|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-860 |
4.49e-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: 76.63 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 592 QKALDDLLRKVTLDGGISLKD---------------AKSSEI------LAAYERKIQMLQLELQM---------KNVPKP 641
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVRPGgvitggsaktnssilERRREIeeleekIEELEEKIAELEKALAElrkeleeleEELEQL 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 642 VVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLK---TQLTES 718
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 719 LQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISA 798
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582118 799 AEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
610-857 |
3.39e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 610 LKDAKSSEILAAY---ERKIQMLQLELQMKNVpkpvvEIETTSQKIRDLAQECEALRDSNKQLTDHMTR-GNLEINQLKV 685
Cdd:TIGR02169 220 KREYEGYELLKEKealERQKEAIERQLASLEE-----ELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 686 QLEEVKQKCDSIETSLGMC-----------------ITEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIE 748
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKereledaeerlakleaeIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 749 LFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKElelieaEKHLKLyESRLSDRE 828
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE------AKINEL-EEEKEDKA 447
|
250 260
....*....|....*....|....*....
gi 922582118 829 RDLNAKNLEIDRLKLDLDAARRNLQKLEQ 857
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-850 |
1.04e-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: 65.86 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 612 DAKSSEILAAYERKIQMLQlELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVK 691
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 692 QKCDSIETSlgmcITEKAGLKTQLTESLQNAERNVHTAQNEISKLNT-------ELAQSVTRIELFLAENRELKQEFEEK 764
Cdd:TIGR02169 336 AEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 765 VVECEVLKEHIRQIDLELKNK-------QSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLE 837
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIeakinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
250
....*....|...
gi 922582118 838 IDRLKLDLDAARR 850
Cdd:TIGR02169 492 LAEAEAQARASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
644-860 |
2.06e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKcdsietslgmcITEKAGLKTQLTESLQNAE 723
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 724 RNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKA 803
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 922582118 804 AKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
613-834 |
2.20e-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: 61.61 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 613 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIE---------TTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQL 683
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEieelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 684 KVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTES-----------------LQNAERNVHTAQNEISKLN-------TE 739
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleelesrleeleeqLETLRSKVAQLELQIASLNneierleAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 740 LAQSVTRIELFLAENRELKQEFEEKvvECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKL 819
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250
....*....|....*
gi 922582118 820 YESRLSDRERDLNAK 834
Cdd:TIGR02168 487 LQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
613-860 |
1.44e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 613 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALrDSNKQLTDhmtrgnLEINQLKVQLEEVKQ 692
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELE------EKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 693 KCDSIETSLGmcitEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLK 772
Cdd:TIGR02168 282 EIEELQKELY----ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 773 EHIRqidlELKNKQSDMERALL----QISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDL-----NAKNLEIDRLKL 843
Cdd:TIGR02168 358 AELE----ELEAELEELESRLEeleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqqEIEELLKKLEEA 433
|
250
....*....|....*..
gi 922582118 844 DLDAARRNLQKLEQMRE 860
Cdd:TIGR02168 434 ELKELQAELEELEEELE 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-857 |
1.50e-08 |
|
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: 58.54 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 613 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETtSQKIRDLAQECEALRDSNKQLTDHMTRgnlEINQLKVQLEEVKQ 692
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 693 KCDSIETSLGMCITEKAGLKTQLTESLQNAERNVHTAQNEISklntELAQsvtRIELFLAENRELKQEFEEKVVEcevlk 772
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK----SIEK---EIENLNGKKEELEEELEELEAA----- 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 773 ehIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRER------DLNAKNLEIDRLKLDLD 846
Cdd:TIGR02169 877 --LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEelseieDPKGEDEEIPEEELSLE 954
|
250
....*....|.
gi 922582118 847 AARRNLQKLEQ 857
Cdd:TIGR02169 955 DVQAELQRVEE 965
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
644-860 |
1.69e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 723
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 724 RNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEkvvecevlkehIRQIDLELKNKQSDME--RALLQISAAEQ 801
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-----------LRADLAELAALRAELEaeRAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 922582118 802 KAAKKELELIEAEKhlklyESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG4942 184 EEERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
714-860 |
2.43e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 714 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERAL 793
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE-------ELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922582118 794 LQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-860 |
3.53e-08 |
|
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: 57.39 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 682 QLKVQLEEVKQKCDSIETSLGMCITEKAGLKT---QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELK 758
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 759 QEFEEKVVECEVLKEHIRQIDLELKNKQSDMERalLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEi 838
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE- 827
|
170 180
....*....|....*....|..
