|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
193-286 |
9.20e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 102.27 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 193 AVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPACAAGSEGVTGW 272
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 961710479 273 TQSPDSILVYEVEM 286
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
184-285 |
1.03e-22 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 93.71 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 184 QDLVVVEGPAVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPACA 263
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|..
gi 961710479 264 AGSEGVTGwTQSPDSILVYEVE 285
Cdd:COG0545 80 YGERGAGG-VIPPNSTLVFEVE 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
566-862 |
1.29e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQR---IIQE-NERLKQeiLEKSSRIEEQNDKISEliERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEK 638
Cdd:COG1196 187 NLERledILGElERQLEP--LERQAEKAERYRELKE--ELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 639 AKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQL 718
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 719 ELKVTSLEEELADLRAEKESLEKNLSERKKKSAQErcraEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQT 798
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710479 799 QWEAKCEHLLASAKDEHLLQYQEvcAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLE 862
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
567-873 |
2.18e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 727 EELADLRAEKESLEKNLSERkkksAQERCRAEEEIDEIrksyQEELDKLRQLLKKARVSTDQAAAEQAELQTQweakcEH 806
Cdd:COG1196 393 RAAAELAAQLEELEEAEEAL----LERLERLEEELEEL----EEALAELEEEEEEEEEALEEAAEEEAELEEE-----EE 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 807 LLASAKDEHLLQYQEVCAQRDASQQELLRLQEKcLALQAQVTALTEQNEQHTKDLENKSHMSGVAAA 873
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-864 |
5.52e-17 |
|
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: 87.03 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 578 KQEILEKSSRIEEQNDKISEL-IERNQRYVEQSNLMME-----KRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEEleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 652 VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD 731
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 732 LRAEKESLE---KNLSERKKKSAQERCRAEEEIDEIR---KSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKcE 805
Cdd:TIGR02168 836 TERRLEDLEeqiEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSEELRELESKRSEL-R 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 806 HLLaSAKDEHLLQYQEVCA---QRDASQQELLR-----LQEKCLALQAQVTALTEQNEQHTKDLENK 864
Cdd:TIGR02168 915 REL-EELREKLAQLELRLEgleVRIDNLQERLSeeyslTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
572-861 |
1.08e-16 |
|
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: 85.88 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QEN-ERLkQEILEKssrIEEQNDKISELIERNQRYVEQSNlmmEKRN----------NSLQTATENTQARVLHAEQEKAK 640
Cdd:TIGR02168 185 RENlDRL-EDILNE---LERQLKSLERQAEKAERYKELKA---ELRElelallvlrlEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 641 VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKESLEKNLSERKKKsAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQW 800
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAE-LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710479 801 EAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDL 861
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
569-838 |
2.51e-16 |
|
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: 84.73 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 569 RIIQENERLKQEILEKSSRIEEQNDKISELIERNQryveqsnlMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAA 648
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 649 TAQVSRLQLKVTAHQKKEAELQMQLTESL------------KETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRR 716
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 717 QLELKVTSLEEELADLRAEKESLE----------KNLSERKKKSAQERCRAEEEIDEIRKSYQE---ELDKLRQLLKKAR 783
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSELK 923
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 784 VstdqAAAEQAELQTQWEAKCEHLLASAkdEHLLQYQEVCAQRDASQQELLRLQE 838
Cdd:TIGR02169 924 A----KLEALEEELSEIEDPKGEDEEIP--EEELSLEDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
566-854 |
3.45e-16 |
|
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: 84.34 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 645
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 726 EEELADLRAEKESLEKNLSE----RKKKSAQ------ERCRAEEEIDEIRKSYQ---EELDKLRQLLKKARVSTDQAAAE 792
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEelsEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 793 QAELQTQW---EAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQN 854
Cdd:TIGR02168 924 LAQLELRLeglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-797 |
2.33e-15 |
|
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: 81.64 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL--------QKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAEL-------SELQETSEQAQSKFKSEKQSRRQLE 719
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 720 LKVTSLEEELADL-------RAEKESLEKNLSERKKKSAQERC----RAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQ 788
Cdd:TIGR02168 400 NEIERLEARLERLedrrerlQQEIEELLKKLEEAELKELQAELeeleEELEELQEELERLEEALEELREELEEAEQALDA 479
|
....*....
gi 961710479 789 AAAEQAELQ 797
Cdd:TIGR02168 480 AERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
573-853 |
2.87e-15 |
|
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: 81.27 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSN-------LMMEKRN----------NSLQTATENTQARVLHAE 635
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREyegyellkekEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 636 QEKAKVTEE--------------LTAATAQVS--------RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAE 693
Cdd:TIGR02169 251 EELEKLTEEiselekrleeieqlLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 694 LSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAE---EEIDEIRKSY-- 768
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkREINELKRELdr 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 769 -QEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLlasAKDEHLLqyQEVCAQRDASQQELLRLQEKCLALQAQV 847
Cdd:TIGR02169 411 lQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL--EQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
....*.
gi 961710479 848 TALTEQ 853
Cdd:TIGR02169 486 SKLQRE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
571-832 |
5.44e-14 |
|
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: 77.03 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARV------LHAEQEKAKVT-- 642
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeLEAEIASLERSia 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 ---EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQsrrqle 719
Cdd:TIGR02169 312 ekeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 720 lKVTSLEEELADLRAEKESLEKNLS---ERKKKSAQERCRAEEEIDEIR---KSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:TIGR02169 386 -ELKDYREKLEKLKREINELKRELDrlqEELQRLSEELADLNAAIAGIEakiNELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 961710479 794 AELQTQWEAKCEHLLASAKDEHLLQ--YQEVCAQRDASQQE 832
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQreLAEAEAQARASEER 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
565-818 |
7.97e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 565 GNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRyveqsnlmmekrnnslqtatenTQARVLHAEQEKAKVTEE 644
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE----------------------LEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 645 LTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 725 LEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAeQAELQTQWEAKC 804
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAA-RLLLLLEAEADY 503
|
250
....*....|....
