|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
648-916 |
3.67e-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: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 648 QKALDDLLRKVTLDGGISLKD---------------AKSSEI------LAAYERKIQMLQLELQM---------KNVPKP 697
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVRPGgvitggsaktnssilERRREIeeleekIEELEEKIAELEKALAElrkeleeleEELEQL 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 698 VVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLK---TQLTES 774
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 775 LQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISA 854
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582116 855 AEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
666-913 |
2.81e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 666 LKDAKSSEILAAY---ERKIQMLQLELQMKNVpkpvvEIETTSQKIRDLAQECEALRDSNKQLTDHMTR-GNLEINQLKV 741
Cdd:TIGR02169 220 KREYEGYELLKEKealERQKEAIERQLASLEE-----ELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 742 QLEEVKQKCDSIETSLGMC-----------------ITEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIE 804
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKereledaeerlakleaeIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 805 LFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKElelieaEKHLKLyESRLSDRE 884
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE------AKINEL-EEEKEDKA 447
|
250 260
....*....|....*....|....*....
gi 922582116 885 RDLNAKNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
668-906 |
8.69e-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: 66.24 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 668 DAKSSEILAAYERKIQMLQlELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVK 747
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 748 QKCDSIETSlgmcITEKAGLKTQLTESLQNAERNVHTAQNEISKLNT-------ELAQSVTRIELFLAENRELKQEFEEK 820
Cdd:TIGR02169 336 AEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 821 VVECEVLKEHIRQIDLELKNK-------QSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLE 893
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIeakinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
250
....*....|...
gi 922582116 894 IDRLKLDLDAARR 906
Cdd:TIGR02169 492 LAEAEAQARASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
700-916 |
2.09e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKcdsietslgmcITEKAGLKTQLTESLQNAE 779
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 780 RNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKA 859
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 922582116 860 AKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-890 |
1.90e-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: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 669 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIE---------TTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQL 739
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEieelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 740 KVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTES-----------------LQNAERNVHTAQNEISKLN-------TE 795
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleelesrleeleeqLETLRSKVAQLELQIASLNneierleAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 796 LAQSVTRIELFLAENRELKQEFEEKvvECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKL 875
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250
....*....|....*
gi 922582116 876 YESRLSDRERDLNAK 890
Cdd:TIGR02168 487 LQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-916 |
1.10e-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: 59.30 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 669 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALrDSNKQLTDhmtrgnLEINQLKVQLEEVKQ 748
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELE------EKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 749 KCDSIETSLGmcitEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLK 828
Cdd:TIGR02168 282 EIEELQKELY----ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 829 EHIRqidlELKNKQSDMERALL----QISAAEQKAAKKELELIEAEKHLKLYESRLSD----RERDLNAKNLEIDRL-KL 899
Cdd:TIGR02168 358 AELE----ELEAELEELESRLEeleeQLETLRSKVAQLELQIASLNNEIERLEARLERledrRERLQQEIEELLKKLeEA 433
|
250
....*....|....*..
gi 922582116 900 DLDAARRNLQKLEQMRE 916
Cdd:TIGR02168 434 ELKELQAELEELEEELE 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-913 |
1.19e-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: 59.31 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 669 AKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETtSQKIRDLAQECEALRDSNKQLTDHMTRgnlEINQLKVQLEEVKQ 748
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 749 KCDSIETSLGMCITEKAGLKTQLTESLQNAERNVHTAQNEISklntELAQsvtRIELFLAENRELKQEFEEKVVEcevlk 828
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK----SIEK---EIENLNGKKEELEEELEELEAA----- 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 829 ehIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRER------DLNAKNLEIDRLKLDLD 902
Cdd:TIGR02169 877 --LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEelseieDPKGEDEEIPEEELSLE 954
|
250
....*....|.
gi 922582116 903 AARRNLQKLEQ 913
Cdd:TIGR02169 955 DVQAELQRVEE 965
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-916 |
1.53e-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: 57.85 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 779
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 780 RNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEkvvecevlkehIRQIDLELKNKQSDME--RALLQISAAEQ 857
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-----------LRADLAELAALRAELEaeRAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 922582116 858 KAAKKELELIEAEKhlklyESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG4942 184 EEERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
643-912 |
2.41e-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: 58.11 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 643 DKESSQKALDD----LLRKVTLDGGISLKDAKSSEILAAY-ERKIQMLQLElqmKNVPKPVVEIETTSQKIRDLAQECEA 717
Cdd:TIGR04523 181 EKLNIQKNIDKiknkLLKLELLLSNLKKKIQKNKSLESQIsELKKQNNQLK---DNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 718 LRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEK-AGLKTQLTESLQNAERNVHTAQNEISKLN--- 793
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQNQISQNNkii 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 794 TELAQSVTRIELFL----AENRELKQEFEEKVVECEVLKEHIRQIDLE---LKNKQSDMERALLQISAAEQ------KAA 860
Cdd:TIGR04523 338 SQLNEQISQLKKELtnseSENSEKQRELEEKQNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQqkdeqiKKL 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 922582116 861 KKELELIEAE-KHLK----LYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLE 912
Cdd:TIGR04523 418 QQEKELLEKEiERLKetiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
770-916 |
2.47e-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: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 770 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERAL 849
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE-------ELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922582116 850 LQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
738-916 |
3.41e-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: 57.77 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 738 QLKVQLEEVKQKCDSIETSLGMCITEKAGLKT---QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELK 814
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 815 QEFEEKVVECEVLKEHIRQIDLELKNKQSDMERalLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEi 894
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE- 827
|
170 180
....*....|....*....|..
