|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1113-1190 |
4.86e-31 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 116.92 E-value: 4.86e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 1113 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1190
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
930-998 |
3.44e-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: 108.83 E-value: 3.44e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 930 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 998
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
541-617 |
1.51e-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: 1.51e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 541 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 617
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-460 |
6.36e-17 |
|
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: 86.61 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 105 LKRELDATATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ-VAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRL 181
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQ-ISQNNKI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 182 IDvpdpvpalDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE----VTIKALKEKIREYEQTLKSQaETIA 257
Cdd:TIGR04523 337 IS--------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsykQEIKNLESQINDLESKIQNQ-EKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 258 LEKEQKLQNDFAEKERKLQETQ--MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERA 335
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIErlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 336 NQRAEVAQREAETLREQ----------LSSANHSL-----QLASQI----QKAPDVEQAIE----VLTRSSLEVELAAKE 392
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEkkeleekvkdLTKKISSLkekieKLESEKkekeSKISDLEDELNkddfELKKENLEKEIDEKN 567
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 393 REIAQLVEDVQRLQASLTKLRE---NSASQISQLEQQLNAKNSTLKQLEEKL-KGQADYEDVKKELTTLKSM 460
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQElidQKEKEKKDLIKEIEEKEKKISSLEKELeKAKKENEKLSSIIKNIKSK 639
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1236-1292 |
2.52e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 74.46 E-value: 2.52e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 1236 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1292
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-448 |
1.38e-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: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 118 NRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaldlgQQ 196
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKE-LKAELRELELALLVLrLEELREELEELQEELKEAEEELEELTAEL-------------QE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 197 LEIKVQRLhdiETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQK--LQNDFAE 270
Cdd:TIGR02168 265 LEEKLEEL---RLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLdeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 271 KERKLQETQMSTTS---KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQR 344
Cdd:TIGR02168 342 LEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 345 EAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLR------ 413
Cdd:TIGR02168 422 EIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEalEELREELEEAEQALDAAERELAQLQARLDSLErlqenl 501
|
330 340 350
....*....|....*....|....*....|....*
gi 564379019 414 ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYE 448
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-461 |
7.95e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 267
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 338 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensa 417
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLR---- 893
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564379019 418 SQISQLEQQLNAKNSTLKQLEEKLKGQAD-YEDVKKELTTLKSME 461
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREkLAQLELRLEGLEVRI 938
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1236-1293 |
8.63e-14 |
|
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: 67.27 E-value: 8.63e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 1236 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1293
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-449 |
2.78e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 196 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyEQTLKSQAETIALEKEQKLQNDFAEKERKL 275
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 276 ---QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQ 352
Cdd:COG1196 305 arlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 353 LSSANHSLQLASQIQKAPDVEQAIEvLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 432
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|....*..
gi 564379019 433 TLKQLEEKLKGQADYED 449
Cdd:COG1196 461 LLELLAELLEEAALLEA 477
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1236-1291 |
4.96e-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: 64.96 E-value: 4.96e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 1236 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1291
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-496 |
9.88e-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: 70.09 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 208 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 284
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 285 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 361
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 362 LASQIQKAPDVEQAIEVLTrSSLEVELAAKEREIAQLVEDVQ---RLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 438
Cdd:TIGR02168 328 LESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564379019 439 EKLKGQAD-----YEDVKKELTTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 496
Cdd:TIGR02168 407 ARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
167-445 |
1.10e-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: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 167 SKEAEAAFLTVYKRLIDVPDPVPALDLGQQLEIKVQRLHDIETE--NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE 244
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDlrLEKLGENAESSKRLNENANNLIKQFENTKEKIAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 245 YEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTAKAD 323
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 324 -----------EIEMIMTDLERANQraEVAQREAETLREQLS-SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAK 391
Cdd:COG5185 381 sfkdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRqIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564379019 392 EREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 445
Cdd:COG5185 459 EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQL 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-454 |
1.19e-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: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 143 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDLGQQLEIKVQRLHDIETENQKLRETLE 219
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 220 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 297
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 298 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdveqaie 377
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------DLKKE------------ 890
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 378 vltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKEL 454
Cdd:TIGR02169 891 ---RDELEAQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-423 |
1.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKR 180
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 181 LIDvpdpvpaldLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAEti 256
Cdd:COG1196 297 LAR---------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeAEEELEEAEAELAEAEE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 257 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERAN 336
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE------EEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 337 QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENS 416
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
....*..
gi 564379019 417 ASQISQL 423
Cdd:COG1196 519 LRGLAGA 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-460 |
1.84e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 161
Cdd:PRK03918 388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 162 ALSKRSKEAEAAFLTVYKRLIDVpdpvpalDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 241
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 242 IREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDEETTA 320
Cdd:PRK03918 534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 321 KADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVE 400
Cdd:PRK03918 608 KDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSR 673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 401 DVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKgqaDYEDVKKELTTLKSM 460
Cdd:PRK03918 674 ELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-459 |
2.60e-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: 68.94 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 197 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 276
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 277 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssA 356
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL--A 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 357 NHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKN 431
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreKLEKLKREINELK 405
|
250 260
....*....|....*....|....*....
gi 564379019 432 STLKQL-EEKLKGQADYEDVKKELTTLKS 459
Cdd:TIGR02169 406 RELDRLqEELQRLSEELADLNAAIAGIEA 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-460 |
7.67e-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: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDF--- 268
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELkse 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 269 -AEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQREAE 347
Cdd:TIGR04523 316 lKNQEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 348 TLREQLSSanhslqLASQIQKAPDVEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQL 427
Cdd:TIGR04523 388 NLESQIND------LESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELII 456
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564379019 428 NAKNSTLKQLEEKLKG--------QADYEDVKKELTTLKSM 460
Cdd:TIGR04523 457 KNLDNTRESLETQLKVlsrsinkiKQNLEQKQKELKSKEKE 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-407 |
1.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLTVYK 179
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 180 RLidvpdpvpaLDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiALE 259
Cdd:COG1196 324 EL---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 260 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEI-EMIMTDLERANQR 338
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeEEEALLELLAELL 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 339 AEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 407
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-457 |
1.92e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNtPEDLR-KQVAPLLKSFQGE-----IDALSKRSKEAEaaflT 176
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKlKELAEQLKELEEKlkkynLEELEKKAEEYE----K 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 177 VYKRLIDVPDPVpaldlgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlks 251
Cdd:PRK03918 530 LKEKLIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 252 qaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTD 331
Cdd:PRK03918 600 -----FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLE 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 332 LERANQRAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAslt 410
Cdd:PRK03918 671 LSRELAGLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA--- 735
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564379019 411 KLRENSASQISQLEQQL-----NAKNS--TLKQLEEKLKGQADYEDVKKELTTL 457
Cdd:PRK03918 736 LLKERALSKVGEIASEIfeeltEGKYSgvRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
212-438 |
2.58e-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: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 290
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 291 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 370
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 371 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 438
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-419 |
3.08e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 190 ALDLGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 266
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 267 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 341
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 342 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 419
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-459 |
3.84e-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: 65.09 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKREL-DATATVLANRQDESEQSRKRLIEQSrefkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:TIGR02169 215 ALLKEKrEYEGYELLKEKEALERQKEAIERQL--------ASLEEE----LEKLTEEISELEKRLEEIE-------QLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 DVPDPVPALDLGQQLEIKvQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 kLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKtkydeettakaDEIEMIMTDLERAnqraeva 342
Cdd:TIGR02169 355 -LTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKLEKLK-----------REINELKRELDRL------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 343 QREAETLREQLssANHSLQLASQIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENsasqisq 422
Cdd:TIGR02169 412 QEELQRLSEEL--ADLNAAIAGIEAKINELEEEKE-----DKALEIKKQEWKLEQLAADLSKYEQELYDLKEE------- 477
|
330 340 350
....*....|....*....|....*....|....*..
gi 564379019 423 leqqlnaknstlkqleeklkgQADYEDvkkELTTLKS 459
Cdd:TIGR02169 478 ---------------------YDRVEK---ELSKLQR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-368 |
5.73e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 274
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 275 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 350
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 564379019 351 EQLSSANHSLQLASQIQK 368
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
121-442 |
7.67e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.85 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 121 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDLGQQL- 197
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 198 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 277
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 278 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 357
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 358 HSLQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQL 437
Cdd:COG1340 216 KEIVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEI 272
|
....*
gi 564379019 438 EEKLK 442
Cdd:COG1340 273 FEKLK 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-460 |
7.93e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 95 RWMLCvagAKLKRELDA-------TATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRS 167
Cdd:COG4717 44 RAMLL---ERLEKEADElfkpqgrKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 168 KEAEAAFLTVYKRLIDVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQ 247
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 248 TLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEM 327
Cdd:COG4717 178 ELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 328 IMT--------DLERANQRAEVAqrEAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLE------------VE 387
Cdd:COG4717 254 IAAallallglGGSLLSLILTIA--GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeeeleellaalgLP 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 388 LAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEDVKKELTTLKSM 460
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-384 |
2.25e-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: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 180
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 181 lidvpdpvpaldlgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 260
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 261 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 337
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 564379019 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, ... |
251-453 |
5.16e-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: 60.16 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 251 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTkydeettakadEIEMI 328
Cdd:COG4942 17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQ-----------ELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 329 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKERE 394
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 395 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKE 453
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-445 |
8.01e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 206 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERKLQETQMsttsK 285
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELEK----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQ 365
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA------ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 366 IQkapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 445
Cdd:COG4942 166 RA-----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
193-459 |
1.02e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 193 LGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDF 268
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 269 AEKERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 346
Cdd:TIGR04523 489 KELKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 347 ETlrEQLSSANHSLqLASQIQKAPDVEQAIEvlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQ 426
Cdd:TIGR04523 569 EI--EELKQTQKSL-KKKQEEKQELIDQKEK--EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSK 639
|
250 260 270
....*....|....*....|....*....|....