gi 961710479 805 EHLLASAKDEHLLQ 818
Cdd:COG1196 504 EGFLEGVKAALLLA 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-900 |
1.31e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 623 ATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE 702
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 703 QAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKK--SAQERCRA-EEEIDEIRKSYQEELDKLRQLL 779
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieQLKEELKAlREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 780 KKARVSTDQAAAEQAELQT---QWEAKCEHLLASAK---------DEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQV 847
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDleeQIEELSEDIESLAAeieeleeliEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 961710479 848 TALTEQNEQHTKDLENKSHMsgVAAAATDpSEKVKKIMNQVFQSLRGEFELEE 900
Cdd:TIGR02168 904 RELESKRSELRRELEELREK--LAQLELR-LEGLEVRIDNLQERLSEEYSLTL 953
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
673-875 |
1.56e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 673 LTESLKE--TDLLKGQLIKLQAELSELQETSEQAQSKfKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSE-RKKK 749
Cdd:COG4717 47 LLERLEKeaDELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 750 SAQERCRAEEEIDEIRKSYQEELDKLR---QLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDE---HLLQYQEVC 823
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 961710479 824 AQRDASQQELLRLQEKCLALQAQVTALtEQNEQHTKDLENKSHMSGVAAAAT 875
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-861 |
3.12e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 626 NTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQM-------------------QLTESLKETDLLKGQ 686
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaereiaELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 687 LIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRA---EEEIDE 763
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 764 IRKSYQEELDKLRQLLKKARvstDQAAAEQAELQTQWEAKCEHLLASAKDEHllQYQEVCAQRDASqqELLRLQEKCLAL 843
Cdd:COG4913 767 LRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLP--EYLALLDRLEED--GLPEYEERFKEL 839
|
250
....*....|....*...
gi 961710479 844 qaqvtaLTEQNEQHTKDL 861
Cdd:COG4913 840 ------LNENSIEFVADL 851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-741 |
6.35e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 517 TEIRMAVSKVADKMDHLMTKVEELQKhsagnslllpsmsvtmETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKIS 596
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 597 ELIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQ 656
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 657 LKVTAHQKKEAELQMQLTEslKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEK 736
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
....*
gi 961710479 737 ESLEK 741
Cdd:TIGR02168 492 DSLER 496
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
509-930 |
9.19e-12 |
|
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: 69.75 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMET--SMIMGNIQRIIQENERLK---QEILE 583
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 584 KSSRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELTAATAQVSRLQLKV 659
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 660 TA-------HQKKEAELQMQL-TESLKETDLlKGQLIKLQAELSEL-QETSE-------QAQSKFKSEKQSRRQLElKVT 723
Cdd:pfam05483 460 TAiktseehYLKEVEDLKTELeKEKLKNIEL-TAHCDKLLLENKELtQEASDmtlelkkHQEDIINCKKQEERMLK-QIE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 724 SLEEELADLRAEKESLEKNLSER------KKKSAQERCRA---------------EEEIDEIRKSYQEELDKLRQLLKKA 782
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKgdevkcKLDKSEENARSieyevlkkekqmkilENKCNNLKKQIENKNKNIEELHQEN 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 783 RVSTDQAAAEQAELQTqWEAKCEHL---LASAK---DEHLLQYQEVCAQRDASQQELLRLQEKclalqAQVTALTEQNEQ 856
Cdd:pfam05483 618 KALKKKGSAENKQLNA-YEIKVNKLeleLASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEK-----AKAIADEAVKLQ 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 857 HTKDLENKSHMSGVAAAAtdpsEKVKKIMNQVFQSLRGEFEL-----EESYNGRAVLGTIMNTIKMVTLQLLNQHEQDK 930
Cdd:pfam05483 692 KEIDKRCQHKIAEMVALM----EKHKHQYDKIIEERDSELGLyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
508-798 |
4.62e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 508 LMTEARQHNTEIRMaVSKVADKMDHLMTKVEELQKhsagnslllpsmsvtmETSMIMGNIQRI---IQENERLKQEILEK 584
Cdd:PRK03918 212 ISSELPELREELEK-LEKEVKELEELKEEIEELEK----------------ELESLEGSKRKLeekIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 585 SSRIEEQNDKISELIERNQRYVEQSNLM---------MEKRNNSLQTATENTQARVLHAEQEKAKVtEELTaataqvsrl 655
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEERIKELEEKEERL-EELK--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 qlkvtahqKKEAELQ---MQLTESLKETDL---LKGQLIKLQAELSELqeTSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:PRK03918 345 --------KKLKELEkrlEELEERHELYEEakaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 730 ADLRAEKESLEKNLSERKKksAQERCR------AEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQT 798
Cdd:PRK03918 415 GELKKEIKELKKAIEELKK--AKGKCPvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-863 |
4.84e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLK------QEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQVSRLQLKVTAHQKKE--AELQMQL------------TESLKETDLLKGQLIKLQAELSELQETSEQAQSK 707
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEErlKEARLLLliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 708 FKSEKQSRRQLELKVTSLE-EELADLRAE---KESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEE--LDKLRQLLKK 781
Cdd:COG4717 299 SLGKEAEELQALPALEELEeEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 782 ARVSTDQ---AAAEQAELQTQWEAKCEHL---LASAKDEHLLQYQEvcAQRDASQQELLRLQEKCLALQAQVTALTEQ-- 853
Cdd:COG4717 379 AGVEDEEelrAALEQAEEYQELKEELEELeeqLEELLGELEELLEA--LDEEELEEELEELEEELEELEEELEELREEla 456
|
330
....*....|.