gi 922582118 839 drlKLDLDAARRNLQklEQMRE 860
Cdd:TIGR02169 828 ---KEYLEKEIQELQ--EQRID 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
569-809 |
5.79e-08 |
|
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: 56.67 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 569 RNDSEDTVNLTG-----SGDIYIDKESSQKALDDllRKVTLDGGISLKDAKSSEIlAAYERKIQMLQLE----------- 632
Cdd:pfam15921 568 RQQIENMTQLVGqhgrtAGAMQVEKAQLEKEIND--RRLELQEFKILKDKKDAKI-RELEARVSDLELEkvklvnagser 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 633 -LQMKNVPKP----VVEIETTSQKIRDLAQECEALRDSNKQLTDHMtrgNLEINQLKVQL-------EEVKQKCDSIETS 700
Cdd:pfam15921 645 lRAVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM---ETTTNKLKMQLksaqselEQTRNTLKSMEGS 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 701 LGMCITEKAGLKTQLT-----------------ESLQNAERNVHTAQNEISKLNTELAQSVTrielflaenrelkqEFEE 763
Cdd:pfam15921 722 DGHAMKVAMGMQKQITakrgqidalqskiqfleEAMTNANKEKHFLKEEKNKLSQELSTVAT--------------EKNK 787
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 922582118 764 KVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELE 809
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
587-860 |
6.96e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 587 DKESSQKALDD----LLRKVTLDGGISLKDAKSSEILAAY-ERKIQMLQLElqmKNVPKPVVEIETTSQKIRDLAQECEA 661
Cdd:TIGR04523 181 EKLNIQKNIDKiknkLLKLELLLSNLKKKIQKNKSLESQIsELKKQNNQLK---DNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 662 LRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEK-AGLKTQLTESLQNAERNVHTAQNEISKLN--- 737
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQNQISQNNkii 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 738 TELAQSVTRIELFL----AENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEA 813
Cdd:TIGR04523 338 SQLNEQISQLKKELtnseSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922582118 814 EKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
674-860 |
8.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 674 TRGNLE-----INQLKVQLEEVKQKCdsietslgmcitEKAGLKTQLTESLQNAERNVhtAQNEISKLNTELAQSVTRIE 748
Cdd:COG1196 184 TEENLErlediLGELERQLEPLERQA------------EKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 749 LFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRE 828
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190
....*....|....*....|....*....|..
gi 922582118 829 RDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
595-860 |
2.18e-07 |
|
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: 54.74 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 595 LDDLLRKVTLD-----GGISLKDAKSSEIlaaYER------KIQMLQLELQMKNVpkpvvEIETTSQKIRDLAQECEALR 663
Cdd:pfam15921 375 LDDQLQKLLADlhkreKELSLEKEQNKRL---WDRdtgnsiTIDHLRRELDDRNM-----EVQRLEALLKAMKSECQGQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 664 DSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIE---TSLGMCITEKAGLKTQLTESLQNAERNVHTAQNEISKLNtel 740
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVeelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR--- 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 741 aqsvTRIELFLAENRELKQE---FEEKVVECEVLKEHIRQID--LELKNKQ-SDMERALLQ--ISAAEQKAAKKELELIE 812
Cdd:pfam15921 524 ----SRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDkvIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEI 599
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 922582118 813 AEKHLKLYESR-LSDRE----RDLNAK--NLEIDRLKLdLDAARRNLQKLEQMRE 860
Cdd:pfam15921 600 NDRRLELQEFKiLKDKKdakiRELEARvsDLELEKVKL-VNAGSERLRAVKDIKQ 653
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
614-855 |
3.01e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.07 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 614 KSSEILAAYERkiQMLQLELQMKNVPKPVVEIETT-SQKIRDLAQECEALRDSN------------KQLTDHMTRGNLEI 680
Cdd:PRK04778 195 EAREILDQLEE--ELAALEQIMEEIPELLKELQTElPDQLQELKAGYRELVEEGyhldhldiekeiQDLKEQIDENLALL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 681 NQLKvqLEEVKQKCDSIETSLgmcitekaglkTQLTESLqnaERNVHtAQNEISKLNTELAQSVTRIElflAENRELKQE 760
Cdd:PRK04778 273 EELD--LDEAEEKNEEIQERI-----------DQLYDIL---EREVK-ARKYVEKNSDTLPDFLEHAK---EQNKELKEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 761 FEE-----KVVECEVlkEHIRQIDLELKNKQSDMERALLQISA---------AEQKAAKKELELIEaEKHLKLYESRLSD 826
Cdd:PRK04778 333 IDRvkqsyTLNESEL--ESVRQLEKQLESLEKQYDEITERIAEqeiayselqEELEEILKQLEEIE-KEQEKLSEMLQGL 409
|
250 260
....*....|....*....|....*....
gi 922582118 827 RERDLNAKNlEIDRLKLDLDAARRNLQKL 855
Cdd:PRK04778 410 RKDELEARE-KLERYRNKLHEIKRYLEKS 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
617-856 |
8.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 617 EILAAYERKIQML-QLELQMKNVPKpvveiETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCD 695
Cdd:PRK03918 355 EELEERHELYEEAkAKKEELERLKK-----RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 696 SIETSLGMC------ITE--KAGLKTQLTESLQNAERNVHTAQNEISKLNTELaqsvTRIELFLAENREL---------- 757
Cdd:PRK03918 430 ELKKAKGKCpvcgreLTEehRKELLEEYTAELKRIEKELKEIEEKERKLRKEL----RELEKVLKKESELiklkelaeql 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 758 -----------KQEFEEKVVECEVLKEHIRQIDLELKNKQSDMER-ALLQISAAEQKAAKKELE---------------- 809
Cdd:PRK03918 506 keleeklkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKlEELKKKLAELEKKLDELEeelaellkeleelgfe 585
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 922582118 810 -LIEAEKHLKLYES------RLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLE 856
Cdd:PRK03918 586 sVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
679-860 |
1.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 679 EINQLKVQLEEVKQKCDSIETSLgmciTEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELK 758
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 759 QEFEEKVvecEVLKEHIRQI-------DLELKNKQSDMERAL--LQISAAEQKAAKKELELIEAEKhlklyeSRLSDRER 829
Cdd:COG4942 97 AELEAQK---EELAELLRALyrlgrqpPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADL------AELAALRA 167
|
170 180 190
....*....|....*....|....*....|.