gi 564379019 427 LNAKNSTLKQLEEKLKG-QADYEDVKKELTTLKS 459
Cdd:TIGR04523 640 KNKLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
103-455 |
1.09e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.24 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YK 179
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 180 RLIdvpdpvpaLDLGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 259 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 337
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 338 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA 407
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDV 592
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 564379019 408 -SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL-KGQADYEDVKKELT 455
Cdd:pfam12128 593 pEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvQANGELEKASREET 642
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
216-437 |
1.75e-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: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 216 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 287
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 288 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 361 QlasqiQKAPD----VEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLNAKNSTLK 435
Cdd:pfam13851 137 Q-----QKTGLknllLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIK 198
|
..
gi 564379019 436 QL 437
Cdd:pfam13851 199 DL 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-459 |
3.70e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 227 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 299
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 300 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLSSANHslqlasqiqkapdveQAIEvl 379
Cdd:COG4913 297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQIRGNGG---------------DRLE-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 380 trsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLNAKNSTLKQLEEKL--------KGQ 444
Cdd:COG4913 342 ---QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALaeaeaalrDLR 418
|
250
....*....|....*
gi 564379019 445 ADYEDVKKELTTLKS 459
Cdd:COG4913 419 RELRELEAEIASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
191-460 |
4.11e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.06 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 191 LDLGQQLEIKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA----ETIA--LEKEQ 262
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 338
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 339 AEVAQREAETLREQLSsanhslQLASQI-QKAPDVEQAIEvltrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSA 417
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIgQEIPSDEDILN------LQCETLVQEEE------------QFLSRLEEKSA 842
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564379019 418 SQIsQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKSM 460
Cdd:TIGR00618 843 TLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
274-452 |
6.66e-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: 55.32 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 274 KLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLRE 351
Cdd:COG1579 11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 352 QLSSA--NHSLQ-LASQIQKApdvEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 426
Cdd:COG1579 81 QLGNVrnNKEYEaLQKEIESL---KRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*...
gi 564379019 427 LNAKNSTLKQLEEKLKGQ--ADYEDVKK 452
Cdd:COG1579 158 LEELEAEREELAAKIPPEllALYERIRK 185
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
236-440 |
7.81e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.95 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 236 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 298
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 299 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 362
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 363 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQL 437
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 564379019 438 EEK 440
Cdd:PHA02562 399 VKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-445 |
9.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 110 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLID 183
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 184 VPDpvpaldLGQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIAlEKEQK 263
Cdd:PRK02224 386 IEE------LEEEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 264 LQ-NDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 340
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 341 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 417
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564379019 418 SQISQLEQQ--------------LNAKNSTLKQLEEKLKGQA 445
Cdd:PRK02224 606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
116-461 |
9.70e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 116 LANRQDESEQSRKRLIEQSREF-----KKNTPEDLRKQVAPLlksfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 190
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakaKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 191 LD-LGQQLEIKVQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAET 255
Cdd:PRK03918 417 LKkEIKELKKAIEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEkerkLRKELRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 256 IALEK--------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK03918 496 IKLKElaeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 311 KTKYDEETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLT 380
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 381 RSSLEVELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTL 457
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKY 733
|
....
gi 564379019 458 KSME 461
Cdd:PRK03918 734 KALL 737
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-580 |
1.11e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 361 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 425
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 426 QLNAKNSTLKQLEEKLK-GQADYEDVKKELTTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:COG3883 176 QQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 505 PYSTNSISSPSPLQQSPDVNGMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSV 580
Cdd:COG3883 256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGG 331
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
143-335 |
1.19e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 55.45 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 143 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDVPDpvpaldlgQQLEIKVQRLHDI-ETENQKL-RETLEE 220
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEKDQ--------TALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 221 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 299
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 564379019 300 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 335
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
99-496 |
1.38e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 56.62 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 99 CVAGAKLKRELDATATVLANRQDESEQSRKRlieQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaAFLTVY 178
Cdd:COG5022 830 KKLRETEEVEFSLKAEVLIQKFGRSLKAKKR---FSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKL-VNLELE 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 179 KRLIDV-----PDPVPALDLGQQLEIKVQRLHD-IETENQKLRetleEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQ 252
Cdd:COG5022 906 SEIIELkkslsSDLIENLEFKTELIARLKKLLNnIDLEEGPSI----EYVKLPELNKLHEV-ESKLKETSEEYEDLLKKS 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 253 AETI-----ALEKEQKLQNDFAEKeRKLQETQMSTTSKLEEAEHKLQTLQTALEktrtelfdlktKYDEETTAKAdeIEM 327
Cdd:COG5022 981 TILVregnkANSELKNFKKELAEL-SKQYGALQESTKQLKELPVEVAELQSASK-----------IISSESTELS--ILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 328 IMTDLERANQrAEVAQREAETLREQL---SSANHSLQLaSQIQKAPDVEQAIEVLTRSSLEVELAAKEReiaqlVEDVQR 404
Cdd:COG5022 1047 PLQKLKGLLL-LENNQLQARYKALKLrreNSLLDDKQL-YQLESTENLLKTINVKDLEVTNRNLVKPAN-----VLQFIV 1119
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 405 LQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELttlksmefAPSEGAGTQDSTKPLEVLLLEK 484
Cdd:COG5022 1120 AQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALP--------SPPPFAALSEKRLYQSALYDEK 1191
|
410
....*....|..
gi 564379019 485 NRSLQSENATLR 496
Cdd:COG5022 1192 SKLSSSEVNDLK 1203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-439 |
1.70e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 194 GQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKER 273
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-----RELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 274 KLQ--ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 351
Cdd:PRK03918 274 EIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 352 QLSSANHSLQLasqiqkapdVEQAIEVLTR-SSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA 429
Cdd:PRK03918 353 RLEELEERHEL---------YEEAKAKKEElERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250
....*....|
gi 564379019 430 KNSTLKQLEE 439
Cdd:PRK03918 424 LKKAIEELKK 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-355 |
1.89e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 168 KEAEAAFLTVYKRlIDVPDPVPAL-----DLGQQLEIKVQ-----RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA 237
Cdd:COG4913 238 ERAHEALEDAREQ-IELLEPIRELaeryaAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 238 LKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEE 317
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190
....*....|....*....|....*....|....*...
gi 564379019 318 TTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-444 |
1.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 202 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 281
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 282 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 357
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 358 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA-KNSTLKQ 436
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPE 831
|
....*...
gi 564379019 437 LEEKLKGQ 444
Cdd:COG4913 832 YEERFKEL 839
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-456 |
2.39e-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: 55.75 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 210 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 286
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 287 EEAEhKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 364
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 365 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250
....*....|....
gi 564379019 443 GQADYEDVKKELTT 456
Cdd:pfam02463 413 LARQLEDLLKEEKK 426
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
190-457 |
2.93e-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: 54.19 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 190 ALDLGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 264
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 265 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 344
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 345 eaetLREQLSSANHSLQ----------------------LASQIQKAPDVEQAIEVLTRSSL----------EVELAAKe 392
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinigkQVFTITITTATTKTVDVTSIGGLingignasddEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379019 393 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEDVKKELTTL 457
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-451 |
4.72e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykrli 182
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 dvpdpvpaldlgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4913 688 ------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 341
Cdd:COG4913 750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 342 AQREAETL-------REQLSSANHS--LQLASQIQKAP-DVEQAIEVLTRSSLEVE--------LAAKEREiaqlVEDVQ 403
Cdd:COG4913 822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIrEIKERIDPLNDSLKRIPfgpgrylrLEARPRP----DPEVR 897
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 564379019 404 RLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQADYEDVK 451
Cdd:COG4913 898 EFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEEESDRR 942
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
272-460 |
4.90e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 272 ERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 346
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 347 ETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA--------------AKEREIA----QLVEDVQRLQAS 408
Cdd:COG3206 243 AALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAelsarytpnhpdviALRAQIAalraQLQQEAQRILAS 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564379019 409 LTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEDVKKELTTLKSM 460
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
236-503 |
5.03e-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: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 236 KALKEKIREYEQTLKSQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLqtaleKTRTELFDLKTKY 314
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEEEYLLYL-----DYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 315 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 394
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 395 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKSmefapSEGAGTQDST 474
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260
....*....|....*....|....*....