gi 961710479 854 -NEQHTKDLEN 863
Cdd:COG4717 457 eLEAELEQLEE 467
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
655-856 |
6.06e-11 |
|
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: 65.56 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 655 LQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRA 734
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 735 EKESLEKNLSERKKKSAqERCRA------------------------------------EEEIDEIRKSyQEELDKLRQL 778
Cdd:COG4942 91 EIAELRAELEAQKEELA-ELLRAlyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRAD-LAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 779 LKKARVSTDQAAAEQAELQTQweakcehlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ 856
Cdd:COG4942 169 LEAERAELEALLAELEEERAA--------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-780 |
1.11e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIER------------NQRYVEQSNL-MMEKRNNSLQTATENTQARVL 632
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldNTRESLETQLkVLSRSINKIKQNLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK---------LQAELSELQETSEQ 703
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkkenLEKEIDEKNKEIEE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 704 AQSKFKSEKQSRRQLELKVTSLEEELADLRAE-------KESLEKNLSERKKKSaqercraeEEIDEIRKSYQEELDKLR 776
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEieekekkISSLEKELEKAKKEN--------EKLSSIIKNIKSKKNKLK 644
|
....
gi 961710479 777 QLLK 780
Cdd:TIGR04523 645 QEVK 648
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
660-827 |
1.15e-10 |
|
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: 63.02 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 660 TAHQKKEAELQMQLTESlkETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESL 739
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 740 EKNLSE-------------------RKKKSAQERCRAEEEIDEIRKSY---QEELDKLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:COG1579 79 EEQLGNvrnnkeyealqkeieslkrRISDLEDEILELMERIEELEEELaelEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180 190
....*....|....*....|....*....|
gi 961710479 798 TQWEAKCEHLLASAKDEHLLQYQEVCAQRD 827
Cdd:COG1579 159 EELEAEREELAAKIPPELLALYERIRKRKN 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-799 |
1.52e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 563 IMGNIQRIIQENERLKqEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtaTENTQARVLHAEQEKAKVT 642
Cdd:COG4913 223 TFEAADALVEHFDDLE-RAHEALEDAREQIELLEPIRELAERYAAARERLAELE-------YLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK-LQAELSELQETSEQAQSKFKSEKQSRRQLELK 721
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 722 VTSLEEELADLRAEkesleknlserkkksAQERCraeEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQ 799
Cdd:COG4913 375 LPASAEEFAALRAE---------------AAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
575-793 |
1.52e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 652 VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD 731
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 732 LRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
579-801 |
2.58e-10 |
|
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: 65.20 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 579 QEILEK-SSRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvteeltaATAQVSRLQL 657
Cdd:pfam01576 348 QEMRQKhTQALEELTEQL-EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK-------LEGQLQELQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 658 KVTAHQKKEAELQMQLTESLKETDLL-------KGQLIKLQAEL----SELQETSE--QAQSKFKSEKQSR-RQLELKVT 723
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVssllneaEGKNIKLSKDVssleSQLQDTQEllQEETRQKLNLSTRlRQLEDERN 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 724 SLEEELADLRAEKESLEKN-------LSERKKKsAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAEL 796
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQlstlqaqLSDMKKK-LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
....*
gi 961710479 797 QTQWE 801
Cdd:pfam01576 579 QQELD 583
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-865 |
4.15e-10 |
|
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: 64.27 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIE---EQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEkakvt 642
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKE----- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTaataqvSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKV 722
Cdd:TIGR04523 306 QDWN------KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 723 TSLEEELADLRAEKESLEKNLSERKKKSAQErcraEEEIDEIRKSYqEELDKLRQLLKKARVSTDQAAAEQAELQTQWEA 802
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEK-ELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 803 KCEHLLASAK------DEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALteqnEQHTKDLENKS 865
Cdd:TIGR04523 455 IIKNLDNTREsletqlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL----EEKVKDLTKKI 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-783 |
4.61e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 506 SFLMTEARqhntEIRMAVSKVADKMDHLMTKVEELQKHsaGNSLLLPSMSVTMETSMIMGNIQRIIQENERLKQEILEKS 585
Cdd:TIGR02169 691 SSLQSELR----RIENRLDELSQELSDASRKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 586 SRIEEQNDKISEL------------------IERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTA 647
Cdd:TIGR02169 765 ARIEELEEDLHKLeealndlearlshsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 648 ATAQVSRLQLKVTAHQKKEAELQMQLTE-SLKETDL------LKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEElEAALRDLesrlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 721 KVTSLEEELADL----RAEKESLEKNLSERKKKSAQERC------------RAEEEIDEIRKSYQEELDKLRQLLKKAR 783
Cdd:TIGR02169 925 KLEALEEELSEIedpkGEDEEIPEEELSLEDVQAELQRVeeeiralepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-837 |
4.81e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQK-KEAELQMQLTESLKET----------DLLKGQLIKLQAELSELQETSEQAQSKFKSE 711
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRAAlrlwfaqrrlELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 712 KQSRRQLELKVTSLE-EELADLRAEKESLEKNLSERKKKSAQ--ERCRA-EEEIDEIRKSYQEELDKLRQLLkkarvstD 787
Cdd:COG4913 322 REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARleALLAAlGLPLPASAEEFAALRAEAAALL-------E 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 961710479 788 QAAAEQAELQTQweakcehllasaKDEHLLQYQEVCAQRDASQQELLRLQ 837
Cdd:COG4913 395 ALEEELEALEEA------------LAEAEAALRDLRRELRELEAEIASLE 432
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
571-866 |
7.45e-10 |
|
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: 63.05 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 641
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQS--KFKSEKQsrrQLE 719
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKD---TIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 720 LKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLK-KARVSTDQAAAEQAELQt 798
Cdd:COG5185 388 STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRLE- 466
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 799 qweakcehllaSAKDEHllqYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSH 866
Cdd:COG5185 467 -----------EAYDEI---NRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLD 520
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-883 |
7.51e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvTEELTAAtAQV 652
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKA-EEL 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 653 SRLQLKVTAHQKKEAE----LQMQLTESLK--------ETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEedknMALRKAEEAKkaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEEladlRAEKESLEKNLSERKKKSAQERCRAEEE---IDEIRKSYQEELDKLRQLLKKARvstDQAAAEQAELQ 797
Cdd:PTZ00121 1638 LKKKEAEE----KKKAEELKKAEEENKIKAAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAE---EAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 798 TQWEAKCEHLLASAKDEHLLQYQEvcAQRDASqqellrlQEKCLALQAQVTALTEQNEQHTKDLENKSHMSGVAAAATDP 877
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEE--AKKEAE-------EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
....*.
