTSKLEEA------EHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDlerANQR-- 338
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERIsgltaeEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADkKAKEILAQ---AIQRca 202
|
170
....*....|.
gi 601984298 339 AEVAqreAETL 349
Cdd:PRK12704 203 ADHV---AETT 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
239-439 |
8.90e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 239 KEKIREYEQTLKSQAETIA----LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALektrtelfdlktKY 314
Cdd:PRK04863 279 NERRVHLEEALELRRELYTsrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL------------RQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 315 DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHS-LQLASQIQkapDVEQAIEVLTRSSLE----VELA 389
Cdd:PRK04863 347 QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEvDELKSQLA---DYQQALDVQQTRAIQyqqaVQAL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 601984298 390 AKEREIAQL----VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 439
Cdd:PRK04863 424 ERAKQLCGLpdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
134-453 |
9.68e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 134 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQLEIKVQRLHDIETENQK 213
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 214 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKL 293
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 294 QTLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLSSANHSLQLASQIQK 368
Cdd:TIGR00618 331 AAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 369 APDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQLNAKNSTLKQLEEKLK 442
Cdd:TIGR00618 404 ILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHL 483
|
330
....*....|.
gi 601984298 443 gqaDYEEVKKE 453
Cdd:TIGR00618 484 ---QETRKKAV 491
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
106-502 |
1.02e-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: 47.04 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 106 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 174
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 175 ----LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 242
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 243 REYEQTLKSQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKLQTLQTALEKTRTELfdlktkYDEETTAKA 322
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 323 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVED 401
Cdd:pfam05557 271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 402 VQRLQASLTKLRENSASQISQLEQQLNAKNSTlKQLEEKLKGQADY-EEVKKELNTLK-SMEFAPSEGAGTQDSTKPLEV 479
Cdd:pfam05557 344 LQRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
|
410 420 430
....*....|....*....|....*....|....*...
gi 601984298 480 LLLEKNR---------------SLQSENATLRISNSDL 502
Cdd:pfam05557 423 ELQALRQqesladpsyskeevdSLRRKLETLELERQRL 460
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
196-446 |
1.13e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.82 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 196 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 273
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 346
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 347 ETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQLVE 400
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 601984298 401 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 446
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
805-1050 |
1.30e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 805 ILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEA 884
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 885 QDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQG 964
Cdd:PRK10263 363 VPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 965 PSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLtpeqyevYMYQEVD 1037
Cdd:PRK10263 442 VAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL-------YYFEEVE 513
|
250
....*....|...
gi 601984298 1038 tiELTRQVKEKLA 1050
Cdd:PRK10263 514 --EKRAREREQLA 524
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
249-453 |
1.33e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 249 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 327
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 328 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQA 407
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-------------EEELE-----KKEKELEQKQQELEKKEEELEELIE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 601984298 408 SLTKLRENsasqISQLEQQlNAKNSTLKQLEEKLKGQA-----DYEEVKKE 453
Cdd:PRK12704 139 EQLQELER----ISGLTAE-EAKEILLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-366 |
1.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 145 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 215
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 216 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 289
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 290 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMI---MTDLERANQRAEVAQREAETLREQLSSAN--HSLQLAS 364
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELkaeLRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
..