gi 922582116 895 drlKLDLDAARRNLQklEQMRE 916
Cdd:TIGR02169 828 ---KEYLEKEIQELQ--EQRID 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
625-865 |
6.08e-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: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 625 RNDSEDTVNLTG-----SGDIYIDKESSQKALDDllRKVTLDGGISLKDAKSSEIlAAYERKIQMLQLE----------- 688
Cdd:pfam15921 568 RQQIENMTQLVGqhgrtAGAMQVEKAQLEKEIND--RRLELQEFKILKDKKDAKI-RELEARVSDLELEkvklvnagser 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 689 -LQMKNVPKP----VVEIETTSQKIRDLAQECEALRDSNKQLTDHMtrgNLEINQLKVQL-------EEVKQKCDSIETS 756
Cdd:pfam15921 645 lRAVKDIKQErdqlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM---ETTTNKLKMQLksaqselEQTRNTLKSMEGS 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 757 LGMCITEKAGLKTQLT-----------------ESLQNAERNVHTAQNEISKLNTELAQSVTrielflaenrelkqEFEE 819
Cdd:pfam15921 722 DGHAMKVAMGMQKQITakrgqidalqskiqfleEAMTNANKEKHFLKEEKNKLSQELSTVAT--------------EKNK 787
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 922582116 820 KVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELE 865
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
730-916 |
8.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 730 TRGNLE-----INQLKVQLEEVKQKCdsietslgmcitEKAGLKTQLTESLQNAERNVhtAQNEISKLNTELAQSVTRIE 804
Cdd:COG1196 184 TEENLErlediLGELERQLEPLERQA------------EKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 805 LFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRE 884
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190
....*....|....*....|....*....|..
gi 922582116 885 RDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
670-911 |
1.68e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 670 KSSEILAAYERkiQMLQLELQMKNVPKPVVEIETT-SQKIRDLAQECEALRDSN------------KQLTDHMTRGNLEI 736
Cdd:PRK04778 195 EAREILDQLEE--ELAALEQIMEEIPELLKELQTElPDQLQELKAGYRELVEEGyhldhldiekeiQDLKEQIDENLALL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 737 NQLKvqLEEVKQKCDSIETSLgmcitekaglkTQLTESLqnaERNVHtAQNEISKLNTELAQSVTRIElflAENRELKQE 816
Cdd:PRK04778 273 EELD--LDEAEEKNEEIQERI-----------DQLYDIL---EREVK-ARKYVEKNSDTLPDFLEHAK---EQNKELKEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 817 FEE-----KVVECEVlkEHIRQIDLELKNKQSDMERALLQISA---------AEQKAAKKELELIEaEKHLKLYESRLSD 882
Cdd:PRK04778 333 IDRvkqsyTLNESEL--ESVRQLEKQLESLEKQYDEITERIAEqeiayselqEELEEILKQLEEIE-KEQEKLSEMLQGL 409
|
250 260
....*....|....*....|....*....
gi 922582116 883 RERDLNAKNlEIDRLKLDLDAARRNLQKL 911
Cdd:PRK04778 410 RKDELEARE-KLERYRNKLHEIKRYLEKS 437
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
651-916 |
2.25e-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: 55.12 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 651 LDDLLRKVTLD-----GGISLKDAKSSEIlaaYER------KIQMLQLELQMKNVpkpvvEIETTSQKIRDLAQECEALR 719
Cdd:pfam15921 375 LDDQLQKLLADlhkreKELSLEKEQNKRL---WDRdtgnsiTIDHLRRELDDRNM-----EVQRLEALLKAMKSECQGQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 720 DSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIE---TSLGMCITEKAGLKTQLTESLQNAERNVHTAQNEISKLNtel 796
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVeelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR--- 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 797 aqsvTRIELFLAENRELKQE---FEEKVVECEVLKEHIRQID--LELKNKQ-SDMERALLQ--ISAAEQKAAKKELELIE 868
Cdd:pfam15921 524 ----SRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDkvIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEI 599
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 922582116 869 AEKHLKLYESR-LSDRE----RDLNAK--NLEIDRLKLdLDAARRNLQKLEQMRE 916
Cdd:pfam15921 600 NDRRLELQEFKiLKDKKdakiRELEARvsDLELEKVKL-VNAGSERLRAVKDIKQ 653
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
673-912 |
3.85e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 673 EILAAYERKIQML-QLELQMKNVPKpvveiETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCD 751
Cdd:PRK03918 355 EELEERHELYEEAkAKKEELERLKK-----RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 752 SIETSLGMC------ITE--KAGLKTQLTESLQNAERNVHTAQNEISKLNTELaqsvTRIELFLAENREL---------- 813
Cdd:PRK03918 430 ELKKAKGKCpvcgreLTEehRKELLEEYTAELKRIEKELKEIEEKERKLRKEL----RELEKVLKKESELiklkelaeql 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 814 -----------KQEFEEKVVECEVLKEHIRQIDLELKNKQSDMER-ALLQISAAEQKAAKKELE---------------- 865
Cdd:PRK03918 506 keleeklkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKlEELKKKLAELEKKLDELEeelaellkeleelgfe 585
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 922582116 866 -LIEAEKHLKLYES------RLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLE 912
Cdd:PRK03918 586 sVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
681-913 |
8.04e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 681 KIQMLQLELQMKNvpkpvveIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCdsietslgmc 760
Cdd:TIGR04523 193 KNKLLKLELLLSN-------LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL---------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 761 itekaglkTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEkvvecevlkEHIRQIDLELKN 840
Cdd:TIGR04523 256 --------NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSELKN 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922582116 841 KQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
735-916 |
1.14e-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: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 735 EINQLKVQLEEVKQKCDSIETSLgmciTEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELK 814
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 815 QEFEEKVvecEVLKEHIRQI-------DLELKNKQSDMERAL--LQISAAEQKAAKKELELIEAEKhlklyeSRLSDRER 885
Cdd:COG4942 97 AELEAQK---EELAELLRALyrlgrqpPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADL------AELAALRA 167
|
170 180 190
....*....|....*....|....*....|.