gi 961710479 878 SEKVKK 883
Cdd:PTZ00121 1782 EEELDE 1787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-803 |
9.24e-10 |
|
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: 63.12 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEliernqryveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQN---------------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQmQLTESLKE-TDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLD-NTRESLETqLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 726 EEELA-------DLRAEKESLEKNLSERKKK-----SAQERCRAEEEIDEirksYQEELDKLRQ----LLKK---ARVST 786
Cdd:TIGR04523 516 TKKISslkekieKLESEKKEKESKISDLEDElnkddFELKKENLEKEIDE----KNKEIEELKQtqksLKKKqeeKQELI 591
|
250
....*....|....*..
gi 961710479 787 DQAAAEQAELQTQWEAK 803
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEK 608
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
575-865 |
1.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSSRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSR 654
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 655 LQ-LKVTAHQKKEAELQMQLTESLK---ETDLLKGQLIKLQAELSELQetseQAQSKFKSEKQSRRQLELKVtslEEEla 730
Cdd:PTZ00121 1615 AEeAKIKAEELKKAEEEKKKVEQLKkkeAEEKKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKK---AEE-- 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 731 DLRAEKESLEKNlSERKKKSAQERCRAEEEI---DEIRKSYQEELDKLRQLLKKARvsTDQAAAEQAELQTQWEAKCEHL 807
Cdd:PTZ00121 1686 DEKKAAEALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEEKKKIAHL 1762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 808 lasaKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAqvtalteqnEQHTKDLENKS 865
Cdd:PTZ00121 1763 ----KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV---------DKKIKDIFDNF 1807
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
636-799 |
1.44e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 636 QEKAKVTEELTAATAQVSRL--QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFksekQ 713
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL----E 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 714 SRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
....*.
gi 961710479 794 AELQTQ 799
Cdd:COG4717 237 EAAALE 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
635-851 |
2.04e-09 |
|
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: 62.11 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 635 EQEKAK--VTEELTAATAQVSRLQLKVT----AHQKKEAELQMQLT----ESLKETDLLKgQLIKLQAELSELQETSEqa 704
Cdd:pfam01576 205 ELEKAKrkLEGESTDLQEQIAELQAQIAelraQLAKKEEELQAALArleeETAQKNNALK-KIRELEAQISELQEDLE-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 705 qskfkSEKQSRRQLELKVTSLEEELADLRAEKESL--------------EKNLSERKKKSAQERCRAEEEIDEIRK---- 766
Cdd:pfam01576 282 -----SERAARNKAEKQRRDLGEELEALKTELEDTldttaaqqelrskrEQEVTELKKALEEETRSHEAQLQEMRQkhtq 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 767 ---SYQEELDKL---RQLLKKARVSTDQAAAE-QAELQTQWEAKCEHLLASAKDEHllQYQEVCAQRDASQQELLRLQEK 839
Cdd:pfam01576 357 aleELTEQLEQAkrnKANLEKAKQALESENAElQAELRTLQQAKQDSEHKRKKLEG--QLQELQARLSESERQRAELAEK 434
|
250
....*....|..
gi 961710479 840 CLALQAQVTALT 851
Cdd:pfam01576 435 LSKLQSELESVS 446
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
600-858 |
3.79e-09 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 60.08 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 600 ERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVtahqkKEAELQM-QLTESLK 678
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI-----RELELEVlKQAQSIK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 679 ETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRrqlelkvtsleeeLADLRA-EKESLEKNLSERKKKSAQERCRA 757
Cdd:pfam15742 108 SQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVC-------------LTDTCIlEKKQLEERIKEASENEAKLKQQY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 758 EEEiDEIRK---SYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLA--SAKDEHLLQYQEVCAQRDASQQE 832
Cdd:pfam15742 175 QEE-QQKRKlldQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENekRKSDEHLKSNQELSEKLSSLQQE 253
|
250 260
....*....|....*....|....*..