gi 601984298 365 QI 366
Cdd:COG4717 523 EY 524
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-458 |
1.67e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 139 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLTVYKRLIDVPDPVPAL----DVG 194
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 195 QQLEIKVQ----RLHDIETENQKLRETLEEYNK--------------EFAEVKNQEVT----IKALKEKIREYEQTLKSq 252
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiindpvyknrnyinDYFKYKNDIENkkqiLSNIDAEINKYHAIIKK- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 253 aetiaLEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDL 332
Cdd:PRK01156 331 -----LSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 333 ERANQRAEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT--------------------------- 380
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynek 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 381 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKE 453
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNR 554
|
....*
gi 601984298 454 LNTLK 458
Cdd:PRK01156 555 YKSLK 559
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
226-444 |
1.80e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETialekeqklqNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 306 ELFD------LKTKYDEETTAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEV 378
Cdd:pfam12795 73 EILAslsleeLEQRLLQTSAQLQELQN----QLAQLNSQLIELQTRPERAQQQLSEARQRLQqIRNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 379 LTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 444
Cdd:pfam12795 149 AQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-461 |
2.26e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 125 QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKrlidvpdpvpaldvgqqLE 198
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEHNLSKIMK-----------------LD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 199 IKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----KIREYEQTL-KSQAETIALEKEQKLQNdfaeKER 273
Cdd:TIGR00606 269 NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrTVREKERELvDCQRELEKLNKERRLLN----QEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 274 KLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDEETTAK----------ADEIEMIMTDLERANQRA 339
Cdd:TIGR00606 343 TELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnfhtlvierqEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 340 EVAQREAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LAAKEREIAQLVEDVQRLQASLTKLRENSAS 418
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLEGSSDRILELDQELRKAERELSKAEKNSLT 496
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 601984298 419 QiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 461
Cdd:TIGR00606 497 E-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
203-518 |
2.40e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.19 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 282
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 283 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVAQREAETLREQLS 354
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKKKKKSSADKSKKA 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 355 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 434
Cdd:PTZ00108 1193 SVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPK 1272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 435 KQLEEKLKGQADYEEVKKELNTLKSmeFAPSEGAGTQDST-KPLEVLLLEKNRSLQSENATLRISNSD---LSGSARRKG 510
Cdd:PTZ00108 1273 NAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVkKRLEGSLAALKKKKKSEKKTARKKKSKtrvKQASASQSS 1350
|
....*...
gi 601984298 511 RDQPESRR 518
Cdd:PTZ00108 1351 RLLRRPRK 1358
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
113-439 |
2.52e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 113 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 192
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 193 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 271
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 272 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 345
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 346 AETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ 406
Cdd:pfam07888 253 VEGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
|
330 340 350
....*....|....*....|....*....|....
gi 601984298 407 ASLTKLRensaSQISQLEQQL-NAKNSTLKQLEE 439
Cdd:pfam07888 332 ERLQEER----MEREKLEVELgREKDCNRVQLSE 361
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
202-307 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 202 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 265
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 601984298 266 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 307
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
197-529 |
2.93e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 197 LEIKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKSQAETIALEKEQkLQNDFAEKERK-- 274
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKin 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 275 --------LQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLktkydEETTAKADE-IEMIMTDLERANQ--RAEVAQ 343
Cdd:pfam10174 398 vlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-----EEALSEKERiIERLKEQREREDRerLEELES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 344 --REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLRENS--- 416
Cdd:pfam10174 473 lkKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAEeav 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 417 ------ASQISQLEQQLNAKNstlkqlEEKLKGQAdyeEVKKELNTLKSMEfapsegagTQDSTKPLEVLLLEKNRSLQS 490
Cdd:pfam10174 551 rtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NEKNDKDKKIAELESLTLRQM 613
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 601984298 491 ENATLRISN-SDLSGSARRKGRDQPESRRPGPLPASPPPQ 529
Cdd:pfam10174 614 KEQNKKVANiKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
206-468 |
2.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 206 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKSQAETIALEKEQKLqndfAEKERKLQETQMSTTS 284
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 285 KLEEAEHKLQTLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 364
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 365 QIQKAPDVEQAIEVltRSSLEVELAakereiaqlvEDVQRLQASLTKLRENSASQISQLEQQLNAKnsTLKQLEEKLKGQ 444
Cdd:PTZ00121 1174 DAKKAEAARKAEEV--RKAEELRKA----------EDARKAEAARKAEEERKAEEARKAEDAKKAE--AVKKAEEAKKDA 1239
|
250 260
....*....|....*....|....