gi 564379019 475 KPLEVLLLEKNRSLQSENATLRISNSDLS 503
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLED 419
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
141-468 |
5.94e-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: 54.46 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 141 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFltvykrlidvpdpvpaldlgQQLEIKVQRLHDietENQKLRETLEE 220
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTAL--------------------KNARLDLRRLFD---EKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 221 YNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQt 295
Cdd:pfam12128 672 ALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 296 lQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVE 373
Cdd:pfam12128 749 -LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIE 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 374 QAIEvltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGqadYEDVKKE 453
Cdd:pfam12128 821 RAIS--------------------------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG---LRCEMSK 871
|
330
....*....|....*
gi 564379019 454 LTTLKsmEFAPSEGA 468
Cdd:pfam12128 872 LATLK--EDANSEQA 884
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
138-676 |
6.09e-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: 54.46 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 138 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDLGQQ-------LEIKVQRLH----- 205
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 206 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ---------KLQNDFAEKER 273
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMImtDLERANQRAEVA-QREAET---- 348
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGI--KDKLAKIREARDrQLAVAEddlq 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 349 -----LREQLSSANHSL-----QLAS-------QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLT 410
Cdd:pfam12128 419 aleseLREQLEAGKLEFneeeyRLKSrlgelklRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 411 KLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADyedvkkeltTLksMEFAPSEGAGTQDST-KPLEVLLL------- 482
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAG---------TL--LHFLRKEAPDWEQSIgKVISPELLhrtdldp 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 483 EKNRSLQSENATLRISNSDLSGPYSTNSISSPSPLQQSPDVngmAPSPSQSESAgSISEGEEiDTAEIARQVKEQLIKHN 562
Cdd:pfam12128 568 EVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDK---AEEALQSARE-KQAAAEE-QLVQANGELEKASREET 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 563 IGQRIFGHYVLGLSQGSVS-EILARPKpwNKLTVRGKEPFHKMKQFLSDEQNIL------ALRSIQGRQRENPGQSLNRL 635
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEkQSEKDKK--NKALAERKDSANERLNSLEAQLKQLdkkhqaWLEEQKEQKREARTEKQAYW 720
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 564379019 636 fQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKREL 676
Cdd:pfam12128 721 -QVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-449 |
7.81e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 111 ATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 190
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEI-----EDLRETIAETER----EREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 191 LDLGQqlEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlksqaetialEKEQKLQNDFAE 270
Cdd:PRK02224 305 DDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 271 KERKLQETQMSTT---SKLEEAEHKLQTLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:PRK02224 368 LESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 348 TLRE--QLSSANHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQL 423
Cdd:PRK02224 447 ALLEagKCPECGQPVEGSPHVETIEEDRERVEELEaeLEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELI 525
|
330 340
....*....|....*....|....*.
gi 564379019 424 EQQLNAKNSTLKQLEEKLKGQADYED 449
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEA 551
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-497 |
8.49e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRA 339
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 340 EVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN--- 415
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEeLQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLESLQEELAALEQElqa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 416 --SASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENA 493
Cdd:COG4372 176 lsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
....
gi 564379019 494 TLRI 497
Cdd:COG4372 256 ILKE 259
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-442 |
8.72e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQ-----RLHDIETENQKLRETLEEY--NKEFAevknqEVTIKALKEKIREYEQTlksQAETIALEKE-QK 263
Cdd:PRK02224 191 QLKAQIEEKEEkdlheRLNGLESELAELDEEIERYeeQREQA-----RETRDEADEVLEEHEER---REELETLEAEiED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 264 LQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTE----------LFDLKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PRK02224 263 LRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 334 RANQRAEVAQREAETLREQLSSANhslqlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL- 412
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELR---------EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDAp 404
|
250 260 270
....*....|....*....|....*....|..
gi 564379019 413 --RENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:PRK02224 405 vdLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
191-412 |
1.08e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 191 LDLGQQlEIKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQN 266
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 267 DFAEKERKLQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 334
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 335 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 412
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
151-454 |
1.13e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 151 PLLKSFQGEIDALSKRsKEAEAAFLTVYKRLIDvpdpvpALDLGQQLEikvqrlhDIETENQKLRETLEEYNKEFAEVKN 230
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 231 QevtIKALKEKIreyEQTLKSQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFdl 310
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 311 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 390
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 391 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------NAKN-----STLKQLEEKLKGQADYED--VKKE 453
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKRltlseKTVQEAQSQDEAARIQANplVAQE 283
|
.
gi 564379019 454 L 454
Cdd:PRK11281 284 L 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-353 |
1.14e-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: 53.52 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 177
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 178 YKRlidvpdpvpALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTLKSQA 253
Cdd:TIGR02168 816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 254 ETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 331
Cdd:TIGR02168 887 EALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
|
250 260
....*....|....*....|..
gi 564379019 332 LERANQRAEVAQREAETLREQL 353
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
683-948 |
1.48e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 53.17 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 683 EPVQASSTASSGNSDDairsILQQARREMEAQQAALDPALKPAPLSQPdltilnpklLSASPMSTVSTYPPLAISLKKTP 762
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 763 AAPEASTSALPSAPALKKEAQDAPTLDPPGSADAtPGVLRPVKNELVRGSTWKDPWWNPVQPERRNLTTSEETKADETNA 842
Cdd:PRK10263 343 TPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPA-PEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYY 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 843 SGKEKTGSSQPRAERSQLQGPSATA-------EYWKEWPNAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAK 915
Cdd:PRK10263 422 APAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETK 500
|
250 260 270
....*....|....*....|....*....|...
gi 564379019 916 PSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 948
Cdd:PRK10263 501 PARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-442 |
1.69e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 296 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 373
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 374 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-459 |
1.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 DVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KLQNDFAEKERKLQ-----------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:COG4717 266 GSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 332 LERANQ-RAEVAQREAETLREQLSSANHSL----------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVE 400
Cdd:COG4717 346 IEELQElLREAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 401 DVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEklkgQADYEDVKKELTTLKS 459
Cdd:COG4717 426 DEEELEEELEELEEELEEleeELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
208-504 |
1.93e-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: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 208 ETENQKLRETLEEYNKEFA---EVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQM 280
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEklaqVLKENKEEEKEKKLQEEEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 281 STTSKLEEAEHKlqtlQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTD-LERANQRAEV-AQREAETLREQLSSAN 357
Cdd:pfam02463 289 KLLAKEEEELKS----ELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEiEELEKELKELeIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 358 --HSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE--IAQLVEDVQRLQASLTKLRENSAS------QISQLEQQL 427
Cdd:pfam02463 365 qeKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQG 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 428 NAKNSTLKQLEEKLKGQADYEDVKKELTTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-461 |
3.15e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 274
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQL-----QAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 275 LQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 354
Cdd:COG4372 103 LESLQ-EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 355 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 434
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260
....*....|....*....|....*..
gi 564379019 435 KQLEEKLKGQADYEDVKKELTTLKSME 461
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEAL 288
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-495 |
3.20e-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: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 203 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKSQAETIALEKEQK----------LQND 267
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEIIQEQARNQnsmymrqlsdLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 348 TLREQlssanhslqlasqiqkapDVEQAIevlTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSASQISQLEQQL 427
Cdd:pfam15921 402 RLWDR------------------DTGNSI---TIDHLRRELDDRNME-------VQRLEALLKAMKSECQGQMERQMAAI 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 428 NAKNSTLKQ---LEEKLKGQADY-EDVKKELTTlKSMEFAPSEgagtqDSTKPLEVLLLEKNRSLQSENATL 495
Cdd:pfam15921 454 QGKNESLEKvssLTAQLESTKEMlRKVVEELTA-KKMTLESSE-----RTVSDLTASLQEKERAIEATNAEI 519
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
198-511 |
3.20e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 198 EIKVQRLHDIETENQKLRE-TLEEYNKEFAEVK-----------NQEVTIKALKEKIREYEQT---LKSQ------AETI 256
Cdd:PRK01156 383 SKNIERMSAFISEILKIQEiDPDAIKKELNEINvklqdisskvsSLNQRIRALRENLDELSRNmemLNGQsvcpvcGTTL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 257 ALEKEQKLQNDFAEKERKLQETQMST---TSKLEEAEHKLQTLQTALEKTRTElfDLKTKYDEETTAKADeIEMIMTDLE 333
Cdd:PRK01156 463 GEEKSNHIINHYNEKKSRLEEKIREIeieVKDIDEKIVDLKKRKEYLESEEIN--KSINEYNKIESARAD-LEDIKIKIN 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 334 RAnqraevaqREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVltRSSLEVE-LAAKEREIAQLVEDV----QRLQAS 408
Cdd:PRK01156 540 EL--------KDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAV--ISLIDIEtNRSRSNEIKKQLNDLesrlQEIEIG 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 409 LTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEDVKKELTTLKSMEfapSEGAGTQDSTKPLEVLLLEKNRSL 488
Cdd:PRK01156 610 FPDDKSYIDKSIREIENEANNLNNKYNEIQEN---KILIEKLRGKIDNYKKQI---AEIDSIIPDLKEITSRINDIEDNL 683
|
330 340
....*....|....*....|...