gi 922582116 886 DLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQ 198
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
679-916 |
1.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 679 ERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRD------SNKQLTDHMTrgNLEINQLKVQLEEVKQKCDS 752
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliKLKELAEQLK--ELEEKLKKYNLEELEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 753 IETSLGMCITEKAGLKT---------QLTESLQNAERNVHTAQNEISKLNTELAQ----SVTRIELFLAENREL------ 813
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSlkkelekleELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFyneyle 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 814 ----KQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEaEKHLKLyesrlsdrERDLNA 889
Cdd:PRK03918 607 lkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-EEYLEL--------SRELAG 677
|
250 260
....*....|....*....|....*..
gi 922582116 890 KNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
700-913 |
3.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSlgmcITEKAGLKTQLTESLQNAE 779
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 780 RNVHTAQNEISKLN--------TELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALlq 851
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK-- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582116 852 iSAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:COG3883 171 -AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
597-875 |
4.50e-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: 50.49 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 597 SEMVASCKSTSQPVSLSQKDSSPDFNRCRNDSEDTVNLTGSGDiYIDKESSQKAlDDLlrKVTLDGgiSLKDAKSSEILA 676
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE-SVREEFIQKG-DEV--KCKLDK--SEENARSIEYEV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 677 AYERKiQMLQLELQMKNVPKpvvEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETS 756
Cdd:pfam05483 583 LKKEK-QMKILENKCNNLKK---QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 757 LGMCITEKAGLKTQLTESLQNAERNVhtaqNEISKLNTELAQSVT-RIELFLAENRELKQEFEEKVVEcevlkehiRQID 835
Cdd:pfam05483 659 YQKEIEDKKISEEKLLEEVEKAKAIA----DEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEE--------RDSE 726
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922582116 836 LEL-KNKQSDME--RALLQIS----AAEQKAAKKELElIEAEKHLKL 875
Cdd:pfam05483 727 LGLyKNKEQEQSsaKAALEIElsniKAELLSLKKQLE-IEKEEKEKL 772
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-912 |
5.71e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQKIRDLAQECEALRDSNKQLTDHMTrgnlEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 779
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 780 R-----NVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMER------- 847
Cdd:PRK03918 284 ElkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhel 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582116 848 ----ALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLE 912
Cdd:PRK03918 364 yeeaKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
685-915 |
6.85e-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: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 685 LQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEK 764
Cdd:pfam12128 583 VKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 765 AGLKTQLTESLQNAERnvhTAQNEISKLNTELAQSVTRIELFLA-------ENRELKQEFEEKVVEcevlkehirqidlE 837
Cdd:pfam12128 663 QSEKDKKNKALAERKD---SANERLNSLEAQLKQLDKKHQAWLEeqkeqkrEARTEKQAYWQVVEG-------------A 726
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582116 838 LKNKqsdmERALLQISAAEQKAAKKELELIEAEKHlklyesrlsdreRDLNAKNLEIDRLkLDLDAARRNL-QKLEQMR 915
Cdd:pfam12128 727 LDAQ----LALLKAAIAARRSGAKAELKALETWYK------------RDLASLGVDPDVI-AKLKREIRTLeRKIERIA 788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
675-877 |
9.05e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 675 LAAYERKIQmlQLELQMKNVPKPVVEIEttsQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKcdsie 754
Cdd:COG1579 12 LQELDSELD--RLEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 755 tsLGMCITEKAglktqltesLQNAERNVHTAQNEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQI 834
Cdd:COG1579 82 --LGNVRNNKE---------YEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 922582116 835 DLELKNKQSDMERALLQISAAEQKAAKKelelIEAEkHLKLYE 877
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAK----IPPE-LLALYE 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
767-913 |
2.01e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 767 LKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEkvvecevLKEHIRQIDLELKNKQSDME 846
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-------LEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582116 847 RALLQISAAEQKAAKKELELIEAEKHLKL-------YESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDleqqrkqLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
709-910 |
2.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 709 RDLAQECEALRDSNKQLTDhmTRGNLEINQLKV-QLEEVKQKCDSIETSLgmciTEKAGLKTQLTE-SLQNAERNVHTAQ 786
Cdd:COG4913 221 PDTFEAADALVEHFDDLER--AHEALEDAREQIeLLEPIRELAERYAAAR----ERLAELEYLRAAlRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 787 NEISKLNTELAQSVTRIElflaenrELKQEFEEKVVECEVLKEHIRQIDLElknkqsDMERALLQISAAEQKAAKKELEL 866
Cdd:COG4913 295 AELEELRAELARLEAELE-------RLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 922582116 867 IEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQK 910
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
670-891 |
3.72e-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: 47.43 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 670 KSSEILAAYERKIQMLQLELQMKNVPKPVVE-IETTSQKIRDLAQECEALRDSNKQLTDhmTRGNLEInqLKVQLEEVKQ 748
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnSKSELARIPELEKELERLREHNKHLNE--NIENKLL--LKEEVEDLKR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 749 KCDSIETSLgmciTEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSvTRIELFLAENRELKQefEEKVVECEVLK 828
Cdd:pfam05557 236 KLEREEKYR----EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQQREIVLKE--ENSSLTSSARQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582116 829 EHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELE--LIEAEKHLKLYESRLSDRERDLNAKN 891
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQrrVLLLTKERDGYRAILESYDKELTMSN 373
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
735-914 |
5.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 735 EINQLKVQLEEVKQKCDSIEtSLGMCITEKAGLKTQLTESLQNAER--NVHTAQNEISKLNTELAQSVTRIELFLAENRE 812
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 813 LKQefeekvvecevLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKK-ELELIEAEKHLKLYESRLSDRERDLNAKN 891
Cdd:COG4717 158 LRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 922582116 892 LEIDRLKLDL--DAARRNLQKLEQM 914
Cdd:COG4717 227 EELEQLENELeaAALEERLKEARLL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
734-910 |
6.69e-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: 45.30 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 734 LEINQLKVQLEEVKQKCDSIETslgmcitEKAGLKTQLTEslqnAERNVHTAQNEISKLNTELAQSVTRIElflaenrel 813
Cdd:COG1579 17 SELDRLEHRLKELPAELAELED-------ELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIK--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 814 kqEFEEKVVECEVLKEhirqidleLKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLE 893
Cdd:COG1579 77 --KYEEQLGNVRNNKE--------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
170
....*....|....*..