gi 601984298 445 ADYEEVKKELNTLKSMEFAPSEGA 468
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMA 1263
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
192-459 |
3.17e-04 |
|
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: 45.33 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKSQAETIALEK-------EQKL 264
Cdd:COG5185 97 KILQEYVNSLIKLPNYEWSADILISLLYLYKSE----IVALKDELIKVEKLDEIADIEASYGEVETGIIkdifgklTQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 265 -QNDFAEKERKLQETQMSTTSKLEEAEH-----------------KLQTLQTALEKTRTE----LFDLKTKYDEETTAKA 322
Cdd:COG5185 173 nQNLKKLEIFGLTLGLLKGISELKKAEPsgtvnsikesetgnlgsESTLLEKAKEIINIEealkGFQDPESELEDLAQTS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 323 DEIEMIMTD-----LERANQRAEVAQR---EAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEVELAAKER 393
Cdd:COG5185 253 DKLEKLVEQntdlrLEKLGENAESSKRlneNANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKR 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 394 EIAqlvEDVQRLQASLTKLREnsasqisQLEQQLNAKNSTLKQLEeklkGQADYEEVKKELNTLKS 459
Cdd:COG5185 333 ETE---TGIQNLTAEIEQGQE-------SLTENLEAIKEEIENIV----GEVELSKSSEELDSFKD 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-537 |
3.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KlqndfAEKERKLQETQmsttSKLEEAEHKLQTLQTALE-KTRTE----LFDLKTKYDE-----------ETTAKADEIE 326
Cdd:PTZ00121 1406 K-----ADELKKAAAAK----KKADEAKKKAEEKKKADEaKKKAEeakkADEAKKKAEEakkaeeakkkaEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 327 MIMTDLERANQ---RAEVAQREAETLREQLSSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSS 383
Cdd:PTZ00121 1477 KKAEEAKKADEakkKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 384 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQadyEEVKKELNTLKSMEfa 463
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA---EEAKIKAEELKKAE-- 1629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601984298 464 psEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQ 537
Cdd:PTZ00121 1630 --EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
153-355 |
3.48e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.86 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 153 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 228
Cdd:pfam00261 17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 229 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam00261 91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 601984298 306 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-317 |
3.84e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDv 193
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE- 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 194 gQQLEIKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKS----QAETIALEKEQKLQNDFA 269
Cdd:TIGR02169 896 -AQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 601984298 270 EKERKLQETQMSTTSKLEEAEHKLQTLQ---TALEKTRTELFDLKTKYDEE 317
Cdd:TIGR02169 965 EEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
193-333 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 193 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlksQAETialekEQKLQNDFAEKE 272
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 273 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 333
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
108-446 |
4.02e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 108 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP 185
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 186 DPVPalDVGQQLEIKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 259 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 325
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 326 EMIMTDLERANQRAEVAQREAETlreqlssanHSLQLASQIQKAPDVEQAIEVLTRSsleveLAAKEREIAQLVEDVQRL 405
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKET---------RALSLARALEEALEAKEELERTNKQ-----LRAEMEDLVSSKDDVGKN 679
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 601984298 406 QASLTKLREnsasqisQLEQQLNAKNSTLKQLEEKLKGQAD 446
Cdd:pfam01576 680 VHELERSKR-------ALEQQVEEMKTQLEELEDELQATED 713
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-458 |
4.68e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 108 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLR----------KQVAPLLKSFQGEIDALSKRSKE---AEAAF 174
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELVDCQRELEKLNKERRLlnqEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 175 LTVYKRLIDVPDPVPALDVGQQLEIKVQRLH------------DIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKE 240
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfsERQIKNfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 241 K-IREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQ--ETQMSTTSKLEEAEHK-LQTLQTALEKTRTElfdlkTKY 314
Cdd:TIGR00606 426 EqADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQqlEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 315 DEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSSLEVEL 388
Cdd:TIGR00606 501 KEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQLEDWL 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 389 AAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 458
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
214-442 |
4.73e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.30 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 214 LRETLEEYNKEFAEVknqevtIKALKEKIREYEQTLKSQAETIAL------EKEQKLQNDFAEkERKLQETQMSTTSKLE 287
Cdd:pfam04108 54 LEKVLNELKKDFKQL------LKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLLDFID-EDSVEILRDALKELID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 288 EAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEAETLREQLssANHsLQLASQIQ 367
Cdd:pfam04108 127 ELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EMASLLESL--TNH-YDQCVTAV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 368 KAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQL 437
Cdd:pfam04108 199 KLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALKEF 278
|
....*
gi 601984298 438 EEKLK 442
Cdd:pfam04108 279 EERWE 283
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
114-504 |
4.78e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 114 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDvpdpvpaldv 193