gi 922582118 830 DLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQ 198
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
644-857 |
2.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSlgmcITEKAGLKTQLTESLQNAE 723
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 724 RNVHTAQNEISKLN--------TELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALlq 795
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK-- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582118 796 iSAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 857
Cdd:COG3883 171 -AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
623-860 |
3.19e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 623 ERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRD------SNKQLTDHMTrgNLEINQLKVQLEEVKQKCDS 696
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliKLKELAEQLK--ELEEKLKKYNLEELEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 697 IETSLGMCITEKAGLKT---------QLTESLQNAERNVHTAQNEISKLNTELAQ----SVTRIELFLAENREL------ 757
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSlkkelekleELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFyneyle 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 758 ----KQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEaEKHLKLyesrlsdrERDLNA 833
Cdd:PRK03918 607 lkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-EEYLEL--------SRELAG 677
|
250 260
....*....|....*....|....*..
gi 922582118 834 KNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
629-859 |
6.49e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 629 LQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEK 708
Cdd:pfam12128 583 VKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 709 AGLKTQLTESLQNAERnvhTAQNEISKLNTELAQSVTRIELFLA-------ENRELKQEFEEKVVEcevlkehirqidlE 781
Cdd:pfam12128 663 QSEKDKKNKALAERKD---SANERLNSLEAQLKQLDKKHQAWLEeqkeqkrEARTEKQAYWQVVEG-------------A 726
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582118 782 LKNKqsdmERALLQISAAEQKAAKKELELIEAEKHlklyesrlsdreRDLNAKNLEIDRLkLDLDAARRNL-QKLEQMR 859
Cdd:pfam12128 727 LDAQ----LALLKAAIAARRSGAKAELKALETWYK------------RDLASLGVDPDVI-AKLKREIRTLeRKIERIA 788
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
541-844 |
8.73e-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: 49.72 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 541 SEMVASCKSTSQPVSLSQKDSSPDFNRCRNDSEDTVNLTGSGDiYIDKESSQKAlDDLlrKVTLDGgiSLKDAKSSEILA 620
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE-SVREEFIQKG-DEV--KCKLDK--SEENARSIEYEV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 621 AYERKiQMLQLELQMKNVPKpvvEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETS 700
Cdd:pfam05483 583 LKKEK-QMKILENKCNNLKK---QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 701 LGMCITEKAGLKTQLTESLQNAERNVhtaqNEISKLntelaqsvtrielflaeNRELKQEFEEKVVECEVLKE-HIRQID 779
Cdd:pfam05483 659 YQKEIEDKKISEEKLLEEVEKAKAIA----DEAVKL-----------------QKEIDKRCQHKIAEMVALMEkHKHQYD 717
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582118 780 LELKNKqsDMERALLQISAAEQKAAKKELELieaekHLKLYESRLSDRERDLNAKNLEIDRLKLD 844
Cdd:pfam05483 718 KIIEER--DSELGLYKNKEQEQSSAKAALEI-----ELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
644-856 |
9.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSNKQLTDHMTrgnlEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 723
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 724 R-----NVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMER------- 791
Cdd:PRK03918 284 ElkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhel 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582118 792 ----ALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLE 856
Cdd:PRK03918 364 yeeaKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
619-821 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 619 LAAYERKIQmlQLELQMKNVPKPVVEIEttsQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKcdsie 698
Cdd:COG1579 12 LQELDSELD--RLEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 699 tsLGMCITEKAglktqltesLQNAERNVHTAQNEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQI 778
Cdd:COG1579 82 --LGNVRNNKE---------YEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 922582118 779 DLELKNKQSDMERALLQISAAEQKAAKKelelIEAEkHLKLYE 821
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAK----IPPE-LLALYE 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
653-854 |
1.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 653 RDLAQECEALRDSNKQLTDhmTRGNLEINQLKV-QLEEVKQKCDSIETSLgmciTEKAGLKTQLTE-SLQNAERNVHTAQ 730
Cdd:COG4913 221 PDTFEAADALVEHFDDLER--AHEALEDAREQIeLLEPIRELAERYAAAR----ERLAELEYLRAAlRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 731 NEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQIDLElknkqsDMERALLQISAAEQKAAKKELEL 810
Cdd:COG4913 295 AELEELRAELARLEAELE-------RLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 922582118 811 IEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQK 854
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
711-857 |
3.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 711 LKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEkvvecevLKEHIRQIDLELKNKQSDME 790
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-------LEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582118 791 RALLQISAAEQKAAKKELELIEAEKHLKL-------YESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 857
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDleqqrkqLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
614-835 |
4.68e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 614 KSSEILAAYERKIQMLQLELQMKNVPKPVVE-IETTSQKIRDLAQECEALRDSNKQLTDhmTRGNLEInqLKVQLEEVKQ 692