gi 564379019 489 QSENATLRISNSDLSGPYSTNSI 511
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIEI 706
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-461 |
4.00e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykrlid 183
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL-------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 184 vpdpvpaldlgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEKeQK 263
Cdd:pfam05483 445 -------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN-KE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 264 LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIMTDL 332
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 333 ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRl 405
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK- 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564379019 406 QASLTKLRENS-----------ASQISQLEQQLNA----KNSTLKQLEEKLKGQAD--YEDVKKELTTLKSME 461
Cdd:pfam05483 662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
211-438 |
4.45e-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: 51.29 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 211 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 289
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 290 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 361
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 362 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLNAKNSTLKQL 437
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 564379019 438 E 438
Cdd:pfam07111 297 E 297
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
196-454 |
4.47e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 196 QLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE 261
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 262 QKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKADEI 325
Cdd:pfam05483 215 FKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKKDHL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 326 EMIMTDLERANQRAEVAQReaeTLREQLSSANHSL-QLASqiQKAPDVEQAIEVLTRSSLEV-ELAAKEREIAQLVE-DV 402
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQK---ALEEDLQIATKTIcQLTE--EKEAQMEELNKAKAAHSFVVtEFEATTCSLEELLRtEQ 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 564379019 403 QRLqasltklrENSASQISQLEQQLNAKNSTLKQLEE-KLKGQADYEDVKKEL 454
Cdd:pfam05483 370 QRL--------EKNEDQLKIITMELQKKSSELEEMTKfKNNKEVELEELKKIL 414
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
154-451 |
5.46e-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: 51.59 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 154 KSFQGEIDAlSKRSKEAEAAFLTVYKRLIDVpdpvpALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV 233
Cdd:TIGR01612 1496 KGCKDEADK-NAKAIEKNKELFEQYKKDVTE-----LLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 234 TIKALK-EKIR---EYEQTLKSQAETIALEKE-QKLQNDFAE------------KERKLQETQMSTTS------KLEEAE 290
Cdd:TIGR01612 1570 KIKEIKkEKFRiedDAAKNDKSNKAAIDIQLSlENFENKFLKisdikkkindclKETESIEKKISSFSidsqdtELKENG 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 291 HKLQTLQTALEKTRTE---LFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQRE-----AETLREQLSSANHSLQl 362
Cdd:TIGR01612 1650 DNLNSLQEFLESLKDQkknIEDKKKELDELDS----EIEKIEIDVDQHKKNYEIGIIEkikeiAIANKEEIESIKELIE- 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 363 asqiqkaPDVEQAIEVLTRSSLE-----VELAAKEREIAQLVEDVQRLQASLTK-LRENSASQISQLE---QQLNAKNST 433
Cdd:TIGR01612 1725 -------PTIENLISSFNTNDLEgidpnEKLEEYNTEIGDIYEEFIELYNIIAGcLETVSKEPITYDEiknTRINAQNEF 1797
|
330
....*....|....*...
gi 564379019 434 LKQLEEKLKGQADYEDVK 451
Cdd:TIGR01612 1798 LKIIEIEKKSKSYLDDIE 1815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-453 |
9.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLI 182
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 DVPDPVPALDLGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI---- 256
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkade 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 257 ---ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE 333
Cdd:PTZ00121 1515 akkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 334 --RANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTK 411
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564379019 412 LRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKE 453
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
127-440 |
1.09e-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: 50.34 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 127 RKRLIEQSREFKKntpeDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaldlgQQLEiK 200
Cdd:COG3096 280 RRELSERALELRR----ELFGARRQLaeeqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL------RQQE-K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 201 VQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKE 272
Cdd:COG3096 349 IERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 273 RKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE---- 340
Cdd:COG3096 427 ALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARellr 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 341 -------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTKL 412
Cdd:COG3096 503 ryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAEA 576
|
330 340
....*....|....*....|....*...
gi 564379019 413 REnsasQISQLEQQLNAKNSTLKQLEEK 440
Cdd:COG3096 577 VE----QRSELRQQLEQLRARIKELAAR 600
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
163-463 |
1.15e-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: 50.21 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 163 LSKRSKEAEAAFLTVYKRLIDVPDPVPALDLGQQLEIK------VQR-LHDIETENQKLRETL----EEYNKEFAEVKNQ 231
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKdtkissLERnIRDLEDEVQMLKTNGllhtEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 232 EVTIKALKEKIREYEQTL-KSQAETIALE-KEQKLQNDFAEKERKLQETQMSTTSKleeaEHKLQTLQTALEKTRTEL-- 307
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEVLKESLTAK----EQRAAILQTEVDALRLRLee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 308 ----FDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVL 379
Cdd:pfam10174 357 kesfLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 380 TRSSLEVELAAKEREIAQLVE-----DVQRLQ--ASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQAdyEDVKK 452
Cdd:pfam10174 437 ALTTLEEALSEKERIIERLKEqrereDRERLEelESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA--SSGLK 514
|
330
....*....|.
gi 564379019 453 ELTTLKSMEFA 463
Cdd:pfam10174 515 KDSKLKSLEIA 525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-452 |
1.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 281 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEeTTAKADEIEMI----MTDLERANQRAEVAQREAEtlREQLSSA 356
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLaeysWDEIDVASAEREIAELEAE--LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 357 NHSL-QLASQIQKapdveqaievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLK 435
Cdd:COG4913 684 SDDLaALEEQLEE---------------LEAELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLAR 744
|
170 180
....*....|....*....|..
gi 564379019 436 Q-----LEEKLKGQADYEDVKK 452
Cdd:COG4913 745 LelralLEERFAAALGDAVERE 766
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-439 |
1.18e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 207 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 286
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 287 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 349
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 350 REQLSsanhslQLASQIQKAPDVEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNA 429
Cdd:COG3206 316 ASLEA------ELEALQAREASLQAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEAL 383
|
250
....*....|
gi 564379019 430 KNSTLKQLEE 439
Cdd:COG3206 384 TVGNVRVIDP 393
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
106-510 |
1.31e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 106 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 174
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 175 ----LTVYKRLIDVPDP--VPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 242
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 243 REYEQTLKSQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKLQTLQTALEKTRTELfdlktkYDEETTAKA 322
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 323 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVED 401
Cdd:pfam05557 271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 402 VQRLQASLTKLR----------------ENSASQISQ-------LEQQLNAKNSTLK----QLEEKLKGQADYED-VKKE 453
Cdd:pfam05557 344 LQRRVLLLTKERdgyrailesydkeltmSNYSPQLLErieeaedMTQKMQAHNEEMEaqlsVAEEELGGYKQQAQtLERE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 454 LTTLKSMEFAPSEGAGTQDST---KPLEVLLLEKNRsLQSENATL--RISNSDLSGPYSTNS 510
Cdd:pfam05557 424 LQALRQQESLADPSYSKEEVDslrRKLETLELERQR-LREQKNELemELERRCLQGDYDPKK 484
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
143-490 |
1.33e-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: 49.69 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 143 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDLGQQLEIKVQRLHDIETENQKLRE 216
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 217 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 277
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 278 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 351
Cdd:pfam05622 160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 352 QLSSANHSL-----------------------------------------------------QLASQIQKAPDVEQAIE- 377
Cdd:pfam05622 236 TLRETNEELrcaqlqqaelsqadallspssdpgdnlaaeimpaeireklirlqhenkmlrlgQEGSYRERLTELQQLLEd 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 378 -VLTRSSLEVEL-AAKER--EIAQLVEDVQR----------------------------LQASLTKLRE----------- 414
Cdd:pfam05622 316 aNRRKNELETQNrLANQRilELQQQVEELQKalqeqgskaedssllkqkleehleklheAQSELQKKKEqieelepkqds 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 415 NSASQISQLEQQLNAKNSTLKQLEEKLKgqadyEDVKKELTTLKSMEfaPSEGAGTQDSTKPLEVLLLEKNRSLQS 490
Cdd:pfam05622 396 NLAQKIDELQEALRKKDEDMKAMEERYK-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-331 |
1.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrli 182
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 dvPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQ 262
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 263 KLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 331
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-461 |
1.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 204 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKlqndfAEKERKLQEtqmstt 283
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 284 skLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 363
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 364 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
250
....*....|....*....
gi 564379019 443 GQADYEDVKKELTTLKSME 461
Cdd:PRK03918 360 RHELYEEAKAKKEELERLK 378
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
203-312 |
1.92e-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: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 276
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 564379019 277 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-495 |
2.25e-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: 49.27 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 215 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 294
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 295 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLASQ 365
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 366 IQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:TIGR00606 392 IKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 443 G--QADYEDVKKELTTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 495
Cdd:TIGR00606 472 RilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
202-344 |
2.44e-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: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 202 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 271
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379019 272 E-RKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTdlERANQRAEVAQR 344
Cdd:COG1579 111 EiLELMERIEELEEELAELEAELAELEAELEEKKAEL-------DEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
105-450 |
2.65e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 105 LKRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSKEAEA 172
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 173 AFLTVYKRLIDVpdpVPALDLGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQT 248
Cdd:PRK04863 391 EVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLSLEQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 249 LkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQTALEKTRTeLFDLKTK 313
Cdd:PRK04863 465 L-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQR-AERLLAE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 314 YDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDVEQAIEVLTRSSLEVEL 388
Cdd:PRK04863 542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAWLAAQDALARLREQSGE 621
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564379019 389 AAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQLEEKLKGQA---DYEDV 450
Cdd:PRK04863 622 EFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGGVLlseIYDDV 694
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-366 |
3.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 145 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDLGQQLEIKVQRLHDIETENQKLR------- 215
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 216 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 289
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 290 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMI---MTDLERANQRAEVAQREAETLREQLSSAN--HSLQLAS 364
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELkaeLRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
..