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 194 gqqleikvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKER 273
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 274 KLQETQMSTTSKLEEAEHKLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 341
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 342 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 405
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 406 QASLTKLREnSASQISQLEQQLN-----------------AKNSTLKQLEEKLKGQA-DYEEVKKELNTLK---SMEFAP 464
Cdd:PRK10929 282 DLIASQQRQ-AASQTLQVRQALNtlreqsqwlgvsnalgeALRAQVARLPEMPKPQQlDTEMAQLRVQRLRyedLLNKQP 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 601984298 465 SEGAGTQDSTKPLEVlllEKNRSLQSENATLR-ISNSDLSG 504
Cdd:PRK10929 361 QLRQIRQADGQPLTA---EQNRILDAQLRTQReLLNSLLSG 398
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
237-438 |
4.90e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 237 ALKEKIREYEQ----TLKSQAETIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:pfam09787 4 SAKQELADYKQkaarILQSKEKLIASLKEGSGVEGL--------DSSTALTLELEELRQERDLLREEIQKLRGQIQQLRT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 313 KydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIEVLTR--SSLEVELaa 390
Cdd:pfam09787 76 E---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELERLQEelRYLEEEL-- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984298 391 kEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQLNA------------------KNSTLKQLE 438
Cdd:pfam09787 131 -RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLHQltetliqkqtmlealsteKNSLVLQLE 201
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
196-496 |
5.11e-04 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 43.82 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 196 QLEIKVQRLhDIET-ENQKLRETlEEYNKEfaevknqevtIKALKEKIREYEQTLKSQAETIA---LEKEQKLQNDFAEK 271
Cdd:pfam14915 5 QDEIAMLRL-EIDTiKNQNQEKE-KKYLED----------IEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 272 ERklqetqmsTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLRE 351
Cdd:pfam14915 73 TM--------LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 352 QLSSANHSLQLASQI--QKAPDVEQAIevltrSSLEVEL---AAKEREIAQLVEDVQRlqasltklrensasQISQLEQQ 426
Cdd:pfam14915 134 KMNFDVSNLRDENEIlsQQLSKAESKA-----NSLENELhrtRDALREKTLLLESVQR--------------DLSQAQCQ 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 427 lnaknstLKQLEEKLkgQADYEEVKKELNTLKSMEfapsegagtqdstkplevlllEKNRSLQSENATLR 496
Cdd:pfam14915 195 -------KKELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
826-1026 |
5.58e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 826 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 905
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 906 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 985
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 601984298 986 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 1026
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-461 |
6.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 118 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLTVYKRLID---- 183
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDarka 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 184 -----------VPDPVPALDVGQQLEI-KVQRLHDIET----ENQKLRETLEEYN--KEFAEVKNQEVTIKALK-----E 240
Cdd:PTZ00121 1167 eearkaedakkAEAARKAEEVRKAEELrKAEDARKAEAarkaEEERKAEEARKAEdaKKAEAVKKAEEAKKDAEeakkaE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 241 KIREYEQTLK-----------SQAETIALEKEQKLQNDFAEKERKLQETQMS-TTSKLEEAEHKlqtlqtALEKTRTElf 308
Cdd:PTZ00121 1247 EERNNEEIRKfeearmahfarRQAAIKAEEARKADELKKAEEKKKADEAKKAeEKKKADEAKKK------AEEAKKAD-- 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 309 DLKTKyDEETTAKADEIEmimTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV-- 386
Cdd:PTZ00121 1319 EAKKK-AEEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKkk 1392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 387 --ELAAKEREIAQLVEDVQRLQASLTKLRE--NSASQISQLEQQlnAKNSTLKQLEEKLKGQAdyEEVKKELNTLKSME 461
Cdd:PTZ00121 1393 adEAKKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKKADEA--KKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
188-461 |
6.32e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 188 VPALDVGQQLEIKVQRLHDIET-ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQn 266
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 267 dfAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL--KTKYDEETTAKADEIEMIMTDL-ERANQRAEVAQ 343
Cdd:TIGR00618 513 --PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSErkQRASLKEQMQEIQQSFSILTQCdNRSKEDIPNLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 344 REAETLR---EQLSSANHSLQLASQIQKapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN-SASQ 419
Cdd:TIGR00618 591 NITVRLQdltEKLSEAEDMLACEQHALL----RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVReHALS 666
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 601984298 420 ISQLEQQLNAKNSTLKQLEEKLKGQADY--EEVKKELNTLKSME 461
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYwkEMLAQCQTLLRELE 710
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
119-459 |
6.45e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.25 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 119 RQDESEQSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRLIDVPdPVP 189
Cdd:pfam05667 241 RKRKRTKLLKRIAEQLRSAALAGTEatsGASRSAQDLAELLSsfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAAT-SSP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 190 ALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ-KLQNDF 268
Cdd:pfam05667 320 PTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTlDLLPDA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 269 AEKERKLQetqmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqraevaqreaet 348
Cdd:pfam05667 400 EENIAKLQ-------ALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKE-------------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 349 LREQLssanhslqlasqiqkapdvEQAIEvltrsslevELAAKEREIAQLVEDVQRLQasltklRENSASQISQ--LEQQ 426
Cdd:pfam05667 459 LREKI-------------------KEVAE---------EAKQKEELYKQLVAEYERLP------KDVSRSAYTRriLEIV 504
|
330 340 350
....*....|....*....|....*....|...