gi 961710479 833 LLRLQEKCLALQAQVTA-LTEQNEQHT 858
Cdd:pfam15742 254 KEALQEELQQVLKQLDVhVRKYNEKHH 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
567-746 |
4.24e-09 |
|
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: 58.40 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIErnqryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKT------ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQEtseqaqskfksekqsrrQLELKVTSLE 726
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------------ELDEELAELE 155
|
170 180
....*....|....*....|
gi 961710479 727 EELADLRAEKESLEKNLSER 746
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-896 |
5.31e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 564 MGNIQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENT-------QARVLH 633
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAKKEELERLKKRLTgltpeklEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVSRL------------QLK------------VTAHQKKE--AELQMQLTESLKETDLLKGQL 687
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKEllEEYTAELKRIEKELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 688 IKLQAELSELqETSEQAQSKFKSEKQSRRQL-----ELKVTSLE-------------EELADLRAEKESLEKNLS----- 744
Cdd:PRK03918 476 RKLRKELREL-EKVLKKESELIKLKELAEQLkeleeKLKKYNLEelekkaeeyeklkEKLIKLKGEIKSLKKELEkleel 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 745 -------ERKKKSAQERCRA----------------EEEIDEIRKSYQE---------ELDKLRQLLKKARVSTDQAAAE 792
Cdd:PRK03918 555 kkklaelEKKLDELEEELAEllkeleelgfesveelEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 793 QAELQTQWE---AKCEHLLASAKDEhllQYQEVcaqrdasQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMSG 869
Cdd:PRK03918 635 LAETEKRLEelrKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
410 420
....*....|....*....|....*..
gi 961710479 870 VAAAATDPSEKVKKIMNQVfQSLRGEF 896
Cdd:PRK03918 705 EREKAKKELEKLEKALERV-EELREKV 730
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
572-908 |
6.60e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.37 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEILEKS--SRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENtqarvLHAEQEKAKVTEELTaaT 649
Cdd:pfam02463 649 RKGVSLEEGLAEKSevKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-----QREKEELKKLKLEAE--E 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 650 AQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSE-LQETSEQAQSKFKSEKQS-RRQLELKVTSLEE 727
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKELAEEREKTEKLKvEEEKEEKLKAQEE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 728 ELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDklRQLLKKARVSTDQA-AAEQAELQTQWEAKCEH 806
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEeITKEELLQELLLKEEEL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 807 LLASAKDEHLLQYQEVCAQRDASQQELLRLQEkcLALQAQVTALTEQNEQH--TKDLENKSHMSGVAAAATDPSEKVKKI 884
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNL--LEEKENEIEERIKEEAEilLKYEEEPEELLLEEADEKEKEENNKEE 957
|
330 340
....*....|....*....|....
gi 961710479 885 MNQVFQSLRGEFELEESYNGRAVL 908
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIE 981
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
555-793 |
7.84e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.38 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 555 SVTMETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 634
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 635 EQ--EKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQ-MQLTESL---KETDL------LKGQLIKLQAEL---SELQE 699
Cdd:COG1340 85 EKlnELREELDELRKELAELNKAGGSIDKLRKEIERLEwRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 700 TSEQAQSKFKSEKQSRRQLE----------LKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcraeEEIDEIRKS-- 767
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELH----EEIIELQKElr 240
|
250 260
....*....|....*....|....*..
gi 961710479 768 -YQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG1340 241 eLRKELKKLRKKQRALKREKEKEELEE 267
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-865 |
1.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 582 LEKSSRIEEQNDKISELIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQaRVLHAEQEKA 639
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLG-EVIKEIKRRI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 640 KVTEELTAATAQVSRLqlkvtahqKKEAElqMQLTESLKETDLLKGQLIKLQAELS----------ELQETSEQAQSKFK 709
Cdd:PRK03918 179 ERLEKFIKRTENIEEL--------IKEKE--KELEEVLREINEISSELPELREELEklekevkeleELKEEIEELEKELE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 710 SEKQSRRQLELKVTSLEEELADLRAEKESLEKN---LSERKKKsaqercraEEEIDEIRKSYQEELDKLRQLLKKARVST 786
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEK--------AEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 787 DQAAAEQAELQTqweakcehllASAKDEHLlqyQEVCAQRDASQQELLRLQEKCLALQaQVTALTEQNEQHTKDLENKS 865
Cdd:PRK03918 321 EEINGIEERIKE----------LEEKEERL---EELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLT 385
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
572-857 |
1.16e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEI-LEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtatentQARVLHAEQEKAKVTEELTAATA 650
Cdd:TIGR00618 386 QQKTTLTQKLqSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ------QRYAELCAAAITCTAQCEKLEKI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 651 QVSRLQLKVTAHQKKEAELQmQLTESLKETDLLKGQLIKLQAELSELQETSE-----QAQSKFKSEKQSRR--QLELKVT 723
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnpARQDIDNPGPLTRRmqRGEQTYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 724 SLEEELADLRAEKESLEKNLSERKKKsAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAK 803
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQ-MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 961710479 804 CEHLLASAKDEHLLQYQEVCAQrdasqqellRLQEKCLALQAQVTALTEQNEQH 857
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQ---------ELALKLTALHALQLTLTQERVRE 662
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
589-865 |
1.23e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 589 EEQNDKISELIERNQryVEQSNLMMEKRNNSLQTATEntqarvlhAEQEKAKVTEELTAataqvSRLQLKVTAHQKKEAE 668
Cdd:TIGR00618 163 KEKKELLMNLFPLDQ--YTQLALMEFAKKKSLHGKAE--------LLTLRSQLLTLCTP-----CMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 669 LQmQLTESLKETDllkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLElKVTSLEEELADLRAEKESleknlsERKK 748
Cdd:TIGR00618 228 LK-HLREALQQTQ-------QSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINR------ARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 749 KSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQ------WEAKCEHlLASAKDEHLLQYQEV 822
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrllqtLHSQEIH-IRDAHEVATSIREIS 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 961710479 823 CAQRdASQQELLRLQEKCLALQAQVTAL-----TEQNEQHTKDLENKS 865
Cdd:TIGR00618 372 CQQH-TLTQHIHTLQQQKTTLTQKLQSLckeldILQREQATIDTRTSA 418
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-777 |
1.23e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 614 EKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTES---------LKETDLLK 684
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 685 GQLIKLQAELSELQETSEQAQSKFKsekqsrrQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDE- 763
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELA-------ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPe 175
|
170
....*....|....