gi 564379019 365 QI 366
Cdd:COG4717 523 EY 524
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1236-1321 |
4.07e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1236 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1315
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 564379019 1316 RSSRAA 1321
Cdd:COG5576 121 EEADLA 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-459 |
4.07e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 195 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKSQaETIALEKEQKLQND--FAEK 271
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 272 ERKLQETQMSTT----SKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQraeva 342
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEkqkkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEElENELNLLEKEKLNI----- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 343 QREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 419
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564379019 420 ISQLE---QQLNAKNSTLKQLEEKLKgqadyeDVKKELTTLKS 459
Cdd:TIGR04523 266 KKQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
741-924 |
4.88e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 741 SASPMSTVSTYPPLAISLKKTPAAPEAST--SALPSAPALKKEAQDAPTLDPPGSADATPGVLRPVknELVRGSTWKDPW 818
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 819 WNPVQPERRNLTTSEETKADETNASGKEKTGSSQPRAERsqlqgpsataeywKEWPNAESPYSQSSELSLTGASRSETPQ 898
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 564379019 899 NSPLPSSPIVPMAKPAKPSVPPLTPE 924
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-322 |
4.97e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 116 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL 191
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDF 268
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564379019 269 AEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 322
Cdd:COG3206 337 AQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
193-446 |
5.55e-05 |
|
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: 47.98 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 193 LGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAE 270
Cdd:pfam15964 361 LKSELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 271 KERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR------ 344
Cdd:pfam15964 436 AQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarar 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 345 -EAETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQ 397
Cdd:pfam15964 516 eECLKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAK 595
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564379019 398 LVEDVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 446
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
201-439 |
6.15e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 201 VQRLHDIETENQKLRETLEEYNKEFAEVKN--QEVT-------IKALKEKIREYEQTLKSQAETIA----LEKEQKLQND 267
Cdd:PRK04863 232 FQDMEAALRENRMTLEAIRVTQSDRDLFKHliTESTnyvaadyMRHANERRVHLEEALELRRELYTsrrqLAAEQYRLVE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALektrtelfdlktKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 347
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAASDHLNLVQTAL------------RQQEKIERYQADLEELEERLEEQNEVVEEADEQQE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 348 TLREQLSSANHS-LQLASQIQkapDVEQAIEVLTRSSLE----VELAAKEREIAQL----VEDVQRLQASLTKLRENSAS 418
Cdd:PRK04863 380 ENEARAEAAEEEvDELKSQLA---DYQQALDVQQTRAIQyqqaVQALERAKQLCGLpdltADNAEDWLEEFQAKEQEATE 456
|
250 260
....*....|....*....|.
gi 564379019 419 QISQLEQQLNAKNSTLKQLEE 439
Cdd:PRK04863 457 ELLSLEQKLSVAQAAHSQFEQ 477
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-458 |
6.90e-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: 47.73 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 108 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLR----------KQVAPLLKSFQGEIDALSKRSKE---AEAAF 174
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELVDCQRELEKLNKERRLlnqEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 175 LTVYKRLIDVPDPVPALDLGQQLEIKVQRLH------------DIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKE 240
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfsERQIKNfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 241 K-IREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQ--ETQMSTTSKLEEAEHK-LQTLQTALEKTRTElfdlkTKY 314
Cdd:TIGR00606 426 EqADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQqlEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 315 DEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSSLEVEL 388
Cdd:TIGR00606 501 KEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQLEDWL 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 389 AAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLK 458
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-453 |
8.23e-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: 47.48 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 208 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 285
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 286 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 352
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 353 LSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--- 413
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaql 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564379019 414 ----ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADY-EDVKKE 453
Cdd:pfam01576 239 akkeEELQAALARLEEETAQKNNALKKIRELEAQISELqEDLESE 283
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
204-509 |
8.27e-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: 47.74 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 204 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKSqAETIALEKEQKLQNDFAEKERKL 275
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 276 -QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 354
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 355 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQL 427
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVK 1213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 428 NAKNSTLKQLEEKLKGQADyEDVKKELTTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGPYS 507
Cdd:TIGR01612 1214 GINLSYGKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHI 1291
|
..
gi 564379019 508 TN 509
Cdd:TIGR01612 1292 IS 1293
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
113-459 |
1.01e-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: 46.81 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 113 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 192
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 193 LGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 271
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 272 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 345
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 346 AETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ 406
Cdd:pfam07888 253 VEGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564379019 407 ASLTKLRensaSQISQLEQQL-NAKNSTLKQLEEKlkgqadyedvKKELTTLKS 459
Cdd:pfam07888 332 ERLQEER----MEREKLEVELgREKDCNRVQLSES----------RRELQELKA 371
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
121-440 |
1.28e-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: 46.89 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 121 DESEQSRKRLIEQSREFK-KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvPALDLGQQLEI 199
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR------------EALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 200 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERKLQETQ 279
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 280 mSTTSKLEEAEHKLQTLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLS 354
Cdd:TIGR00618 318 -SKMRSRAKLLMKRAAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 355 SANHSLQLASQIQKAPDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQ-------- 422
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLqesaqslk 469
|
330
....*....|....*....
gi 564379019 423 -LEQQLNAKNSTLKQLEEK 440
Cdd:TIGR00618 470 eREQQLQTKEQIHLQETRK 488
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-461 |
1.48e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEA 172
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 173 AFLTVYKrlidvpdpvpaldlgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----KIREYEQT 248
Cdd:TIGR00606 260 NLSKIMK-----------------LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrTVREKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 249 L-KSQAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDEETTAK-- 321
Cdd:TIGR00606 321 LvDCQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnf 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 322 --------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LAAKE 392
Cdd:TIGR00606 396 htlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLEGSS 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379019 393 REIAQLVEDVQRLQASLTKLRENSASQiSQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKSME 461
Cdd:TIGR00606 471 DRILELDQELRKAERELSKAEKNSLTE-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
226-444 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETialekeqklqNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 306 ELFD------LKTKYDEETTAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEV 378
Cdd:pfam12795 73 EILAslsleeLEQRLLQTSAQLQELQN----QLAQLNSQLIELQTRPERAQQQLSEARQRLQqIRNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 379 LTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 444
Cdd:pfam12795 149 AQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
259-502 |
1.72e-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: 46.27 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 259 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 339 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVElAAKER--EIAQLVED 401
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVK-NSKSElaRIPELEKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 402 VQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQlEEKLKGQADYEDVKKE--LTTLKSMEfapsEGAGTQDSTKPLEV 479
Cdd:pfam05557 206 LERLREHNKHLNENIEN-KLLLKEEVEDLKRKLER-EEKYREEAATLELEKEklEQELQSWV----KLAQDTGLNLRSPE 279
|
250 260
....*....|....*....|...
gi 564379019 480 LLLEKNRSLQSENATLRISNSDL 502
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSL 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-317 |
1.80e-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: 46.21 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpaLDL 193
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKER--DEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 194 GQQLEIKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKS----QAETIALEKEQKLQNDFA 269
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564379019 270 EKERKLQETQMSTTSKLEEAEHKLQTLQ---TALEKTRTELFDLKTKYDEE 317
Cdd:TIGR02169 965 EEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
200-458 |
1.94e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 200 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKLQTLQT------ALEKTRTELFDLKTKYDEETTA---------- 320
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 321 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 390
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 391 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKL-KGQADYEDVKKELTTL 457
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQVVQA 1113
|
.
gi 564379019 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 |
2.41e-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: 45.87 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 240 EKIREYEQTLKSQAEtialEKEQKLQND--FAEKERK-LQETQM---STTSKLEEAEHKLQTLQTALEKTR--TELFDLK 311
Cdd:pfam05483 88 EKIKKWKVSIEAELK----QKENKLQENrkIIEAQRKaIQELQFeneKVSLKLEEEIQENKDLIKENNATRhlCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 312 TKYDEETTAK----ADEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSLQLASQIQKAPDVEQAIEvltrSSLEVE 387
Cdd:pfam05483 164 CARSAEKTKKyeyeREETRQVYMDL---NNNIEKMILAFEELRVQ--AENARLEMHFKLKEDHEKIQHLE----EEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 388 LAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEDVKKELTtlKSMEF 462
Cdd:pfam05483 235 INDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHlTKELEDIKMSLQ--RSMST 311
|
250 260 270
....*....|....*....|....*....|
gi 564379019 463 APSEGAGTQDSTKPLEVLLLEKNRSLQSEN 492
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
202-307 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 202 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 265
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564379019 266 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 307
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
237-438 |
2.53e-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: 44.75 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 237 ALKEKIREYEQT----LKSQAETIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 312
Cdd:pfam09787 4 SAKQELADYKQKaariLQSKEKLIASLKEGSGVEGL--------DSSTALTLELEELRQERDLLREEIQKLRGQIQQLRT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 313 KydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIEVLTR--SSLEVELaa 390
Cdd:pfam09787 76 E---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELERLQEelRYLEEEL-- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 391 kEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQLNA------------------KNSTLKQLE 438
Cdd:pfam09787 131 -RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLHQltetliqkqtmlealsteKNSLVLQLE 201
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-450 |
2.54e-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: 45.71 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 290
Cdd:COG3096 495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 291 HKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSsanhsLQLASqiq 367
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSG-----EALAD--- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 368 kAPDVEQAIEvltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLNAKNSTLKQLEEKLKGQ--A 445
Cdd:COG3096 625 -SQEVTAAMQ---------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGGVllS 687
|
....*.