gi 601984298 427 LNAKnstlKQLEEKLKGQADYEEVKKELNTLKS 459
Cdd:pfam05667 505 KNIK----KQKEEITKILSDTKSLQKEINSLTG 533
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
362-515 |
6.98e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 362 LASQIQKAPDVEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQL 437
Cdd:PRK11281 19 LLCLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 438 EEKLKgqadyeEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSarrkgRDQPE 515
Cdd:PRK11281 93 PAKLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL-----QTQPE 159
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-443 |
7.27e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 290
Cdd:COG3096 495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 291 HKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSsanhsLQLASqiq 367
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSG-----EALAD--- 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 368 kAPDVEQAIEvltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLNAKNSTLKQLEEKLKG 443
Cdd:COG3096 625 -SQEVTAAMQ---------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
200-458 |
7.39e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 200 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKLQTLQT------ALEKTRTELFDLKTKYDEETTA---------- 320
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 321 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 390
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 391 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTL 457
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQVVQA 1113
|
.
gi 601984298 458 K 458
Cdd:COG3096 1114 K 1114
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
240-492 |
7.88e-04 |
|
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: 44.33 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 240 EKIREYEQTLKSQAEtialEKEQKLQND--FAEKERK-LQETQM---STTSKLEEAEHKLQTLQTALEKTR--TELFDLK 311
Cdd:pfam05483 88 EKIKKWKVSIEAELK----QKENKLQENrkIIEAQRKaIQELQFeneKVSLKLEEEIQENKDLIKENNATRhlCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 312 TKYDEETTAK----ADEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSLQLASQIQKAPDVEQAIEvltrSSLEVE 387
Cdd:pfam05483 164 CARSAEKTKKyeyeREETRQVYMDL---NNNIEKMILAFEELRVQ--AENARLEMHFKLKEDHEKIQHLE----EEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 388 LAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNtlKSMEF 462
Cdd:pfam05483 235 INDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHlTKELEDIKMSLQ--RSMST 311
|
250 260 270
....*....|....*....|....*....|
gi 601984298 463 APSEGAGTQDSTKPLEVLLLEKNRSLQSEN 492
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-276 |
8.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVY-- 178
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINel 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 179 KRLIDvpdpvPALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIA 257
Cdd:TIGR02169 405 KRELD-----RLQEELQRLSEELADLNaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
170 180
....*....|....*....|.
gi 601984298 258 -LEKEQ-KLQNDFAEKERKLQ 276
Cdd:TIGR02169 480 rVEKELsKLQRELAEAEAQAR 500
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
113-503 |
8.51e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 113 ATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ---VAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRL 181
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLlgtIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 182 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREyeqtLKSQAETIALEKE 261
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----------IQHLKSKTNE----LKSEKLQIGTNLQ 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 262 QKLQndFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 331
Cdd:TIGR00606 882 RRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 332 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 397
Cdd:TIGR00606 960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 398 LvedvqrlqasLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT-LKSMEFAPSEgagtqdstk 475
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIKHFKKeLREPQFRDAE--------- 1100
|
410 420
....*....|....*....|....*...
gi 601984298 476 plevlllEKNRSLQSENATLRISNSDLS 503
Cdd:TIGR00606 1101 -------EKYREMMIVMRTTELVNKDLD 1121
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-313 |
8.98e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 148 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldvgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 227
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 228 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 304
Cdd:COG1579 85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155
|
....*....