gi 922582116 894 IDRLKLDLDAARRNLQK 910
Cdd:COG1579 147 LDEELAELEAELEELEA 163
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
730-914 |
7.29e-05 |
|
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: 44.90 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 730 TRGNLE-INQLKVQLEEVKQKCDSIETslGMCITEKAglKTQLTESLQNAERNVHTAQNEI---SKLNTELAQSVTRIel 805
Cdd:pfam13851 21 TRNNLElIKSLKEEIAELKKKEERNEK--LMSEIQQE--NKRLTEPLQKAQEEVEELRKQLenyEKDKQSLKNLKARL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 806 flaenRELKQEFEEKVVECEVLKEHIRQIDLE---LKNKQSDMerallqISAAEQKAAKKELELieaEKHLKLYESRLSD 882
Cdd:pfam13851 95 -----KVLEKELKDLKWEHEVLEQRFEKVERErdeLYDKFEAA------IQDVQQKTGLKNLLL---EKKLQALGETLEK 160
|
170 180 190
....*....|....*....|....*....|..
gi 922582116 883 RERDLNAKnleIDRLKLDLDAARRNLQKLEQM 914
Cdd:pfam13851 161 KEAQLNEV---LAAANLDPDALQAVTEKLEDV 189
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
674-914 |
8.02e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 674 ILAAYERKIQMLQLELQ---------MKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEinqLKVQLE 744
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTaiktseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE---LKKHQE 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 745 EVKQkcdsietslgmCITEKAGLKTQLtESLQNAERNVhtaQNEISKLntelaqsvtrielflaeNRELKQEFEEkvVEC 824
Cdd:pfam05483 521 DIIN-----------CKKQEERMLKQI-ENLEEKEMNL---RDELESV-----------------REEFIQKGDE--VKC 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 825 EVLK--EHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLD 902
Cdd:pfam05483 567 KLDKseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
250
....*....|..
gi 922582116 903 AARrnlQKLEQM 914
Cdd:pfam05483 647 SAK---QKFEEI 655
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
676-915 |
8.18e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 676 AAYERKIQMLQLELQMKNVPK-PVVEIETTS---QKIRDLAQE-CEALRDSNKQLTDHMTRGNLEInqLKVQLEEVKQKC 750
Cdd:COG3206 114 ASREAAIERLRKNLTVEPVKGsNVIEISYTSpdpELAAAVANAlAEAYLEQNLELRREEARKALEF--LEEQLPELRKEL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 751 DSIETSL-------GmcITEKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELK-----QEFE 818
Cdd:COG3206 192 EEAEAALeefrqknG--LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviQQLR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 819 EKVVECEVLKEHIRQIDLE-------LKNKQSDMERALLQISAAEQKAAKKELELIEA-EKHLKLYESRLSDRERDLNAK 890
Cdd:COG3206 270 AQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQArEASLQAQLAQLEARLAELPEL 349
|
250 260
....*....|....*....|....*....
gi 922582116 891 NLEIDRLKLDLDAARRN----LQKLEQMR 915
Cdd:COG3206 350 EAELRRLEREVEVARELyeslLQRLEEAR 378
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
770-916 |
1.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 770 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERAL 849
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582116 850 LQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLD--LDAARRNLQKLEQMRE 916
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKEEELAE 204
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
670-911 |
1.08e-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: 46.00 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 670 KSSEILAAYERkiQMLQLELQMKNVPKPVVEIETT-SQKIRDLAQECEALRDSNKQLTDHmtrgNL--EINQLKVQLEEV 746
Cdd:pfam06160 176 EAREVLEKLEE--ETDALEELMEDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHL----NVdkEIQQLEEQLEEN 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 747 KQ-----KCDSIETSLGMcITEKaglKTQLTESLqnaERNVHtAQNEISKLNTELAQSVTRIElflAENRELKQEFEEkV 821
Cdd:pfam06160 250 LAllenlELDEAEEALEE-IEER---IDQLYDLL---EKEVD-AKKYVEKNLPEIEDYLEHAE---EQNKELKEELER-V 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 822 VECEVLKEH----IRQIDLELKNKQSDMERALLQISAAEQ---------KAAKKELELIEaEKHLKLYESRLSDRERDLN 888
Cdd:pfam06160 318 QQSYTLNENelerVRGLEKQLEELEKRYDEIVERLEEKEVayselqeelEEILEQLEEIE-EEQEEFKESLQSLRKDELE 396
|
250 260
....*....|....*....|...
gi 922582116 889 AKNlEIDRLKLDLDAARRNLQKL 911
Cdd:pfam06160 397 ARE-KLDEFKLELREIKRLVEKS 418
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
694-916 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 694 VPKPVV---EIETTSQKIRDLAQECEAlrdSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQ 770
Cdd:pfam07888 26 VPRAELlqnRLEECLQERAELLQAQEA---ANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 771 LTEslqnAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQsdmerall 850
Cdd:pfam07888 103 YKE----LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE-------- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922582116 851 qisaAEQKAAKKELELIEAEKH---LKLYESRLSDRERDLNAKNL--EIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:pfam07888 171 ----AERKQLQAKLQQTEEELRslsKEFQELRNSLAQRDTQVLQLqdTITTLTQKLTTAHRKEAENEALLE 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
771-904 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 771 LTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFlaeNRELKQEFEEKVVEcevlkEHIRQIDlELKNKQSDMERALL 850
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL---QRLAEYSWDEIDVA-----SAEREIA-ELEAELERLDASSD 685
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 922582116 851 QISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAA 904
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
681-916 |
1.93e-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: 45.48 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 681 KIQMLQLELQM------KNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIE 754
Cdd:pfam05483 223 KIQHLEEEYKKeindkeKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 755 TSLGMCITEKAGLKT----------QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLaenRELKQEFEEKvvec 824
Cdd:pfam05483 303 MSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKN---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 825 evlKEHIRQIDLELKNKQSDMERalLQISAAEQKAAKKELELIEAEKHLKLYESRlsdrerdlnaknlEIDRLKLDLDAA 904
Cdd:pfam05483 376 ---EDQLKIITMELQKKSSELEE--MTKFKNNKEVELEELKKILAEDEKLLDEKK-------------QFEKIAEELKGK 437
|
250
....*....|..