gi 564379019 446 D-YEDV 450
Cdd:COG3096 688 EiYDDV 693
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
214-442 |
2.72e-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: 45.07 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 214 LRETLEEYNKEFAEVknqevtIKALKEKIREYEQTLKSQAETIAL------EKEQKLQNDFAEkERKLQETQMSTTSKLE 287
Cdd:pfam04108 54 LEKVLNELKKDFKQL------LKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLLDFID-EDSVEILRDALKELID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 288 EAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEAETLREQLssANHsLQLASQIQ 367
Cdd:pfam04108 127 ELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EMASLLESL--TNH-YDQCVTAV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 368 KAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQL 437
Cdd:pfam04108 199 KLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALKEF 278
|
....*
gi 564379019 438 EEKLK 442
Cdd:pfam04108 279 EERWE 283
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
306-458 |
2.78e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.23 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 306 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 382
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 383 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEDVKKELTTLK 458
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
249-445 |
2.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 249 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 327
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 328 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQA 407
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-------------EEELE-----KKEKELEQKQQELEKKEEELEELIE 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 564379019 408 SLTKLRENsasqISQLEQQlNAKNSTLKQLEEKLKGQA 445
Cdd:PRK12704 139 EQLQELER----ISGLTAE-EAKEILLEKVEEEARHEA 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
113-508 |
3.34e-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: 45.42 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 113 ATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ---VAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRL 181
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLlgtIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 182 IDVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREyeqtLKSQAETIALEKE 261
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----------IQHLKSKTNE----LKSEKLQIGTNLQ 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 262 QKLQndFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 331
Cdd:TIGR00606 882 RRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 332 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 397
Cdd:TIGR00606 960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 398 LvedvqrlqasLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEDVKKELTT-LKSMEFAPSEgagtqdstk 475
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIKHFKKeLREPQFRDAE--------- 1100
|
410 420 430
....*....|....*....|....*....|...
gi 564379019 476 plevlllEKNRSLQSENATLRISNSDLSGPYST 508
Cdd:TIGR00606 1101 -------EKYREMMIVMRTTELVNKDLDIYYKT 1126
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
114-429 |
3.63e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 114 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDvpdPVPAL-- 191
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---NFPKLsa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQRLHDIEtENQklreTLEEYNKEFAEVKNQevtikaLKEKIREYEQtlksqaetialekEQKLQNDFAEK 271
Cdd:PRK10929 83 ELRQQLNNERDEPRSVP-PNM----STDALEQEILQVSSQ------LLEKSRQAQQ-------------EQDRAREISDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 272 ERKLQETQMSTTSKLEEAEHKLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRA 339
Cdd:PRK10929 139 LSQLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 340 EVAQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQ 403
Cdd:PRK10929 211 ELAKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQ 279
|
330 340
....*....|....*....|....*.
gi 564379019 404 RLQASLTKLREnSASQISQLEQQLNA 429
Cdd:PRK10929 280 RMDLIASQQRQ-AASQTLQVRQALNT 304
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
203-549 |
3.63e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.42 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 203 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 282
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 283 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVAQREAETLREQLS 354
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKKKKKSSADKSKKA 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 355 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 434
Cdd:PTZ00108 1193 SVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPK 1272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 435 KQLEEKLKGQADYEDVKKELTTLKSmeFAPSEGAGTQDST-KPLEVLLLEKNRSLQSENATLRISNSDlsgpysTNSISS 513
Cdd:PTZ00108 1273 NAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVkKRLEGSLAALKKKKKSEKKTARKKKSK------TRVKQA 1344
|
330 340 350
....*....|....*....|....*....|....*.
gi 564379019 514 PSPLQQSPdvngmAPSPSQSESAGSISEGEEIDTAE 549
Cdd:PTZ00108 1345 SASQSSRL-----LRRPRKKKSDSSSEDDDDSEVDD 1375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
188-461 |
4.12e-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: 44.96 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 188 VPALDLGQQLEIKVQRLHDIET-ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQn 266
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 267 dfAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL--KTKYDEETTAKADEIEMIMTDL-ERANQRAEVAQ 343
Cdd:TIGR00618 513 --PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSErkQRASLKEQMQEIQQSFSILTQCdNRSKEDIPNLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 344 REAETLR---EQLSSANHSLQLASQIQKapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN-SASQ 419
Cdd:TIGR00618 591 NITVRLQdltEKLSEAEDMLACEQHALL----RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVReHALS 666
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564379019 420 ISQLEQQLNAKNSTLKQLEEKLKGQADY--EDVKKELTTLKSME 461
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYwkEMLAQCQTLLRELE 710
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
153-355 |
4.14e-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: 43.48 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 153 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDLGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 228
Cdd:pfam00261 17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 229 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 305
Cdd:pfam00261 91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564379019 306 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 355
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1307-1504 |
4.65e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1307 AGASDSPSARSSRAAPSSEGDSCDGVEAADTEEPGGNivaTKSQGGPAEVTAAPADREEATQPAEKAKAQPLSSGTPgqd 1386
Cdd:PHA03307 217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPEN---ECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1387 DGEDAGRSRPPPEGLADAPAPVPNLAAPAAGEDAATSATAPAMATEAPGAARAGPAERSSALPSTSAPANAPARRPSSLQ 1466
Cdd:PHA03307 291 PRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR 370
|
170 180 190
....*....|....*....|....*....|....*...
gi 564379019 1467 SLFGLPEAAGARDNPVRKKKAANLNSIIHRLEKAASRE 1504
Cdd:PHA03307 371 PSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
196-496 |
5.98e-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: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 196 QLEIKVQRLhDIET-ENQKLRETlEEYNKEfaevknqevtIKALKEKIREYEQTLKSQAETIA---LEKEQKLQNDFAEK 271
Cdd:pfam14915 5 QDEIAMLRL-EIDTiKNQNQEKE-KKYLED----------IEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 272 ERklqetqmsTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLRE 351
Cdd:pfam14915 73 TM--------LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 352 QLSSANHSLQLASQI--QKAPDVEQAIevltrSSLEVEL---AAKEREIAQLVEDVQRlqasltklrensasQISQLEQQ 426
Cdd:pfam14915 134 KMNFDVSNLRDENEIlsQQLSKAESKA-----NSLENELhrtRDALREKTLLLESVQR--------------DLSQAQCQ 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 427 lnaknstLKQLEEKLkgQADYEDVKKELTTLKSMEfapsegagtqdstkplevlllEKNRSLQSENATLR 496
Cdd:pfam14915 195 -------KKELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
212-302 |
6.30e-04 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 41.10 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 280
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 564379019 281 STTSKLEEAEHKLQTLQTALEK 302
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
212-461 |
6.35e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMSTTSKLEEAEH 291
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKLRSRVDL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 292 KLQTLQtALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQ------------RAEVAQREAETLREQLSSA 356
Cdd:pfam15921 529 KLQELQ-HLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 357 NHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER---------EIAQLVEDVQRLQASLTKLRENsasqISQLEQQL 427
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlravkdikqERDQLLNEVKTSRNELNSLSED----YEVLKRNF 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 564379019 428 NAKNSTLKQLEEKLKGQADYEDVKKELT--TLKSME 461
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTrnTLKSME 719
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-454 |
6.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE--QKLQNDFAEKE 272
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEAQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 273 RKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAET 348
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllkeANRNAEKEEELAEAEKLIESLPRELAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 349 LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 428
Cdd:COG4372 219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLL 298
|
250 260
....*....|....*....|....*.
gi 564379019 429 AKNSTLKQLEEKLKGQADYEDVKKEL 454
Cdd:COG4372 299 ALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1301-1488 |
7.56e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.07 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1301 AGSQGQAGASDSPsARSSRAAPSSEGDSCDGVEAADTEEPGGNIVATKSQGGPAEVTAAPADREEA----TQPAEKAKA- 1375
Cdd:PRK07003 361 AVTGGGAPGGGVP-ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAppaaPAPPATADRg 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1376 -QPLSSGTPGQDDGEDAGRSRPPPEGLADAPAPVPNLAAPAAGEDAATSATAPamATEAPGAARAGPAERSSALPSTSAP 1454
Cdd:PRK07003 440 dDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPAAAS 517
|
170 180 190
....*....|....*....|....*....|....
gi 564379019 1455 ANAPARRPSSLQSLFGLPEAAGARDnPVRKKKAA 1488
Cdd:PRK07003 518 REDAPAAAAPPAPEARPPTPAAAAP-AARAGGAA 550
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
108-446 |
7.80e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 108 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP 185
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 186 DPVPalDLGQQLEIKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 259 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 325
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 326 EMIMTDLERANQRAEVAQREAETlreqlssanHSLQLASQIQKAPDVEQAIEVLTRSsleveLAAKEREIAQLVEDVQRL 405
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKET---------RALSLARALEEALEAKEELERTNKQ-----LRAEMEDLVSSKDDVGKN 679
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564379019 406 QASLTKLREnsasqisQLEQQLNAKNSTLKQLEEKLKGQAD 446
Cdd:pfam01576 680 VHELERSKR-------ALEQQVEEMKTQLEELEDELQATED 713
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
212-355 |
7.93e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.33 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 286
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564379019 287 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 355
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-313 |
8.14e-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: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 148 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldlgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 227
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 228 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 304
Cdd:COG1579 85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155
|
....*....