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnSKSELARIPELEKELERLREHNKHLNE--NIENKLL--LKEEVEDLKR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 693 KCDSIETSLgmciTEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSvTRIELFLAENRELKQefEEKVVECEVLK 772
Cdd:pfam05557 236 KLEREEKYR----EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQQREIVLKE--ENSSLTSSARQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582118 773 EHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELE--LIEAEKHLKLYESRLSDRERDLNAKN 835
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQrrVLLLTKERDGYRAILESYDKELTMSN 373
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
644-859 |
6.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSN---------KQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMcitekagLKTQ 714
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS-------GPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 715 LTESLQNAErnVHTAQNEISKLNTELAQSVTRielFLAENRELKQefeekvvecevLKEHIRQIDLELKNkqsdMERALL 794
Cdd:COG3206 256 LPELLQSPV--IQQLRAQLAELEAELAELSAR---YTPNHPDVIA-----------LRAQIAALRAQLQQ----EAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582118 795 QISAAEQKAAKKELELIEAEkhlklyESRLSDRERDLNAKNLEIDRLKLDLDAARRN----LQKLEQMR 859
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLEREVEVARELyeslLQRLEEAR 378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-858 |
7.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 679 EINQLKVQLEEVKQKCDSIEtSLGMCITEKAGLKTQLTESLQNAER--NVHTAQNEISKLNTELAQSVTRIELFLAENRE 756
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 757 LKQefeekvvecevLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKK-ELELIEAEKHLKLYESRLSDRERDLNAKN 835
Cdd:COG4717 158 LRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 922582118 836 LEIDRLKLDL--DAARRNLQKLEQM 858
Cdd:COG4717 227 EELEQLENELeaAALEERLKEARLL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
705-854 |
1.03e-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: 44.53 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 705 ITEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQ---SVTRIELFLAENRELKQEFEEKVVECEVLKEhirqidle 781
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-------- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922582118 782 LKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQK 854
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
715-848 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 715 LTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFlaeNRELKQEFEEKVVEcevlkEHIRQIDlELKNKQSDMERALL 794
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL---QRLAEYSWDEIDVA-----SAEREIA-ELEAELERLDASSD 685
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 922582118 795 QISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAA 848
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
618-858 |
1.37e-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: 45.48 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 618 ILAAYERKIQMLQLELQ---------MKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEinqLKVQLE 688
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTaiktseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE---LKKHQE 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 689 EVKQkcdsietslgmCITEKAGLKTQLtESLQNAERNVhtaQNEISKLntelaqsvtrielflaeNRELKQEFEEkvVEC 768
Cdd:pfam05483 521 DIIN-----------CKKQEERMLKQI-ENLEEKEMNL---RDELESV-----------------REEFIQKGDE--VKC 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 769 EVLK--EHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLD 846
Cdd:pfam05483 567 KLDKseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
250
....*....|..
gi 922582118 847 AARrnlQKLEQM 858
Cdd:pfam05483 647 SAK---QKFEEI 655
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
714-860 |
1.46e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 714 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERAL 793
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582118 794 LQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLD--LDAARRNLQKLEQMRE 860
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKEEELAE 204
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
638-860 |
1.69e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 638 VPKPVV---EIETTSQKIRDLAQECEAlrdSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQ 714
Cdd:pfam07888 26 VPRAELlqnRLEECLQERAELLQAQEA---ANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 715 LTEslqnAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQsdmerall 794
Cdd:pfam07888 103 YKE----LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE-------- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922582118 795 qisaAEQKAAKKELELIEAEKH---LKLYESRLSDRERDLNAKNL--EIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:pfam07888 171 ----AERKQLQAKLQQTEEELRslsKEFQELRNSLAQRDTQVLQLqdTITTLTQKLTTAHRKEAENEALLE 237
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
674-858 |
1.72e-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: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 674 TRGNLE-INQLKVQLEEVKQKCDSIETSLgmciTEKAGLKTQLTESLQNAERNVHTAQNEI---SKLNTELAQSVTRIel 749
Cdd:pfam13851 21 TRNNLElIKSLKEEIAELKKKEERNEKLM----SEIQQENKRLTEPLQKAQEEVEELRKQLenyEKDKQSLKNLKARL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 750 flaenRELKQEFEEKVVECEVLKEHIRQIDLE---LKNKQSDMerallqISAAEQKAAKKELELieaEKHLKLYESRLSD 826
Cdd:pfam13851 95 -----KVLEKELKDLKWEHEVLEQRFEKVERErdeLYDKFEAA------IQDVQQKTGLKNLLL---EKKLQALGETLEK 160
|
170 180 190
....*....|....*....|....*....|..