gi 922582116 905 RRNLQKLEQMRE 916
Cdd:pfam05483 438 EQELIFLLQARE 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
675-907 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 675 LAAYERKIQMLQLEL--------QMKNVPKPVVEIETTSQKIR-------DLAQECEALRDSNKQLtDHMTRGNLEINQL 739
Cdd:COG4913 612 LAALEAELAELEEELaeaeerleALEAELDALQERREALQRLAeyswdeiDVASAEREIAELEAEL-ERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 740 KVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTEslqnAERNVHTAQNEISklntELAQSVTRIELFLAENR---ELKQE 816
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLE----AAEDLARLELRALLEERfaaALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 817 FEEKVVecEVLKEHIRQIDLELKNKQSDMERAL-------------LQISAAEQKAAKKELELIEAEkHLKLYESRLSDR 883
Cdd:COG4913 763 VERELR--ENLEERIDALRARLNRAEEELERAMrafnrewpaetadLDADLESLPEYLALLDRLEED-GLPEYEERFKEL 839
|
250 260
....*....|....*....|....*
gi 922582116 884 erdLNAKNLE-IDRLKLDLDAARRN 907
Cdd:COG4913 840 ---LNENSIEfVADLLSKLRRAIRE 861
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-905 |
2.46e-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: 45.01 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 679 ERKIQMLQLELQM--KNVPKPVVEIETTSQKIRDLAQE----------CEALRDSNKQLTDHMTRgnlEINQLKVQLEEV 746
Cdd:TIGR04523 411 DEQIKKLQQEKELleKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRESLETQLKVLSR---SINKIKQNLEQK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 747 KQKCDSIETSLGMCITEKaglkTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRI----ELFLAENRELKQEFEEKVV 822
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEK----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNKDDFELKKENLEKEI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 823 -----ECEVLKEHI-------RQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAK 890
Cdd:TIGR04523 564 deknkEIEELKQTQkslkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
250
....*....|....*
gi 922582116 891 NLEIDRLKLDLDAAR 905
Cdd:TIGR04523 644 KQEVKQIKETIKEIR 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
808-911 |
2.57e-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: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 808 AENRELKQEFEEkvvecevLKEHIRQIDLELKNKQSDMERALLQISAAEQKaakkeleLIEAEKHLKLYESRLSDRERDL 887
Cdd:COG4942 20 DAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 922582116 888 NAKNLEIDRLKLDLDAARRNLQKL 911
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL 109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
788-913 |
3.25e-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: 43.37 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 788 EISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDME--RALLQISAAEQKAAK--KE 863
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEevEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 922582116 864 LELIEAE-KHLKLYESRLSDRERDLNAknlEIDRLKLDLDAARRNLQKLEQ 913
Cdd:COG1579 91 YEALQKEiESLKRRISDLEDEILELME---RIEELEEELAELEAELAELEA 138
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
707-898 |
3.92e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 707 KIRDLAQE---CEALRDSNKQLTDhmTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAgLKTQLTESLQNAERNVH 783
Cdd:PHA02562 175 KIRELNQQiqtLDMKIDHIQQQIK--TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKA-EIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 784 TAQNEISKLNTELAQSVTRIELFlaeNRELKqeFEEKVVECEVLKEHIRQID---LELKNKQSDMERALLQISAAEQKAA 860
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQF---QKVIK--MYEKGGVCPTCTQQISEGPdriTKIKDKLKELQHSLEKLDTAIDELE 326
|
170 180 190
....*....|....*....|....*....|....*...
gi 922582116 861 KKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLK 898
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK 364
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
670-915 |
4.43e-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: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 670 KSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKirDLAQECEALRD-----SNKQLTDHMTRGNLEINQLKVQLE 744
Cdd:pfam17380 331 RQAAIYAEQERMAMERERELERIRQEERKRELERIRQE--EIAMEISRMRElerlqMERQQKNERVRQELEAARKVKILE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 745 EVKQKcdsietslgmcitekaGLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIelflaenRELKQEFEEKVvec 824
Cdd:pfam17380 409 EERQR----------------KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV-------RLEEQERQQQV--- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 825 evlkEHIRQIDLELKNKQSDMERALLQISAAEQ---KAAKKELE-----LIEAEKHLKLYESRLSDRERDL----NAKNL 892
Cdd:pfam17380 463 ----ERLRQQEEERKRKKLELEKEKRDRKRAEEqrrKILEKELEerkqaMIEEERKRKLLEKEMEERQKAIyeeeRRREA 538
|
250 260
....*....|....*....|...
gi 922582116 893 EIDRLKLDLDAARRNLQklEQMR 915
Cdd:pfam17380 539 EEERRKQQEMEERRRIQ--EQMR 559
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
681-911 |
7.63e-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: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 681 KIQMLQLELQMKNVPKPVVEIEttsQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSlgmc 760
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT---- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 761 itekaglKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKN 840
Cdd:TIGR04523 463 -------RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582116 841 KqsdmerallqisaaEQKAAKKELELIEAEKHLKlyesrLSDRERDLNAKNLEIDRLKLD---LDAARRNLQKL 911
Cdd:TIGR04523 536 K--------------ESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTqksLKKKQEEKQEL 590
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
787-916 |
9.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 787 NEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAakKELEL 866
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKE 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 922582116 867 IE--AEKHLKLYE--SRLSDRERDLnakNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:PRK03918 288 LKekAEEYIKLSEfyEEYLDELREI---EKRLSRLEEEINGIEERIKELEEKEE 338
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
649-913 |
9.39e-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: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 649 KALDDLLRKVTLDGGISLKDAKSSEILAAYERKIQMlqlelqmknvPKPVVEIETTSQKIRDLAqecealrdsnkqltdh 728
Cdd:pfam09731 189 EALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKL----------PEHLDNVEEKVEKAQSLA---------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 729 mtrgnLEINQLKVQLEE----VKQKCDSIETSLGMCITEKAGLKTQLTESLqnaernVHTAQNEISKLNTELAQSVTRIE 804
Cdd:pfam09731 243 -----KLVDQYKELVASerivFQQELVSIFPDIIPVLKEDNLLSNDDLNSL------IAHAHREIDQLSKKLAELKKREE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 805 LFLAENRElKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIE--AEKHLK--LYESRL 880
Cdd:pfam09731 312 KHIERALE-KQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAeaHEEHLKdvLVEQEI 390
|
250 260 270
....*....|....*....|....*....|....*..