gi 564379019 305 TELFDLKTK 313
Cdd:COG1579 156 AELEELEAE 164
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
193-333 |
8.91e-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: 41.61 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 193 LGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlksQAETialekEQKLQNDFAEKE 272
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 273 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 333
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-277 |
1.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 103 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaafltvyKRLI 182
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 DVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQ 262
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
|
170
....*....|....*
gi 564379019 263 KLQNDFAEKERKLQE 277
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1255-1289 |
1.15e-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: 1.15e-03
10 20 30
....*....|....*....|....*....|....*
gi 564379019 1255 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1289
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1340-1474 |
1.28e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1340 PGGNIVATKSQGGPAEVTAAPADREEATQPAEKAKAQPLSSGTPGQDDGEdaGRSRPPPEGLADAPAPvPNLAAPAAGED 1419
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAP--ARRSPAPEALAAARQA-SARGPGGAPAP 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564379019 1420 AATSATAPAMATEAPGAARAGPAERSSALPSTSAPANAPARRPSSLQSLFGLPEA 1474
Cdd:PRK12323 451 APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPE 505
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
117-362 |
1.30e-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: 43.21 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 117 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldLGQQ 196
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 197 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 265
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 266 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 342
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 564379019 343 QREAETLREQLSSANHSLQL 362
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-458 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 384 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 441
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 564379019 442 KG-QADYEDVKKELTTLK 458
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
116-373 |
1.92e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 116 LANRQDESEQSRKRLIEQSREFKKNTPE-DLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKR---LIDV------- 184
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVvqrrahf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 185 --PDPVPALDLGQQLEIKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKEKIREYEQTLKsqaetialEKE 261
Cdd:PRK04863 972 syEDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKSSYDAKRQMLQ--------ELK 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 262 QKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkydeettakadEIEMimtdlERAN 336
Cdd:PRK04863 1041 QELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC----------------EAEM-----DNLT 1094
|
250 260 270
....*....|....*....|....*....|....*..
gi 564379019 337 QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 373
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-363 |
2.15e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEikvQRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIAL 258
Cdd:COG3096 984 DLNEKLR---ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERAR 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 259 EKEQKLQN---------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEI 325
Cdd:COG3096 1059 IRRDELHEelsqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVL 1121
|
170 180 190
....*....|....*....|....*....|....*....
gi 564379019 326 EMIM-TDLERANQRAEVAQREAETLREQLSSANHSLQLA 363
Cdd:COG3096 1122 RLARdNDVERRLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-459 |
2.38e-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: 42.47 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 195 QQLEIKVQRLHDIETENQKLRETLEEYNKEF-AEVKNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKER 273
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLSKERKLLEERISEFtSNLAEEEEKAKSLSKLKNKHEAMISDLEER--LKKEEKGRQELEKAKR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 274 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD------EIEMIMTDLERANQRAEVAQREAE 347
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNalkkirELEAQISELQEDLESERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 348 TLREQLSSANHSLQlaSQIQKAPDVEQAIEVLtRSSLEVELAAKEREIAqlvEDVQRLQASLTKLRENSASQISQLEQQL 427
Cdd:pfam01576 292 KQRRDLGEELEALK--TELEDTLDTTAAQQEL-RSKREQEVTELKKALE---EETRSHEAQLQEMRQKHTQALEELTEQL 365
|
250 260 270
....*....|....*....|....*....|...
gi 564379019 428 -NAKNSTLKQLEEKLKGQADYEDVKKELTTLKS 459
Cdd:pfam01576 366 eQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
337-466 |
2.41e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 337 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 402
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 403 QRLQASLTKLRENS------------------ASQISQLEQQLNAKNS----------TLKQLEEKLKG----------- 443
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180
....*....|....*....|...
gi 564379019 444 QADYEDVKKELTTLKSMEFAPSE 466
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSE 962
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1306-1481 |
2.59e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1306 QAGASDSPSARSSRAAPSSEGDSCDGVEAADTEEPGGNiVATKSQGGPAEVTAAPADREEATQPAEKAKAQPLSSGTPGQ 1385
Cdd:PRK07764 587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP-AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1386 DDGEDAGRSRPPPEGLADAPAPVPnlaapaaGEDAATSATAPAMATEAPGAARAGPAERSSALPSTSAPANAPARRPSSL 1465
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAA-------PAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
|
170
....*....|....*.
gi 564379019 1466 QSLFGLPEAAGARDNP 1481
Cdd:PRK07764 739 VPLPPEPDDPPDPAGA 754
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
226-395 |
2.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 226 AEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKLQTLQTALEKtRT 305
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 306 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 382
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 564379019 383 SLEVELAAKEREI 395
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
708-919 |
2.98e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 708 RREMEAQQAALDPALKPAP----LSQPDLTILNPKLLSASPMSTVSTYPPLAISLKKTPAAPEASTSALPSAPALKKEAQ 783
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 784 DAPTLDPPGSADATPGVLRPVKNELVRGSTWKDPWWNPVQPERRNLTTSEETKADETNASGKEKTGSSQPRAERSQlQGP 863
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETD-PPP 3021
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 864 SATAEYWkeWPNAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVP 919
Cdd:PHA03247 3022 VSLKQTL--WPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATP 3075
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
207-338 |
3.17e-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: 40.28 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 207 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 282
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 283 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 338
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
320-446 |
3.32e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 320 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 399
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 564379019 400 edvqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 446
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
193-376 |
3.56e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 193 LGQQLEIKVQRLHDIETENQKLRETLEEynkefAEVKNQEVTIKAlkEKIREYEQTLKSQAETIalekeqKLQNDfaeke 272
Cdd:pfam17078 57 LSSMLNRKERRLKDLEDQLSELKNSYEE-----LTESNKQLKKRL--ENSSASETTLEAELERL------QIQYD----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 273 rKLQETQMSTTSKLEEaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET-LRE 351
Cdd:pfam17078 119 -ALVDSQNEYKDHYQQ---EINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNkLLT 194
|
170 180
....*....|....*....|....*
gi 564379019 352 QLSSANHSLQLASQIQKAPDVEQAI 376
Cdd:pfam17078 195 KLDSLAQLLDLPSWLNLYPESRNKI 219
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
122-441 |
3.88e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 122 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlTVYKRLIDVPDPVPALDLGQQLEI 199
Cdd:PRK04778 133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVEAREILDQLEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 200 KV------------------------------------------------QRLHDIETENQKLRETLEEYNKEFAEVKNQ 231
Cdd:PRK04778 206 ELaaleqimeeipellkelqtelpdqlqelkagyrelveegyhldhldieKEIQDLKEQIDENLALLEELDLDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 232 EvtikaLKEKIRE-YEQtlksqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKLQTLQTALEKTRTELFDL 310
Cdd:PRK04778 286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 311 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQKAPDvEQAIevlTRSSLEVE 387
Cdd:PRK04778 330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EITERIA-EQEI---AYSELQEE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 388 LAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLnaknSTLKQLEEKL 441
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
200-453 |
4.13e-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: 41.76 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 200 KVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIREYEQtlksQAETIALEKEQKLQNDfaekerklqet 278
Cdd:pfam06160 33 KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELLFEAEE----LNDKYRFKKAKKALDE----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 279 qmsTTSKLEEAEHKLQTLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevAQREA----- 346
Cdd:pfam06160 91 ---IEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------ANRFSygpai 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 347 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLRE-------- 414
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELKEgyremeee 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564379019 415 -------NSASQISQLEQQLNAKNSTLKQLE--------EKLKGQAD--YEDVKKE 453
Cdd:pfam06160 227 gyalehlNVDKEIQQLEEQLEENLALLENLEldeaeealEEIEERIDqlYDLLEKE 282
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
219-306 |
4.47e-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: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 219 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 293
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 564379019 294 QTLQTALEKTRTE 306
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
192-441 |
4.62e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 192 DLGQQLEIKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQTLKSQaetiaLEKEQKLQNDFAE 270
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQKYEDE-----LNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 271 KERKLQETQMSTTskleEAEHKLQTLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 349
Cdd:pfam00038 108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 350 REQLSS-ANHSLQLASQIQKApDVEQAIEVLTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 425
Cdd:pfam00038 176 RAQYEEiAAKNREEAEEWYQS-KLEELQQAAARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
|
250 260
....*....|....*....|
gi 564379019 426 ----QLNAKNSTLKQLEEKL 441
Cdd:pfam00038 253 ryelQLADYQELISELEAEL 272
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-442 |
4.68e-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: 41.70 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 207 IETENQKLRETLEEYNKEFAEVKNQEVTIKA-LKEKIREYEQTLKSQAETIAL--EKEQKLQNDFAEKERkLQETQMSTT 283
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAqMKDLQRELEEARASRDEILAQskESEKKLKNLEAELLQ-LQEDLAASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 284 SKLEEAEHKLQTLQTALE---KTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 360
Cdd:pfam01576 854 RARRQAQQERDELADEIAsgaSGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTS 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 361 QlasqiqkapDVEQAIEVLTRSSleVELAAKEREIAQLVEdvQRLQASLTKLRensaSQISQLEQQLN-------AKNST 433
Cdd:pfam01576 934 Q---------KSESARQQLERQN--KELKAKLQEMEGTVK--SKFKSSIAALE----AKIAQLEEQLEqesrerqAANKL 996
|
....*....
gi 564379019 434 LKQLEEKLK 442
Cdd:pfam01576 997 VRRTEKKLK 1005
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
100-451 |
5.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 100 VAGAKLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRKQvapllksfQGEIDALSKRSKEAEAAFLTvyk 179
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREEL-EQAREELEQLEEELEQA--------RSELEQLEEELEELNEQLQA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 180 rlidvpdpvpaldLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAETIale 259
Cdd:COG4372 92 -------------AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 260 keQKLQNDFAEKERKLQETQMST-TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQR 338
Cdd:COG4372 153 --KELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 339 AEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS 418
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE--KDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350
....*....|....*....|....*....|...