gi 922582118 827 RERDLNAKnleIDRLKLDLDAARRNLQKLEQM 858
Cdd:pfam13851 161 KEAQLNEV---LAAANLDPDALQAVTEKLEDV 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
619-851 |
1.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 619 LAAYERKIQMLQLEL--------QMKNVPKPVVEIETTSQKIR-------DLAQECEALRDSNKQLtDHMTRGNLEINQL 683
Cdd:COG4913 612 LAALEAELAELEEELaeaeerleALEAELDALQERREALQRLAeyswdeiDVASAEREIAELEAEL-ERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 684 KVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTEslqnAERNVHTAQNEISklntELAQSVTRIELFLAENR---ELKQE 760
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLE----AAEDLARLELRALLEERfaaALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 761 FEEKVVecEVLKEHIRQIDLELKNKQSDMERAL-------------LQISAAEQKAAKKELELIEAEkHLKLYESRLSDR 827
Cdd:COG4913 763 VERELR--ENLEERIDALRARLNRAEEELERAMrafnrewpaetadLDADLESLPEYLALLDRLEED-GLPEYEERFKEL 839
|
250 260
....*....|....*....|....*
gi 922582118 828 erdLNAKNLE-IDRLKLDLDAARRN 851
Cdd:COG4913 840 ---LNENSIEfVADLLSKLRRAIRE 861
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
627-855 |
1.93e-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: 44.84 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 627 QMLQLELQMKNVPKPVVEIETT-SQKIRDLAQECEALRDSNKQLTDHmtrgNL--EINQLKVQLEEVKQ-----KCDSIE 698
Cdd:pfam06160 187 ETDALEELMEDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHL----NVdkEIQQLEEQLEENLAllenlELDEAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 699 TSLGMcITEKaglKTQLTESLqnaERNVHtAQNEISKLNTELAQSVTRIElflAENRELKQEFEEkVVECEVLKEH---- 774
Cdd:pfam06160 263 EALEE-IEER---IDQLYDLL---EKEVD-AKKYVEKNLPEIEDYLEHAE---EQNKELKEELER-VQQSYTLNENeler 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 775 IRQIDLELKNKQSDMERALLQISAAEQ---------KAAKKELELIEaEKHLKLYESRLSDRERDLNAKNlEIDRLKLDL 845
Cdd:pfam06160 331 VRGLEKQLEELEKRYDEIVERLEEKEVayselqeelEEILEQLEEIE-EEQEEFKESLQSLRKDELEARE-KLDEFKLEL 408
|
250
....*....|
gi 922582118 846 DAARRNLQKL 855
Cdd:pfam06160 409 REIKRLVEKS 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
752-855 |
2.65e-04 |
|
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: 44.37 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 752 AENRELKQEFEEkvvecevLKEHIRQIDLELKNKQSDMERALLQISAAEQKaakkeleLIEAEKHLKLYESRLSDRERDL 831
Cdd:COG4942 20 DAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 922582118 832 NAKNLEIDRLKLDLDAARRNLQKL 855
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
625-860 |
2.93e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 625 KIQMLQLELQM------KNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIE 698
Cdd:pfam05483 223 KIQHLEEEYKKeindkeKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 699 TSLGMCITEKAGLKT----------QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLaenRELKQEFEEKvvec 768
Cdd:pfam05483 303 MSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKN---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 769 evlKEHIRQIDLELKNKQSDMERalLQISAAEQKAAKKELELIEAEKHLKLYESRlsdrerdlnaknlEIDRLKLDLDAA 848
Cdd:pfam05483 376 ---EDQLKIITMELQKKSSELEE--MTKFKNNKEVELEELKKILAEDEKLLDEKK-------------QFEKIAEELKGK 437
|
250
....*....|..
gi 922582118 849 RRNLQKLEQMRE 860
Cdd:pfam05483 438 EQELIFLLQARE 449
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
614-859 |
4.00e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 614 KSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKirDLAQECEALRD-----SNKQLTDHMTRGNLEINQLKVQLE 688
Cdd:pfam17380 331 RQAAIYAEQERMAMERERELERIRQEERKRELERIRQE--EIAMEISRMRElerlqMERQQKNERVRQELEAARKVKILE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 689 EVKQKcdsietslgmcitekaGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIelflaenRELKQEFEEKVvec 768
Cdd:pfam17380 409 EERQR----------------KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV-------RLEEQERQQQV--- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 769 evlkEHIRQIDLELKNKQSDMERALLQISAAEQ---KAAKKELE-----LIEAEKHLKLYESRLSDRERDL----NAKNL 836
Cdd:pfam17380 463 ----ERLRQQEEERKRKKLELEKEKRDRKRAEEqrrKILEKELEerkqaMIEEERKRKLLEKEMEERQKAIyeeeRRREA 538
|
250 260
....*....|....*....|...
gi 922582118 837 EIDRLKLDLDAARRNLQklEQMR 859
Cdd:pfam17380 539 EEERRKQQEMEERRRIQ--EQMR 559
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
651-842 |
4.31e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 651 KIRDLAQE---CEALRDSNKQLTDhmTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAgLKTQLTESLQNAERNVH 727
Cdd:PHA02562 175 KIRELNQQiqtLDMKIDHIQQQIK--TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKA-EIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 728 TAQNEISKLNTELAQSVTRIELFlaeNRELKqeFEEKVVECEVLKEHIRQID---LELKNKQSDMERALLQISAAEQKAA 804
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQF---QKVIK--MYEKGGVCPTCTQQISEGPdriTKIKDKLKELQHSLEKLDTAIDELE 326
|
170 180 190
....*....|....*....|....*....|....*...