gi 601984298 305 TELFDLKTK 313
Cdd:COG1579 156 AELEELEAE 164
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
122-441 |
9.55e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 122 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlTVYKRLIDVPDPVPALDVGQQLEI 199
Cdd:PRK04778 133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVEAREILDQLEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 200 KV------------------------------------------------QRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:PRK04778 206 ELaaleqimeeipellkelqtelpdqlqelkagyrelveegyhldhldieKEIQDLKEQIDENLALLEELDLDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 232 EvtikaLKEKIRE-YEQtlksqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK04778 286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 311 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQKAPDvEQAIevlTRSSLEVE 387
Cdd:PRK04778 330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EITERIA-EQEI---AYSELQEE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 388 LAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLnaknSTLKQLEEKL 441
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
212-302 |
9.71e-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: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 280
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 601984298 281 STTSKLEEAEHKLQTLQTALEK 302
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-458 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 384 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 441
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 601984298 442 KG-QADYEEVKKELNTLK 458
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
192-454 |
1.03e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 192 DVGQQLEIKVQRLHDIETENQKLREtleeynkefAEVKNQEVtIKALKEKIREYEQTLKSQA----ETIA-LEKE-QKLQ 265
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQELLE---------SEEKNREE-VEQLKDLYRELRKSLLANRfsfgPALDeLEKQlENLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 266 NDFAEKERKLQETQMSTTSK-LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLERANQRAEVAQ- 343
Cdd:PRK04778 179 EEFSQFVELTESGDYVEAREiLDQLEEELAALEQIMEEIPELLKELQTELPDQL----QELKAGYRELVEEGYHLDHLDi 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 344 -REAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTrSSLEVELAAK---EREIAQLVEDVQRLQASLTKLREns 416
Cdd:PRK04778 255 eKEIQDLKEQIDENLallEELDLDEAEEKNEEIQERIDQLY-DILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKE-- 331
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 601984298 417 asQISQLEQ--QLNAKN-STLKQLEEKLKG-QADYEEVKKEL 454
Cdd:PRK04778 332 --EIDRVKQsyTLNESElESVRQLEKQLESlEKQYDEITERI 371
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
212-355 |
1.04e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.95 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 286
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 601984298 287 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 355
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1357-1391 |
1.22e-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: 1.22e-03
10 20 30
....*....|....*....|....*....|....*
gi 601984298 1357 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1391
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
306-458 |
2.06e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 306 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANhslqlaSQIQkapDVEQAIEVLtrs 382
Cdd:PRK04778 64 EKFEeWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFrkAKHEINEIESLLDLIE------EDIE---QILEELQEL--- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 383 sleVELAAKER-EIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 458
Cdd:PRK04778 132 ---LESEEKNReEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESGDYVEAREILDQLE 204
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
117-362 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 196
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 197 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 265
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 266 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 342
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 601984298 343 QREAETLREQLSSANHSLQL 362
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
116-373 |
2.48e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 116 LANRQDESEQSRKRLIEQSREFKKNTPE-DLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP--------- 185
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTevvqrrahf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 186 ---DPVPALDVGQQLEIKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKEKIREYEQTLKsqaetialEKE 261
Cdd:PRK04863 972 syeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKSSYDAKRQMLQ--------ELK 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 262 QKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkydeettakadEIEMimtdlERAN 336
Cdd:PRK04863 1041 QELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC----------------EAEM-----DNLT 1094
|
250 260 270
....*....|....*....|....*....|....*..
gi 601984298 337 QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 373
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
337-466 |
2.73e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 337 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 402
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 403 QRLQASLTKLRENS------------------ASQISQLEQQLNAKNS----------TLKQLEEKLKG----------- 443
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180
....*....|....*....|...