gi 961710479 764 IRKSYqeelDKLRQ 777
Cdd:COG1579 176 LLALY----ERIRK 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-863 |
2.42e-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: 58.49 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLK----QEILEKSSRIEEQNDKISELIERNQRYveqsnlmmEKRNNSLqtatentqarvlhaEQEKAKV 641
Cdd:TIGR04523 128 KLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEEL--------ENELNLL--------------EKEKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQVSRLQLKVTAHQKKEA---ELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQS---- 714
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnki 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 715 -----RRQLEL-----KVTSLEE-------ELADLRAEKES-LEKNLSERKKKSAQERCRAEEEIDEIRKSyqeeLDKLR 776
Cdd:TIGR04523 266 kkqlsEKQKELeqnnkKIKELEKqlnqlksEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKI----ISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 777 QLLKKARVSTDQAAAEQAELQTQWEAKCEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQN 854
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
....*....
gi 961710479 855 EQHTKDLEN 863
Cdd:TIGR04523 422 ELLEKEIER 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-800 |
2.55e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENER----LKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 642
Cdd:COG4942 32 LQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAA--TAQVSRLQLKVTAHQKKEAELQMQLTESLKETDllKGQLIKLQAELSELQETSEQAQSKfksekqsRRQLEL 720
Cdd:COG4942 108 ELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALRAELEAE-------RAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEiRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQW 800
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
566-789 |
3.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELiernqryveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEel 645
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEI---------------SSELPELREELEKLEKEVKELEELKEEIEE-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 646 taataqVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ--AQSKFKSEKQSRRQlelkvt 723
Cdd:PRK03918 243 ------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELR------ 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 724 SLEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYqEELDKLRQLLKKARVSTDQA 789
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRL-EELEERHELYEEAKAKKEEL 374
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
566-803 |
3.49e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQArvlhAEQEKAKVT 642
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE-----QAQSKFKSEKQSRRQ 717
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 718 LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
....*.
gi 961710479 798 TQWEAK 803
Cdd:COG4372 275 EEELEI 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
578-859 |
4.30e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 578 KQEILEKSSRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATentqarvlhAEQEK-AKVTEELTAATAQVSRLQ 656
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTAL---------RQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 657 LKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQL---ELKVTSLEEELADLR 733
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 734 AEKESLEKNLSERKKKSAQercrAEEEIDEIRKSYQ------------EELDKLRQLLKK--------ARVST------- 786
Cdd:COG3096 448 AKEQQATEEVLELEQKLSV----ADAARRQFEKAYElvckiageversQAWQTARELLRRyrsqqalaQRLQQlraqlae 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 787 -DQAAAEQAELQTQWEAKCEHL---LASAKD-EHLLQYQEvcAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTK 859
Cdd:COG3096 524 lEQRLRQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-783 |
5.77e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERnqryvEQSNLMMEKRNNSLQTATENTQARVLHAEQ--EKAKVTEE 644
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKL-----EKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKDEL 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 645 LTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK--LQAELSELQETSEQAQ-SKFKSEKQSRRQLELK 721
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYeeEPEELLLEEADEKEKEeNNKEEEEERNKRLLLA 968
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 722 VTSLEEELADLRAEKESLEknlsERKKKSAQERCRAEEEIDEIRksyQEELDKLRQLLKKAR 783
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKE----ERYNKDELEKERLEEEKKKLI---RAIIEETCQRLKEFL 1023
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
661-863 |
6.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 661 AHQK-KEAELQMQLTESLKEtdlLKGQLIKLQAELSELQETSEQAQSKFksekqSRRQLELkvtsLEEELADLRAEKESL 739
Cdd:COG4913 240 AHEAlEDAREQIELLEPIRE---LAERYAAARERLAELEYLRAALRLWF-----AQRRLEL----LEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 740 EknlsERKKKSAQERCRAEEEIDEIRKSYQE----ELDKLRQLLKKARVSTDQAAAEQAELQtQWEAKCEHLLASAKDEH 815
Cdd:COG4913 308 E----AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLE-ALLAALGLPLPASAEEF 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 961710479 816 LLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLEN 863
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
572-802 |
7.32e-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: 55.93 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEILEKSSRIEEQNDKISELiernqryveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAL---------------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 652 VSRLQlkvtahqKKEAELQMQLTEslkETDLLKGQLIKLQ-----AELSEL--QETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG4942 85 LAELE-------KEIAELRAELEA---QKEELAELLRALYrlgrqPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 725 LEEELADLRAEKESLEKNLsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEA 802
Cdd:COG4942 155 LRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
565-770 |
7.58e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 565 GNIQRIIQENErlkQEILEKSSRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTEE 644
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 645 LTAATAQVSRLQLKVTAHQKKEAELQmQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSekqSRRQLElKVTS 724
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING---IEERIK-ELEE 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 725 LEEELADLRAEKESLEKNLSE-----------RKKKSAQERCRAE---EEIDEIRKSYQE 770
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEEleerhelyeeaKAKKEELERLKKRltgLTPEKLEKELEE 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
575-765 |
8.79e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEqsnlmMEKRNNSLQTATENTQARVLHAEQEKA--KVTEELTAATAQV 652
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 653 SRLQLKVTAHQKKEAELQmQLTESLKEtdlLKGQLIKLQAELSEL-QETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD 731
Cdd:COG4717 142 AELPERLEELEERLEELR-ELEEELEE---LEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|....