gi 922582118 805 KKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLK 842
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK 364
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
732-857 |
4.67e-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: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 732 EISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDME--RALLQISAAEQKAAK--KE 807
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEevEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 922582118 808 LELIEAE-KHLKLYESRLSDRERDLNAknlEIDRLKLDLDAARRNLQKLEQ 857
Cdd:COG1579 91 YEALQKEiESLKRRISDLEDEILELME---RIEELEEELAELEAELAELEA 138
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
623-849 |
6.17e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 623 ERKIQMLQLELQM--KNVPKPVVEIETTSQKIRDLAQE----------CEALRDSNKQLTDHMTRgnlEINQLKVQLEEV 690
Cdd:TIGR04523 411 DEQIKKLQQEKELleKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRESLETQLKVLSR---SINKIKQNLEQK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 691 KQKCDSIETSLGMCITEKaglkTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRI----ELFLAENRELKQEFEEKVV 766
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEK----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNKDDFELKKENLEKEI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 767 -----ECEVLKEHI-------RQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAK 834
Cdd:TIGR04523 564 deknkEIEELKQTQkslkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
250
....*....|....*
gi 922582118 835 NLEIDRLKLDLDAAR 849
Cdd:TIGR04523 644 KQEVKQIKETIKEIR 658
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
712-860 |
7.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 712 KTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEF----------EEKVVEC-EVLKEHIRQI-- 778
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqaeiaeaEAEIEERrEELGERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 779 ----------------------DLELKNKQSDMERALL-QISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKN 835
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldRLSALSKIADADADLLeELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....*
gi 922582118 836 LEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
593-857 |
9.08e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 593 KALDDLLRKVTLDGGISLKDAKSSEILAAYERKIQMlqlelqmknvPKPVVEIETTSQKIRDLAqecealrdsnkqltdh 672
Cdd:pfam09731 189 EALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKL----------PEHLDNVEEKVEKAQSLA---------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 673 mtrgnLEINQLKVQLEE----VKQKCDSIETSLGMCITEKAGLKTQLTESLqnaernVHTAQNEISKLNTELAQSVTRIE 748
Cdd:pfam09731 243 -----KLVDQYKELVASerivFQQELVSIFPDIIPVLKEDNLLSNDDLNSL------IAHAHREIDQLSKKLAELKKREE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 749 LFLAENRElKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIE--AEKHLK--LYESRL 824
Cdd:pfam09731 312 KHIERALE-KQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAeaHEEHLKdvLVEQEI 390
|
250 260 270
....*....|....*....|....*....|....*..
gi 922582118 825 S-DRE--RDLNAKNL-EIDRLKLDLDAARRNLQKLEQ 857
Cdd:pfam09731 391 ElQREflQDIKEKVEeERAGRLLKLNELLANLKGLEK 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-859 |
1.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQK------IRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLeeVKQKCDSIETSLgmcitekaglkTQLTE 717
Cdd:COG4913 243 ALEDAREQiellepIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAEL-----------ARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 718 SLQNAERNVHTAQNEISKLNTELAQS-VTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQI 796
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582118 797 sAAEQKAAKKELELIEAEKHlklyesRLSDRERDLNAknleidrlkldldaARRNLQK-LEQMR 859
Cdd:COG4913 390 -AALLEALEEELEALEEALA------EAEAALRDLRR--------------ELRELEAeIASLE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
614-860 |
1.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 614 KSSEILAAYERKIQMLQ-LELQMKNVPKPVVEIETT----SQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLE 688
Cdd:PRK02224 238 EADEVLEEHEERREELEtLEAEIEDLRETIAETEREreelAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 689 EVKQKCDSIETSLGMCitekaglKTQLTESLQNAERnvhtaqneisklnteLAQSVTRIELFLAENRELKQEFEEKVVEC 768
Cdd:PRK02224 318 ELEDRDEELRDRLEEC-------RVAAQAHNEEAES---------------LREDADDLEERAEELREEAAELESELEEA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 769 EVLKEhirqidlELKNKQSDMERallQISAAEQKAAKKELELIEAEKHLKLYESRLSD-RERdlnaknleIDRLKLDLDA 847
Cdd:PRK02224 376 REAVE-------DRREEIEELEE---EIEELRERFGDAPVDLGNAEDFLEELREERDElRER--------EAELEATLRT 437
|
250
....*....|...
gi 922582118 848 ARRNLQKLEQMRE 860
Cdd:PRK02224 438 ARERVEEAEALLE 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
731-860 |
1.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 731 NEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAakKELEL 810
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKE 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 922582118 811 IE--AEKHLKLYE--SRLSDRERDLnakNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:PRK03918 288 LKekAEEYIKLSEfyEEYLDELREI---EKRLSRLEEEINGIEERIKELEEKEE 338
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
753-860 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 753 ENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERD-- 830
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 922582118 831 ------------LNAKNLE--IDRLKLDLDAARRNLQKLEQMRE 860
Cdd:COG3883 97 rsggsvsyldvlLGSESFSdfLDRLSALSKIADADADLLEELKA 140
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
625-855 |
1.75e-03 |
|
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: 41.93 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 625 KIQMLQLELQMKNVPKPVVEIEttsQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSlgmc 704
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT---- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 705 itekaglKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKN 784
Cdd:TIGR04523 463 -------RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582118 785 KqsdmerallqisaaEQKAAKKELELIEAEKHLKlyesrLSDRERDLNAKNLEIDRLKLD---LDAARRNLQKL 855
Cdd:TIGR04523 536 K--------------ESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTqksLKKKQEEKQEL 590
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
605-858 |
2.19e-03 |
|
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: 41.42 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 605 DGGISLKDAKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQltdhmtrgnlEINQLK 684
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA----------ERKQLQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 685 VQLEEVKQKCDSIETSLgmcitekaglkTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRI---ELFLAENRELKQEF 761
Cdd:pfam07888 178 AKLQQTEEELRSLSKEF-----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 762 EEKVVECEVLKEHIRQIDLELKNKQSDMERALLQisaaeqkAAKKELELIEAEKHLKLYESRLSdRERDLNAKNLEIDRL 841
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAELHQARLQ-------AAQLTLQLADASLALREGRARWA-QERETLQQSAEADKD 318
|
250
....*....|....*...