gi 601984298 444 QADYEEVKKELNTLKSMEFAPSE 466
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSE 962
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
191-457 |
2.78e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 191 LDVGQQLEiKVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIREYEQtlksQAETIALEKEQKLQNDfa 269
Cdd:pfam06160 25 LPVQEELS-KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELLFEAEE----LNDKYRFKKAKKALDE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 270 ekerklqetqmsTTSKLEEAEHKLQTLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevA 342
Cdd:pfam06160 91 ------------IEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 343 QREA-----ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLR 413
Cdd:pfam06160 140 NRFSygpaiDELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELK 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 414 E---------------NSASQISQLEQQLNAKNSTLKQLEekLKG-QADYEEVKKELNTL 457
Cdd:pfam06160 218 EgyremeeegyalehlNVDKEIQQLEEQLEENLALLENLE--LDEaEEALEEIEERIDQL 275
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
226-395 |
2.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKLQTLQTALEKtRT 305
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 306 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 382
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 601984298 383 SLEVELAAKEREI 395
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
382-500 |
3.67e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.59 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 382 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 461
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 601984298 462 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 500
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
191-376 |
4.18e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.49 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 191 LDVGQQLEIK-VQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAEtialekeqKLQNDFA 269
Cdd:pfam17078 33 LEIAQQKESKfLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLE--------NSSASET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 270 EKERKLQETQMS----TTSKLEEAEH---KLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 342
Cdd:pfam17078 105 TLEAELERLQIQydalVDSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNI 184
|
170 180 190
....*....|....*....|....*....|....*
gi 601984298 343 QREAET-LREQLSSANHSLQLASQIQKAPDVEQAI 376
Cdd:pfam17078 185 YVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
320-446 |
4.39e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 320 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 399
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 601984298 400 edvqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 446
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
207-338 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 207 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 282
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601984298 283 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 338
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
219-306 |
4.70e-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: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 219 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 293
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 601984298 294 QTLQTALEKTRTE 306
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-277 |
5.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
|
170
....*....|....*
gi 601984298 263 KLQNDFAEKERKLQE 277
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
196-504 |
5.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 196 QLEIKVQRLHD---------------------IETENQKLRE---------------------TLEEYNKEFAEVK---- 229
Cdd:PRK01156 340 DYIKKKSRYDDlnnqilelegyemdynsylksIESLKKKIEEyskniermsafiseilkiqeiDPDAIKKELNEINvklq 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 230 -------NQEVTIKALKEKIREYEQT---LKSQ------AETIALEKEQKLQNDFAEKERKLQETQMST---TSKLEEAE 290
Cdd:PRK01156 420 disskvsSLNQRIRALRENLDELSRNmemLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIeieVKDIDEKI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 291 HKLQTLQTALEKTRTElfDLKTKYDEETTAKADeIEMIMTDLERAnqraevaqREAETLREQLSSANHSLQLASQIQKAP 370
Cdd:PRK01156 500 VDLKKRKEYLESEEIN--KSINEYNKIESARAD-LEDIKIKINEL--------KDKHDKYEEIKNRYKSLKLEDLDSKRT 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 371 DVEQAIEVltRSSLEVE-LAAKEREIAQLVEDV----QRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQA 445
Cdd:PRK01156 569 SWLNALAV--ISLIDIEtNRSRSNEIKKQLNDLesrlQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN---KI 643
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 446 DYEEVKKELNTLKSmefAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:PRK01156 644 LIEKLRGKIDNYKK---QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-442 |
6.01e-03 |
|
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: 41.31 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 207 IETENQKLRETLEEYNKEFAEVKNQEVTIKA-LKEKIREYEQTLKSQAETIAL--EKEQKLQNDFAEKERkLQETQMSTT 283
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAqMKDLQRELEEARASRDEILAQskESEKKLKNLEAELLQ-LQEDLAASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 284 SKLEEAEHKLQTLQTALE---KTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam01576 854 RARRQAQQERDELADEIAsgaSGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTS 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 361 QlasqiqkapDVEQAIEVLTRSSleVELAAKEREIAQLVEdvQRLQASLTKLRensaSQISQLEQQLN-------AKNST 433
Cdd:pfam01576 934 Q---------KSESARQQLERQN--KELKAKLQEMEGTVK--SKFKSSIAALE----AKIAQLEEQLEqesrerqAANKL 996
|
....*....