gi 922582116 881 S-DRE--RDLNAKNL-EIDRLKLDLDAARRNLQKLEQ 913
Cdd:pfam09731 391 ElQREflQDIKEKVEeERAGRLLKLNELLANLKGLEK 427
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
768-916 |
1.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 768 KTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEF----------EEKVVEC-EVLKEHIRQI-- 834
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqaeiaeaEAEIEERrEELGERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 835 ----------------------DLELKNKQSDMERALL-QISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKN 891
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldRLSALSKIADADADLLeELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....*
gi 922582116 892 LEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-915 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQK------IRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLeeVKQKCDSIETSLgmcitekaglkTQLTE 773
Cdd:COG4913 243 ALEDAREQiellepIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAEL-----------ARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 774 SLQNAERNVHTAQNEISKLNTELAQS-VTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQI 852
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582116 853 sAAEQKAAKKELELIEAEKHlklyesRLSDRERDLNAknleidrlkldldaARRNLQK-LEQMR 915
Cdd:COG4913 390 -AALLEALEEELEALEEALA------EAEAALRDLRR--------------ELRELEAeIASLE 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
681-915 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 681 KIQMLQLELQmkNVPKPVVEIETTSQKI-RDLAQECEALRDSNKQLTDHmTRGNLEINQLKVQLEEvkqkcdsietslgm 759
Cdd:pfam01576 434 KLSKLQSELE--SVSSLLNEAEGKNIKLsKDVSSLESQLQDTQELLQEE-TRQKLNLSTRLRQLED-------------- 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 760 citEKAGLKTQL---TESLQNAERNVHTAQNEISKLNTELAQSVTRIEL-------FLAENRELKQEFEEKVVECEVLK- 828
Cdd:pfam01576 497 ---ERNSLQEQLeeeEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAleegkkrLQRELEALTQQLEEKAAAYDKLEk 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 829 ----------------EHIRQIDLELKNKQSDMERALLQ---ISA--------AEQKAAKKELELIEAEKHLKLYESRLS 881
Cdd:pfam01576 574 tknrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLAEekaISAryaeerdrAEAEAREKETRALSLARALEEALEAKE 653
|
250 260 270
....*....|....*....|....*....|....
gi 922582116 882 DRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMR 915
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
670-916 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 670 KSSEILAAYERKIQMLQ-LELQMKNVPKPVVEIETT----SQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLE 744
Cdd:PRK02224 238 EADEVLEEHEERREELEtLEAEIEDLRETIAETEREreelAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 745 EVKQKCDSIETSLGMCitekaglKTQLTESLQNAERnvhtaqneisklnteLAQSVTRIELFLAENRELKQEFEEKVVEC 824
Cdd:PRK02224 318 ELEDRDEELRDRLEEC-------RVAAQAHNEEAES---------------LREDADDLEERAEELREEAAELESELEEA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 825 EVLKEhirqidlELKNKQSDMERallQISAAEQKAAKKELELIEAEKHLKLYESRLSD-RERdlnaknleIDRLKLDLDA 903
Cdd:PRK02224 376 REAVE-------DRREEIEELEE---EIEELRERFGDAPVDLGNAEDFLEELREERDElRER--------EAELEATLRT 437
|
250
....*....|...
gi 922582116 904 ARRNLQKLEQMRE 916
Cdd:PRK02224 438 ARERVEEAEALLE 450
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
649-909 |
1.75e-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: 42.34 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 649 KALDDLlRKVTLDGGISLKDAKSSEIL------AAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSN 722
Cdd:TIGR00606 186 KALETL-RQVRQTQGQKVQEHQMELKYlkqykeKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 723 KQLTDHMT---RGNLEINQLKVQLEEVKQKCdsietslgmciteKAGLKTQLTESLQNAERNVHTAQNEISKLNTELAQS 799
Cdd:TIGR00606 265 MKLDNEIKalkSRKKQMEKDNSELELKMEKV-------------FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 800 VTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIE--AEKHLKLYE 877
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIerQEDEAKTAA 411
|
250 260 270
....*....|....*....|....*....|..
gi 922582116 878 SRLSDRERDLNAKNLEIDRLKLDLDAARRNLQ 909
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIE 443
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
661-914 |
1.87e-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: 41.80 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 661 DGGISLKDAKSSEILAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQltdhmtrgnlEINQLK 740
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA----------ERKQLQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 741 VQLEEVKQKCDSIETSLgmcitekaglkTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRI---ELFLAENRELKQEF 817
Cdd:pfam07888 178 AKLQQTEEELRSLSKEF-----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 818 EEKVVECEVLKEHIRQIDLELKNKQSDMERALLQisaaeqkAAKKELELIEAEKHLKLYESRLSdRERDLNAKNLEIDRL 897
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAELHQARLQ-------AAQLTLQLADASLALREGRARWA-QERETLQQSAEADKD 318
|
250
....*....|....*...