gi 922582118 842 KLD-LDAArrnLQKLEQM 858
Cdd:pfam07888 319 RIEkLSAE---LQRLEER 333
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
625-859 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 625 KIQMLQLELQmkNVPKPVVEIETTSQKI-RDLAQECEALRDSNKQLTDHmTRGNLEINQLKVQLEEvkqkcdsietslgm 703
Cdd:pfam01576 434 KLSKLQSELE--SVSSLLNEAEGKNIKLsKDVSSLESQLQDTQELLQEE-TRQKLNLSTRLRQLED-------------- 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 704 citEKAGLKTQL---TESLQNAERNVHTAQNEISKLNTELAQSVTRIEL-------FLAENRELKQEFEEKVVECEVLK- 772
Cdd:pfam01576 497 ---ERNSLQEQLeeeEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAleegkkrLQRELEALTQQLEEKAAAYDKLEk 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 773 ----------------EHIRQIDLELKNKQSDMERALLQ---ISA--------AEQKAAKKELELIEAEKHLKLYESRLS 825
Cdd:pfam01576 574 tknrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLAEekaISAryaeerdrAEAEAREKETRALSLARALEEALEAKE 653
|
250 260 270
....*....|....*....|....*....|....
gi 922582118 826 DRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMR 859
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
511-858 |
2.40e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 511 ISYGDQETVQQAFLTYSHcaQVPAFPSHL-------------LSEMVASCKSTSQPVSLsQKDSSPDFNR--------CR 569
Cdd:pfam15921 68 IAYPGKEHIERVLEEYSH--QVKDLQRRLnesnelhekqkfyLRQSVIDLQTKLQEMQM-ERDAMADIRRresqsqedLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 570 NDSEDTVN-LTGSGDIYIDKESSQKALDDLLRKVTLDGGISLKDAKSseILAAYE----RKI--QMLQLELQMKNVPKPV 642
Cdd:pfam15921 145 NQLQNTVHeLEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRS--ILVDFEeasgKKIyeHDSMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 643 veiettSQKIRDLAQECEALRDSNKQLTDHMTRGNLEiNQLKVQLEeVKQKCDSIETSLG------MCITEKAGLKTQLT 716
Cdd:pfam15921 223 ------SKILRELDTEISYLKGRIFPVEDQLEALKSE-SQNKIELL-LQQHQDRIEQLISeheveiTGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 717 ESLQNAERNVH-TAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVEcevLKEHIRQIDLELKNKQSDMERALLQ 795
Cdd:pfam15921 295 NSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922582118 796 ISAAEQKAAKKELELIEAEKHLKLYES---RLSDRErdlNAKNLEIDRLKLDLDAARRNLQKLEQM 858
Cdd:pfam15921 372 SGNLDDQLQKLLADLHKREKELSLEKEqnkRLWDRD---TGNSITIDHLRRELDDRNMEVQRLEAL 434
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
593-853 |
2.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 593 KALDDLlRKVTLDGGISLKDAKSSEIL------AAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSN 666
Cdd:TIGR00606 186 KALETL-RQVRQTQGQKVQEHQMELKYlkqykeKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 667 KQLTDHMT---RGNLEINQLKVQLEEVKQKCdsietslgmciteKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQS 743
Cdd:TIGR00606 265 MKLDNEIKalkSRKKQMEKDNSELELKMEKV-------------FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 744 VTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIE--AEKHLKLYE 821
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIerQEDEAKTAA 411
|
250 260 270
....*....|....*....|....*....|..
gi 922582118 822 SRLSDRERDLNAKNLEIDRLKLDLDAARRNLQ 853
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIE 443
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
734-857 |
2.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 734 SKLNTELAQSVTRIELFLAE-NRELKQEFEEKVVEcevLKEhirqidlELKNKQSDMERallQISAAEQKAAKKELELIE 812
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLE---AKE-------EIHKLRNEFEK---ELRERRNELQKLEKRLLQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 922582118 813 AEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 857
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
612-855 |
3.51e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 612 DAKSSEILAAYERKIQMLQ-------LELQMKNVPKPVVE-IETTSQKIRDLAQECEALRD--SNKQLTDHMTRGNLEIN 681
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAaaeaeqeLEESKRETETGIQNlTAEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 682 QLKVQLEEVKQKCDSIETSlgmcitekagLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEF 761
Cdd:COG5185 381 SFKDTIESTKESLDEIPQN----------QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISEL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 762 EEKVVECEV-----LKEHIRQIDLELKNKQSDMERALLQIsAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNL 836
Cdd:COG5185 451 NKVMREADEesqsrLEEAYDEINRSVRSKKEDLNEELTQI-ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF 529
|
250
....*....|....*....