gi 601984298 434 LKQLEEKLK 442
Cdd:pfam01576 997 VRRTEKKLK 1005
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-459 |
6.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLI 182
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 183 DVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 263 K----------------------LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTA 320
Cdd:COG1196 584 AraalaaalargaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 321 KADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdvEQAIEVLTRSSLEVELAAKEREIAQLVE 400
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEE-----ALLAEEEEER---ELAEAEEERLEEELEEEALEEQLEAERE 735
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601984298 401 DVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG------QA--DYEEVKKELNTLKS 459
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnlLAieEYEELEERYDFLSE 802
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
202-363 |
6.29e-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: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 202 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 266
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 267 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 334
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 601984298 335 ANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
262-451 |
6.67e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 262 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYDEETTAKAdeiemimtdleranqR 338
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrkLRETQNTLNQLNKQIDELNASIA---------------K 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 339 AEVAQREAET-LREQLSSA----NHS-LQL-----ASQ-----------IQKAPdvEQAIEVLTRSSleVELAAKEREIa 396
Cdd:PRK11637 115 LEQQQAAQERlLAAQLDAAfrqgEHTgLQLilsgeESQrgerilayfgyLNQAR--QETIAELKQTR--EELAAQKAEL- 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 601984298 397 qlvEDVQRLQASLtkLRENSASQiSQLEQQLNAKNSTLKQLEEKL-KGQADYEEVK 451
Cdd:PRK11637 190 ---EEKQSQQKTL--LYEQQAQQ-QKLEQARNERKKTLTGLESSLqKDQQQLSELR 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
319-456 |
6.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 319 TAKADEIEmimtdlERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQL 398
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKL-----------RNEFEKELRERRNELQKL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 601984298 399 VEDVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT 456
Cdd:PRK12704 88 EKRLLQKEENL----DRKLELLEKREEELEKKEKELEQKQQELEKkEEELEELIEEQLQ 142
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
212-390 |
7.32e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 290
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 291 HKLQTLQTALEKTRTELFDLKTKYDE----ETTAKADE----------IEMIMTDLERANQRaeVAQREAEtlreqlssa 356
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKDTlkarAKAAKAQEkvnealsgidSDDATSALERMEEK--IEEMEAR--------- 180
|
170 180 190
....*....|....*....|....*....|....*
gi 601984298 357 nhsLQLASQIQKAPDVEQAIEVL-TRSSLEVELAA 390
Cdd:COG1842 181 ---AEAAAELAAGDSLDDELAELeADSEVEDELAA 212
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
362-453 |
7.73e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 362 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKL 441
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
|
90
....*....|....
gi 601984298 442 K--GQADYEEVKKE 453
Cdd:COG2433 451 SeaRSEERREIRKD 464
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
204-518 |
7.87e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 204 LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEkirEYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTT 283
Cdd:PTZ00440 2338 LDNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKE---EFSKLLKNIKRNNTLCNNNNIKDFISNIGKSVETIKQRFS 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 284 SKLEEAEhklqtlqtalektrtELFDLKTKYDEettakadeIEMIMTDLERANQRAEVAQREAETLREQLSSANHslqla 363
Cdd:PTZ00440 2415 SNLPEKE---------------KLHQIEENLNE--------IKNIMNETKRISNVDAFTNKILQDIDNEKNKENN----- 2466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 364 sqIQKAPDVEQAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKL----------RENSA---------------S 418
Cdd:PTZ00440 2467 --NMNAEKIDDLIENVT--SHNEKIKSELLIINDALRRVKEKKDEMNKLfnsltennnnNNNSAknivdnstyiineleS 2542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 419 QISQLEQQLNAKNSTLKQLEE---KLKGQADYEEVKKELNTLKSMEfapSEGAGTQDSTKPLE---VLLLEKNRSLQSEN 492
Cdd:PTZ00440 2543 HVSKLNELLSYIDNEIKELENeklKLLEKAKIEESRKERERIESET---QEDNTDEEQINRQQqerLQKEEEQKAYSQER 2619
|
330 340
....*....|....*....|....*.
gi 601984298 493 ATLRISNSDLSGSARRKGRDQPESRR 518
Cdd:PTZ00440 2620 LNREVSGTDDTNKNHNTGHDESNYGR 2645
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
200-454 |
8.61e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 200 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQ 279
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 280 MSTTSKLEEAEHKLQTL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 346
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 347 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 426
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260
....*....|....*....|....*...
gi 601984298 427 LNAKNSTLKQLEEKLKGQADYEEVKKEL 454
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
196-313 |
8.79e-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: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 196 QLEIKVQRLHDIETENQKLRE----------TLEEYN--------KEFAEVKNQevtIKALKEKI-REYEQTLKSQAETI 256
Cdd:pfam04849 165 QLDALQEKLRGLEEENLKLRSeashlktetdTYEEKEqqlmsdcvEQLSEANQQ---MAELSEELaRKMEENLRQQEEIT 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 257 AL-----EKEQKLQNDFAEKERKLQ------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTK 313
Cdd:pfam04849 242 SLlaqivDLQHKCKELGIENEELQQhlqaskEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
210-358 |
9.56e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601984298 210 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKSQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 289
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601984298 290 EHKLQTLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 358
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| |