gi 922582116 898 KLD-LDAArrnLQKLEQM 914
Cdd:pfam07888 319 RIEkLSAE---LQRLEER 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
809-916 |
2.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 809 ENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERD-- 886
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 922582116 887 ------------LNAKNLE--IDRLKLDLDAARRNLQKLEQMRE 916
Cdd:COG3883 97 rsggsvsyldvlLGSESFSdfLDRLSALSKIADADADLLEELKA 140
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
790-913 |
2.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 790 SKLNTELAQSVTRIELFLAE-NRELKQEFEEKVVEcevLKEhirqidlELKNKQSDMERallQISAAEQKAAKKELELIE 868
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLE---AKE-------EIHKLRNEFEK---ELRERRNELQKLEKRLLQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 922582116 869 AEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
567-914 |
2.38e-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: 42.03 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 567 ISYGDQETVQQAFLTYSHcaQVPAFPSHL-------------LSEMVASCKSTSQPVSLsQKDSSPDFNR--------CR 625
Cdd:pfam15921 68 IAYPGKEHIERVLEEYSH--QVKDLQRRLnesnelhekqkfyLRQSVIDLQTKLQEMQM-ERDAMADIRRresqsqedLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 626 NDSEDTVN-LTGSGDIYIDKESSQKALDDLLRKVTLDGGISLKDAKSseILAAYE----RKI--QMLQLELQMKNVPKPV 698
Cdd:pfam15921 145 NQLQNTVHeLEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRS--ILVDFEeasgKKIyeHDSMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 699 veiettSQKIRDLAQECEALRDSNKQLTDHMTRGNLEiNQLKVQLEeVKQKCDSIETSLG------MCITEKAGLKTQLT 772
Cdd:pfam15921 223 ------SKILRELDTEISYLKGRIFPVEDQLEALKSE-SQNKIELL-LQQHQDRIEQLISeheveiTGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 773 ESLQNAERNVH-TAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVEcevLKEHIRQIDLELKNKQSDMERALLQ 851
Cdd:pfam15921 295 NSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922582116 852 ISAAEQKAAKKELELIEAEKHLKLYES---RLSDRErdlNAKNLEIDRLKLDLDAARRNLQKLEQM 914
Cdd:pfam15921 372 SGNLDDQLQKLLADLHKREKELSLEKEqnkRLWDRD---TGNSITIDHLRRELDDRNMEVQRLEAL 434
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
668-911 |
2.58e-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: 41.48 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 668 DAKSSEILAAYERKIQMLQ-------LELQMKNVPKPVVE-IETTSQKIRDLAQECEALRD--SNKQLTDHMTRGNLEIN 737
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAaaeaeqeLEESKRETETGIQNlTAEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 738 QLKVQLEEVKQKCDSIETSlgmcitekagLKTQLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEF 817
Cdd:COG5185 381 SFKDTIESTKESLDEIPQN----------QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISEL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 818 EEKVVECEV-----LKEHIRQIDLELKNKQSDMERALLQIsAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNL 892
Cdd:COG5185 451 NKVMREADEesqsrLEEAYDEINRSVRSKKEDLNEELTQI-ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF 529
|
250
....*....|....*....
gi 922582116 893 EIDRlKLDLDAARRNLQKL 911
Cdd:COG5185 530 MRAR-GYAHILALENLIPA 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
773-898 |
2.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 773 ESLQNAERNvhtaqneISKLNTELAQSVTRIELFLA-----ENR--ELKQEFEEKVVECEVLKEHIRQIDLELKNkqsdM 845
Cdd:PRK03918 158 DDYENAYKN-------LGEVIKEIKRRIERLEKFIKrteniEELikEKEKELEEVLREINEISSELPELREELEK----L 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 922582116 846 ERALLQISAAEQKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLK 898
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
675-913 |
2.91e-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: 40.95 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 675 LAAYERKIQMLQLELQMKNVPKPVVEIETTSQKIRDLAQEcealrdsnkqltdhmtRGNLE--INQLKVQLEEVKQKcds 752
Cdd:pfam15905 49 TPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQE----------------RGEQDkrLQALEEELEKVEAK--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 753 ietsLGMCITEKaglkTQLTESLQNAERNVH--TAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEh 830
Cdd:pfam15905 110 ----LNAAVREK----TSLSASVASLEKQLLelTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 831 irQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEAEKH---LKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRN 907
Cdd:pfam15905 181 --GMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSEtekLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDE 258
|
....*.
gi 922582116 908 LQKLEQ 913
Cdd:pfam15905 259 IESLKQ 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-867 |
3.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 686 QLELQMKNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRgnLEInqlKVQLEEVKQKCDSIETSLGMCITEKA 765
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEK---LLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 766 GLKTQLTEsLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAEN-RELKQEFEEKVVECEVLKEHIRQIDLELKNKQSD 844
Cdd:COG4717 150 ELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|...