gi 922582118 837 EIDRlKLDLDAARRNLQKL 855
Cdd:COG5185 530 MRAR-GYAHILALENLIPA 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
592-860 |
3.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 592 QKALDDLL--------RKVTLDGGISLKDAKSseilaayERKIQMLQLELQM-----KNVPKPVVEIETTSQKIRDLAQE 658
Cdd:PRK02224 152 QDMIDDLLqlgkleeyRERASDARLGVERVLS-------DQRGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 659 CEALRDSNKQltdhmTRGNL-----EINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQlteslqnaernVHTAQNEI 733
Cdd:PRK02224 225 YEEQREQARE-----TRDEAdevleEHEERREELETLEAEIEDLRETIAETEREREELAEE-----------VRDLRERL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 734 SKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEA 813
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922582118 814 EKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
630-811 |
3.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 630 QLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRgnLEInqlKVQLEEVKQKCDSIETSLGMCITEKA 709
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEK---LLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 710 GLKTQLTEsLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAEN-RELKQEFEEKVVECEVLKEHIRQIDLELKNKQSD 788
Cdd:COG4717 150 ELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|...
gi 922582118 789 MERALLQISAAEQKAAKKELELI 811
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLL 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
717-842 |
4.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 717 ESLQNAERNvhtaqneISKLNTELAQSVTRIELFLA-----ENR--ELKQEFEEKVVECEVLKEHIRQIDLELKNkqsdM 789
Cdd:PRK03918 158 DDYENAYKN-------LGEVIKEIKRRIERLEKFIKrteniEELikEKEKELEEVLREINEISSELPELREELEK----L 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 922582118 790 ERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLK 842
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-848 |
4.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 644 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 723
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 724 RnvhtAQNEISKLNTELAQSVTRIElflaENRELKQefEEKVVECEVLKE---HIRQIDlELKNKQSDMERALLQIsAAE 800
Cdd:PRK02224 423 E----LREREAELEATLRTARERVE----EAEALLE--AGKCPECGQPVEgspHVETIE-EDRERVEELEAELEDL-EEE 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582118 801 QKAAKKELE----LIEAEKHL-------KLYESRLSDRERDLNAKNLEIDRL---KLDLDAA 848
Cdd:PRK02224 491 VEEVEERLEraedLVEAEDRIerleerrEDLEELIAERRETIEEKRERAEELrerAAELEAE 552
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
715-860 |
4.33e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 715 LTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKvvecevlKEHIRQIDLELKnkqsdmerall 794
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-------DERIERLERELS----------- 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922582118 795 qisaaeqKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRnLQKLEQMRE 860
Cdd:COG2433 452 -------EARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGE 509
|
|
| BAR |
smart00721 |
BAR domain; |
712-860 |
4.91e-03 |
|
BAR domain;
Pssm-ID: 214787 [Multi-domain] Cd Length: 239 Bit Score: 39.67 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 712 KTQLTESLQNAERNVHTAQNEISKLntelaqsVTRIELFLAENRELKQEFEEKVVECEVLKE-HIRQIDLELKNKQSDME 790
Cdd:smart00721 22 KTKLDEDFEELERRFDTTEAEIEKL-------QKDTKLYLQPNPAVRAKLASQKKLSKSLGEvYEGGDDGEGLGADSSYG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582118 791 RALLQISAAEQKAAKKELELIEAEKH-----LKLYESRLSDrerdLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:smart00721 95 KALDKLGEALKKLLQVEESLSQVKRTfilplLNFLLGEFKE----IKKARKKLERKLLDYDSARHKLKKAKKSKE 165
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
619-857 |
5.16e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 619 LAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQEcealrdsnkqltdhmtRGNLE--INQLKVQLEEVKQKcds 696
Cdd:pfam15905 49 TPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQE----------------RGEQDkrLQALEEELEKVEAK--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 697 ietsLGMCITEKaglkTQLTESLQNAERNVH--TAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEh 774
Cdd:pfam15905 110 ----LNAAVREK----TSLSASVASLEKQLLelTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 775 irQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKH---LKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRN 851
Cdd:pfam15905 181 --GMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSEtekLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDE 258
|
....*.
gi 922582118 852 LQKLEQ 857
Cdd:pfam15905 259 IESLKQ 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
714-821 |
5.53e-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: 40.54 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 714 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENR-------ELKQEFEEKVVECEVLKEHIRQidLELKNKQ 786
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRrleariaQLEEELEEEQSNTELLNDRLRK--STLQVEQ 921
|
90 100 110
....*....|....*....|....*....|....*
gi 922582118 787 SDMERALLQISAAEQKAAKKELELIEAEKHLKLYE 821
Cdd:pfam01576 922 LTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
|
| BAR |
pfam03114 |
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ... |
712-860 |
5.94e-03 |
|
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.
Pssm-ID: 460810 [Multi-domain] Cd Length: 235 Bit Score: 39.24 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 712 KTQLTESLQNAERNVHTAQNEISKLntelaqsVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMEr 791
Cdd:pfam03114 21 KTKLDEDFEELERRFDTTEKEIKKL-------QKDTKGYLQPNPGARAKQTVLEQPEELLAESMIEAGKDLGEDSSFGK- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582118 792 ALLQISAAEQKAAKKELEL-IEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 860
Cdd:pfam03114 93 ALEDYGEALKRLAQLLEQLdDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKS 162
|
|
| |