gi 961710479 732 LRAEKESLEKNLSERKKKsaQERCRAEEEIDEIR 765
Cdd:COG4717 218 AQEELEELEEELEQLENE--LEAAALEERLKEAR 249
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
658-797 |
9.95e-08 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 53.76 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 658 KVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQaqskFKSEKQSRRQLELKVTSLEEELADLRAEKE 737
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 738 SLEknlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKaRVSTDQAAAEQAELQ 797
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KLQALGETLEKKEAQ 164
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-783 |
1.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaeqEKAKVT--EELTAATA 650
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL----AEAGVEdeEELRAALE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 651 QVSRLQlkvtAHQKKEAELQMQLTESLKE--TDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE- 727
Cdd:COG4717 393 QAEEYQ----ELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEd 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 728 -ELADLRAEKESLEKNLSERKKKsAQERCRAEEEIDEIRKSYQEEldKLRQLLKKAR 783
Cdd:COG4717 469 gELAELLQELEELKAELRELAEE-WAALKLALELLEEAREEYREE--RLPPVLERAS 522
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
618-741 |
1.07e-07 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 51.87 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 618 NSLQTATENTQARVLHAEQEKAKVTEELTAataQVSRLQlkvTAHQKKEAELQMQlTESLKETDLLKGQLIKLQAELSEL 697
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEK---QAEIAR---EAQQNYERELVLH-AEDIKALQALREELNELKAEIAEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 961710479 698 QETSEQAQSKFKSEKQSrrqLELKVTSLEEELADLRAEKESLEK 741
Cdd:pfam07926 77 KAEAESAKAELEESEES---WEEQKKELEKELSELEKRIEDLNE 117
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
576-853 |
1.19e-07 |
|
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: 55.20 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 576 RLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAkvteELTAATAQVSRl 655
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKT----SLSASVASLEK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 qlkvtahqkkeaelqmQLTESLKETDLLK------GQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:pfam15905 130 ----------------QLLELTRVNELLKakfsedGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 730 ADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRK--SYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHL 807
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITElsCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 961710479 808 LASAKDEhllqyQEVCAQRDASQQELLR-LQEKCLALQAQVTALTEQ 853
Cdd:pfam15905 274 SKQIKDL-----NEKCKLLESEKEELLReYEEKEQTLNAELEELKEK 315
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
568-859 |
1.76e-07 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 55.68 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELta 647
Cdd:pfam15964 381 EKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEK----VTREKNSLVSQLEEAQKQLASQEMDVTKVCGEM-- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 648 ataqvsRLQLKVTAHQKKEAELQMQ--LTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:pfam15964 455 ------RYQLNQTKMKKDEAEKEHReyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGES 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 726 EEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDklrqllkKARVSTDQAAAEQAELQTQWEAKCe 805
Cdd:pfam15964 529 EHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHD-------KTVNEQYSLLTSQNTFIAKLKEEC- 600
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 961710479 806 HLLASAKDEHLLQYQEVCAQRDasqQELLRLQEKCLALQAQVTALTEQNEQHTK 859
Cdd:pfam15964 601 CTLAKKLEEITQKSRSEVEQLS---QEKEYLQDRLEKLQKRNEELEEQCVQHGR 651
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-781 |
2.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELE 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLK---------------ETDLLKGQLIKLQAELSELQETSEQAQSKFKSE 711
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaealenkiedDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL 998
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710479 712 KQsRRQLelkvtsLEEELADLRAEKESLEKnlserkkksaqercrAEEEID-EIRKSYQEELDKLRQLLKK 781
Cdd:TIGR02168 999 KE-RYDF------LTAQKEDLTEAKETLEE---------------AIEEIDrEARERFKDTFDQVNENFQR 1047
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
191-309 |
2.13e-07 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 53.61 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 191 GPAVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSgkVIKAWEDGMLGMKKGGKRLLVIPPACAAGSEGVT 270
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLID----GKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 961710479 271 GWtqSPDSILVYEVEMRRVKFARDSGSDGHSVSSRDSAA 309
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
664-779 |
2.86e-07 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 50.72 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSE--KQSR-----RQLELKVTSLEEELADLRAEK 736
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvLHAEdikalQALREELNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 961710479 737 ESLEKNLSERKKKSAQERCRAEEEIDEIRKSYqEELDKLRQLL 779
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
511-803 |
3.26e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 511 EARQHNTEIRM-AVSKV--ADKMDHLMTKVEELQKHSAGNSLLLPSMSVtmetsmiMGNIQRIIQENERLKQEILEKSsr 587
Cdd:PTZ00121 1216 EARKAEDAKKAeAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAH-------FARRQAAIKAEEARKADELKKA-- 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 588 ieEQNDKISELIERNQ-RYVEQSNLMME--KRNNSLQTATENTQ--ARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAH 662
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEkKKADEAKKKAEeaKKADEAKKKAEEAKkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQltESLKETDLLK--GQLIKLQAELSE-LQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADlRAEKESL 739
Cdd:PTZ00121 1365 KAEAAEKKKE--EAKKKADAAKkkAEEKKKADEAKKkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD-EAKKKAE 1441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 740 EKNLSERKKKSAQERCRAEE---EIDEIRKSYQ-----EELDKLRQLLKKArvstDQAAAEQAELQTQWEAK 803
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEakkKAEEAKKADEakkkaEEAKKADEAKKKA----EEAKKKADEAKKAAEAK 1509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-863 |