gi 922582116 845 MERALLQISAAEQKAAKKELELI 867
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLL 251
|
|
| BAR |
smart00721 |
BAR domain; |
768-916 |
3.52e-03 |
|
BAR domain;
Pssm-ID: 214787 [Multi-domain] Cd Length: 239 Bit Score: 40.06 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 768 KTQLTESLQNAERNVHTAQNEISKLntelaqsVTRIELFLAENRELKQEFEEKVVECEVLKE-HIRQIDLELKNKQSDME 846
Cdd:smart00721 22 KTKLDEDFEELERRFDTTEAEIEKL-------QKDTKLYLQPNPAVRAKLASQKKLSKSLGEvYEGGDDGEGLGADSSYG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582116 847 RALLQISAAEQKAAKKELELIEAEKH-----LKLYESRLSDrerdLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:smart00721 95 KALDKLGEALKKLLQVEESLSQVKRTfilplLNFLLGEFKE----IKKARKKLERKLLDYDSARHKLKKAKKSKE 165
|
|
| BAR |
pfam03114 |
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ... |
768-916 |
4.21e-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: 40.01 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 768 KTQLTESLQNAERNVHTAQNEISKLntelaqsVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMEr 847
Cdd:pfam03114 21 KTKLDEDFEELERRFDTTEKEIKKL-------QKDTKGYLQPNPGARAKQTVLEQPEELLAESMIEAGKDLGEDSSFGK- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 848 ALLQISAAEQKAAKKELEL-IEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:pfam03114 93 ALEDYGEALKRLAQLLEQLdDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKS 162
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
648-916 |
4.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 648 QKALDDLL--------RKVTLDGGISLKDAKSseilaayERKIQMLQLELQM-----KNVPKPVVEIETTSQKIRDLAQE 714
Cdd:PRK02224 152 QDMIDDLLqlgkleeyRERASDARLGVERVLS-------DQRGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 715 CEALRDSNKQltdhmTRGNL-----EINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQlteslqnaernVHTAQNEI 789
Cdd:PRK02224 225 YEEQREQARE-----TRDEAdevleEHEERREELETLEAEIEDLRETIAETEREREELAEE-----------VRDLRERL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 790 SKLNTELAQSVTRIELFLAENRELKQEFEEKVVECEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIEA 869
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922582116 870 EKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
771-916 |
4.70e-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: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 771 LTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKvvecevlKEHIRQIDLELKnkqsdmerall 850
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-------DERIERLERELS----------- 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922582116 851 qisaaeqKAAKKELELIEAEKHLKLYESRLSDRERDLNAKNLEIDRLKLDLDAARRnLQKLEQMRE 916
Cdd:COG2433 452 -------EARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGE 509
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
700-904 |
4.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 700 EIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE 779
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 780 RnvhtAQNEISKLNTELAQSVTRIElflaENRELKQefEEKVVECEVLKE---HIRQIDlELKNKQSDMERALLQIsAAE 856
Cdd:PRK02224 423 E----LREREAELEATLRTARERVE----EAEALLE--AGKCPECGQPVEgspHVETIE-EDRERVEELEAELEDL-EEE 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922582116 857 QKAAKKELE----LIEAEKHL-------KLYESRLSDRERDLNAKNLEIDRL---KLDLDAA 904
Cdd:PRK02224 491 VEEVEERLEraedLVEAEDRIerleerrEDLEELIAERRETIEEKRERAEELrerAAELEAE 552
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
770-877 |
4.95e-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: 40.93 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 770 QLTESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENR-------ELKQEFEEKVVECEVLKEHIRQidLELKNKQ 842
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRrleariaQLEEELEEEQSNTELLNDRLRK--STLQVEQ 921
|
90 100 110
....*....|....*....|....*....|....*
gi 922582116 843 SDMERALLQISAAEQKAAKKELELIEAEKHLKLYE 877
Cdd:pfam01576 922 LTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-916 |
6.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 692 KNVPKPVVEIETTSQKIRDLAQECEALRDSNKQLTDHMTRGNLEINQLKVQLEEVKQKCDSIEtslgmciTEKAGLKtQL 771
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-------KEVKELE-EL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 772 TESLQNAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQ------EFEEKVVECEVLKE-------HIRQIDLEL 838
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEfyeeyldELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 839 KNKQSDMERALLQISAAEQKAAKKElELIEAEKHLKLYESRLSDRER---DLNAKNLEIDRLK-----LDLDAARRNLQK 910
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHElyeEAKAKKEELERLKkrltgLTPEKLEKELEE 395
|
....*.
gi 922582116 911 LEQMRE 916
Cdd:PRK03918 396 LEKAKE 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
731-916 |
7.29e-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: 40.34 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 731 RGNLEINQLKVQLEE--VKQKCDSIETSLGMCITEKAGLKTQLTESLQNAE--RNVHTAQNEISKLNTELAQSVTRIELF 806
Cdd:TIGR00618 193 HGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAylTQKREAQEEQLKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 807 LAENRELKQEFEEKVVECEVLK-----EHIRQIDLELKNKQSDM---ERALLQISAAEQKAAKKELELIEAEKHLKLYES 878
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAAPlaahiKAVTQIEQQAQRIHTELqskMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190
....*....|....*....|....*....|....*...
gi 922582116 879 RlSDRERDLNAKNLEIDRLKLDLDAARRNLQKLEQMRE 916
Cdd:TIGR00618 353 Q-EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
701-911 |
7.33e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 701 IETTSQKIRDLAQECEALRDSNKQLTDhmtrgnlEINQLKVQLEEVKQKCDSIETSLGMCIT--EK--AGLKTQLTESLQ 776
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNRE-------EVEQLKDLYRELRKSLLANRFSFGPALDelEKqlENLEEEFSQFVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 777 -NAERNVHTAQNEISKLNTELAQSVTRIELFLAENRELKQEFEEKVVEcevLKEHIRQ------------IDLELKNKQS 843
Cdd:PRK04778 187 lTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQE---LKAGYRElveegyhldhldIEKEIQDLKE 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922582116 844 DMERALLQISAAEQKAAKKELELIEAEKHlKLYESrlsdRERDLNAKN---LEIDRLKLDLDAARRNLQKL 911
Cdd:PRK04778 264 QIDENLALLEELDLDEAEEKNEEIQERID-QLYDI----LEREVKARKyveKNSDTLPDFLEHAKEQNKEL 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
666-913 |
7.42e-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: 40.00 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 666 LKDAKSS--EILAAYERKIQML-QLELQMKNVPKPVVEIETtsqKIRDLAQECEAlrDSNKQLTDHMTRGNLEINQLKVQ 742
Cdd:TIGR04523 255 LNQLKDEqnKIKKQLSEKQKELeQNNKKIKELEKQLNQLKS---EISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 743 LEEVKQKCDSIETSLGMCITEKAGLKT---QLTESLQNAERNVHTAQNEISKLNTE---LAQSVTRIELFLAENRELKQE 816
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESensEKQRELEEKQNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582116 817 FEEKVvecEVLKEHIRQIDLELKNKQSDMERALLQISAAEQKAAKKELELIE-------AEKHLKLYESRLSDRERDLNA 889
Cdd:TIGR04523 410 KDEQI---KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntresLETQLKVLSRSINKIKQNLEQ 486
|
250 260
....*....|....*....|....
gi 922582116 890 KNLEIDRLKLDLDAARRNLQKLEQ 913
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEE 510
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