gi 564379019 419 QISQLEQQLNAKNSTLKQLEEKLKGQADYEDVK 451
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-461 |
5.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 118 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLTVYKRLIDVPDP 187
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 188 VPALDLGQQLEIKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKSQAETIALE 259
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 260 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfDLK----TKYDEETTAKADEIEmimtDLERA 335
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKkaeeKKKADEAKKKAEEAK----KADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 336 NQRAEVAQREAETLREQlssanhslqlASQIQKAPDVEQAIEvlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 415
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKK----------AEEAKKAAEAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564379019 416 SASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKSME 461
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
212-409 |
5.53e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 290
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 291 HKLQTLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 364
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564379019 365 -----QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 409
Cdd:COG1842 169 rmeekIEEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-491 |
5.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 104 KLKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLTVYKRLI 182
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 183 DVPDPVPALDLGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 262
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 263 KlqndfAEKERKLQETQmsttSKLEEAEHKLQTLQTALE-KTRTElfdlKTKYDEETTAKADEiemimtdleraNQRAEV 341
Cdd:PTZ00121 1406 K-----ADELKKAAAAK----KKADEAKKKAEEKKKADEaKKKAE----EAKKADEAKKKAEE-----------AKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 342 AQREAETLREqlssANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER---EIAQLVEDVQRLQASLTKLRENSAS 418
Cdd:PTZ00121 1462 AKKKAEEAKK----ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKAD 1537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 419 QISQLEQQLNA----KNSTLKQLEEKLKG-QADYEDVKKELTTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSE 491
Cdd:PTZ00121 1538 EAKKAEEKKKAdelkKAEELKKAEEKKKAeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
362-504 |
6.30e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 362 LASQIQKAPDVEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQL 437
Cdd:PRK11281 19 LLCLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379019 438 EEKLKgqadyeDVKKELTTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 504
Cdd:PRK11281 93 PAKLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1267-1406 |
6.37e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 1267 ELATQLNLKTStvinwfhnyrSRIRR-ELF--IEEIQAGSQGQAGASDSPSARSSRAAPSSEGDSCDGVEAADTEEPGGN 1343
Cdd:PRK12678 33 ALAKQLGIKGT----------SGMRKgELIaaIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564379019 1344 IVATKSQGGPAEVTAAPADREEATQPAEKAKAQPLSSGTPGQDDGEDAGRSRPPPEGLADAPA 1406
Cdd:PRK12678 103 EAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTE 165
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
196-313 |
7.12e-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: 40.39 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 196 QLEIKVQRLHDIETENQKLRE----------TLEEYN--------KEFAEVKNQevtIKALKEKI-REYEQTLKSQAETI 256
Cdd:pfam04849 165 QLDALQEKLRGLEEENLKLRSeashlktetdTYEEKEqqlmsdcvEQLSEANQQ---MAELSEELaRKMEENLRQQEEIT 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 257 AL-----EKEQKLQNDFAEKERKLQ------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTK 313
Cdd:pfam04849 242 SLlaqivDLQHKCKELGIENEELQQhlqaskEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
199-459 |
7.79e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 199 IKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAL--------EKEQKLQNDFAE 270
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDHLNLvqtalrqqEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 271 KERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKY-------DEETT------------AKADEI-EMIMT 330
Cdd:COG3096 359 LTERLEEQEEV----VEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqalDVQQTraiqyqqavqalEKARALcGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 331 DLERANQRAEVAQREAETLREQLSSANHSLQLASQiqKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLT 410
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA--ARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564379019 411 KLrENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEDVKKELTTLKS 459
Cdd:COG3096 513 RL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA 560
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
212-326 |
8.35e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 212 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ------KLQNDFAEKERKL---QETQMST 282
Cdd:pfam11559 20 GLLFDTAEGVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERlqskieRLKTQLEDLERELallQAKERQL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564379019 283 TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIE 326
Cdd:pfam11559 100 EKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIE 143
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
191-428 |
8.57e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 191 LDLGQQLE---IKVQRLHDIETENQ----KLRETLEEYNKEFAEvKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQK 263
Cdd:pfam02841 71 LDLHRDCEkeaIAVFMKRSFKDENQefqkELVELLEAKKDDFLK-QNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 264 LQnDFAEKERKLQETQMSTTSKLEEAEHKLQTL---QTALEKTrtelfdlKTKYDEETTAKADEIEMimtdlERAnqRAE 340
Cdd:pfam02841 150 YK-LFLEERDKLEAKYNQVPRKGVKAEEVLQEFlqsKEAVEEA-------ILQTDQALTAKEKAIEA-----ERA--KAE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 341 VAQREAETLREQLSSanHSLQLASQIQKAPD-VEQAIEvltrsSLEVELAAKEREIAQLVEdvQRLQASLTKLRENSASQ 419
Cdd:pfam02841 215 AAEAEQELLREKQKE--EEQMMEAQERSYQEhVKQLIE-----KMEAEREQLLAEQERMLE--HKLQEQEELLKEGFKTE 285
|
....*....
gi 564379019 420 ISQLEQQLN 428
Cdd:pfam02841 286 AESLQKEIQ 294
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
216-442 |
8.86e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 216 ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN------DFAEKERKLQETQMSTTSKLEEA 289
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVlekelkHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 290 EHKLQtLQTALEKTRTELfdlktkydEETTAKADEIEMIMTDLERANQRAEVA--QREAETLREQLSSANHSLQlaSQIQ 367
Cdd:TIGR00618 253 EEQLK-KQQLLKQLRARI--------EELRAQEAVLEETQERINRARKAAPLAahIKAVTQIEQQAQRIHTELQ--SKMR 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379019 368 KAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 442
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
679-920 |
9.06e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 679 QKTAEPVQASSTASSGNSDDAIRSILQQARREM--EAQQAALDPALKPAPLSQPDLTILNPKLLSASPMSTVSTYPPlai 756
Cdd:PHA03307 112 SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPgpPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 757 slKKTPAAPEASTSALPSAPALKKEAQDAPTLDPPGSADATPGVLRPVKNELVRGSTWKDPWW-----NPVQPERRNLTT 831
Cdd:PHA03307 189 --PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWgpeneCPLPRPAPITLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 832 SEETKADETNASGKEKT--GSSQPRAERSQLQGPSATAEYWKEWPNAESPYSQSSELSLTGASRSETPQNSPLPSSPIVP 909
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGpaSSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346
|
250
....*....|.
gi 564379019 910 MAKPAKPSVPP 920
Cdd:PHA03307 347 PSRSPSPSRPP 357
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
210-358 |
9.16e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 210 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKSQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 289
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379019 290 EHKLQTLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 358
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
262-458 |
9.55e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 262 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYDEETTAKAdeiemimtdleranqR 338
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrkLRETQNTLNQLNKQIDELNASIA---------------K 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 339 AEVAQREAET-LREQLSSA----NHS-LQL-----ASQ-----------IQKAPdvEQAIEVLTRSSleVELAAKEREIa 396
Cdd:PRK11637 115 LEQQQAAQERlLAAQLDAAfrqgEHTgLQLilsgeESQrgerilayfgyLNQAR--QETIAELKQTR--EELAAQKAEL- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564379019 397 qlvEDVQRLQASLtkLRENSASQiSQLEQQLNAKNSTLKQLEEKL-KGQADYEDVKKELTTLK 458
Cdd:PRK11637 190 ---EEKQSQQKTL--LYEQQAQQ-QKLEQARNERKKTLTGLESSLqKDQQQLSELRANESRLR 246
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
189-298 |
9.72e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 39.17 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 189 PALDLGQQLEIKVQRLHDIETENQKLRETLEEYNkefaeVKNQEVT-IKALKEKIREYEQTLKSQAETIALEKEQKLQND 267
Cdd:cd16855 2 SHLEIRQQLEELRQRTQETENDLRNLQQKQESFV-----IQYQESQkIQAQLQQLQQQPQNERIELEQQLQQQKEQLEQL 76
|
90 100 110
....*....|....*....|....*....|.
gi 564379019 268 FAEKERKLQETQMSTTSKLEEAEHKLQTLQT 298
Cdd:cd16855 77 LNAKAQELLQLRMELADKFKKTIQLLSKLQS 107
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
331-458 |
9.82e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 331 DLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDV--------------EQAIEVLTRSSLEVELAAKEREIA 396
Cdd:PLN02939 157 DLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEIleeqleklrnelliRGATEGLCVHSLSKELDVLKEENM 236
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564379019 397 QLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLEEKLkgQADYEDVKKeLTTLK 458
Cdd:PLN02939 237 LLKDDIQFLKAELIEVAETEER-VFKLEKERSLLDASLRELESKF--IVAQEDVSK-LSPLQ 294
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
720-924 |
1.00e-02 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 720 PALKPAPLSQPDLTILNPKLLSASPMSTVSTYPPLAISLKKTPAAPEAS---TSALPSAPALKKEAQDAPTLDPPGSADA 796
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppAAVLAPAAALPPAASPAGPLPPPTSAQP 2836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379019 797 TPGVLRPvknELVRGSTWKDPWWNPVQPERRNLTtseetkadeTNASGKEKTGSSQPRAERSQLQGPSATAEywkewPNA 876
Cdd:PHA03247 2837 TAPPPPP---GPPPPSLPLGGSVAPGGDVRRRPP---------SRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFA 2899
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564379019 877 ESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 924
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| |