3.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 QLKVTAHQKKEAELQMQLTESLKETD--LLKGQLIKLQAELSELQETSEQAQSKfksekqsrrqlelkvtsLEEELADLR 733
Cdd:COG1196 201 QLEPLERQAEKAERYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAE-----------------LEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 734 ---------------AEKESLEKNLSERKKKSAQERCRAEEEIDEIRKS--------YQEELDKLRQLLKKARVSTDQAA 790
Cdd:COG1196 264 eleaeleelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeLEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 791 AEQAELQTQWEAKCEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLEN 863
Cdd:COG1196 344 EELEEAEEELEEAEAELaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
557-899 |
3.71e-07 |
|
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: 54.36 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 557 TMETSMIMGNIQRIIQE----NERLKQEILEK--SSRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQAr 630
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHqkavSERQQQEKFEKmeQERLRQEKEEKAREVERRRK--------LEEAEKARQAEMDRQAA- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 631 vLHAEQEKAKVTEEltaatAQVSRLQLKvtaHQKKEAElQMQLTESLKETDLLKgQLIKLQAELSELQETSEQAQSKFKS 710
Cdd:pfam17380 335 -IYAEQERMAMERE-----RELERIRQE---ERKRELE-RIRQEEIAMEISRMR-ELERLQMERQQKNERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 711 EKQSRRQLELKVTSLEEELADLRAEKESLEKnlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQ--------LLKKA 782
Cdd:pfam17380 404 VKILEEERQRKIQQQKVEMEQIRAEQEEARQ---REVRRLEEERAREMERVRLEEQERQQQVERLRQqeeerkrkKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 783 RVSTDQAAAEQAE---LQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTK 859
Cdd:pfam17380 481 KEKRDRKRAEEQRrkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 961710479 860 DLENKSHMsgvaaaatDPSEKVKKIMNQVFQSLRGEFELE 899
Cdd:pfam17380 561 ATEERSRL--------EAMEREREMMRQIVESEKARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
511-781 |
3.94e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQK-----HSAGNSLLLPSMSVTMETSM-IMGNIQRIIQENERLKQEILEK 584
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEKELKEIEEK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 585 SSRIEEQNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARVLHAEQEKA-KVTEELTAATAQVSRLQLKVtahq 663
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKEL---- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ---------------------AQSKFKSEKQSRRQLELKV 722
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeleerlkelepfyneylelkdAEKELEREEKELKKLEEEL 628
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 723 TSLEEELADLRAEKESLEKNLSERKKKSAQERCR-AEEEIDEIRKSYQ------EELDKLRQLLKK 781
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAglraelEELEKRREEIKK 694
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
530-844 |
4.51e-07 |
|
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: 53.75 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 530 MDHLMTKVEELQKHSAGNSLLLPSMSVTMetsmimgnIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQS 609
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 610 NLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQmQLTESLKETDLLKgqlik 689
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 690 lQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQercraeeeideirksYQ 769
Cdd:pfam07888 149 -ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ---------------LQ 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 770 EELDKLRQLLKKARvstdQAAAEQAELQTQWEAKCEHLLASAKDEHLL--QYQEVCAQRDASQQEL--LRLQEKCLALQ 844
Cdd:pfam07888 213 DTITTLTQKLTTAH----RKEAENEALLEELRSLQERLNASERKVEGLgeELSSMAAQRDRTQAELhqARLQAAQLTLQ 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
633-864 |
6.26e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTEslketdlLKGQLIKLQAELSELQETSEQAQSKFKSEK 712
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------LNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQercrAEEEIDEIrksyQEELDKLRQllKKARVSTDQAAAE 792
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE----LEEQLESL----QEELAALEQ--ELQALSEAEAEQA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 793 QAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENK 864
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
650-797 |
8.07e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 53.32 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 650 AQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKvtsLEEEl 729
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 730 ADLRAekeSLEKNLSERKKKSAQERCRAEE----------EIDEIRKSYQEELD-KLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:pfam09726 478 QEARA---SAEKQLAEEKKRKKEEEATAARavalaaasrgECTESLKQRKRELEsEIKKLTHDIKLKEEQIRELEIKVQ 553
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
588-847 |
8.98e-07 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 52.28 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 588 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtatentqarvlhaEQEKaKVTEELTAATAQVSRLQLKVTAHQKKEA 667
Cdd:pfam09311 14 IQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKK-------------ELED-KMNQLSEETSNQVSTLAKRNQKSETLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 668 ELQMQLTESLKET----DLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRR-----------QLELKVTSLEEELADL 732
Cdd:pfam09311 80 ELQQAFSQAKRNFqdqlAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQaekfdmpdtvqELQELVLKYREELIEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 733 RAEKESLEKNLSER----KKKSAQERCRAEEEIDEIR---KSYQEELDKLRQLlkkaRVSTDQAAAEQAELQTQWEAKCE 805
Cdd:pfam09311 160 RTAADHMEEKLKAEilflKEQIQAEQCLKENLEETLQaeiENCKEEIASISSL----KVELERIKAEKEQLENGLTEKIR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 961710479 806 HL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQV 847
Cdd:pfam09311 236 QLedLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
518-916 |
9.90e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 518 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSLLlpSMSVTMETSMimGNIQRIIQE-----NERLKQ------EILEKSS 586
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 587 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTEELTAAT---------- 649
Cdd:pfam05483 255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEDLQIATkticqlteek 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 650 -AQVSRLQLKVTAHQKKEAELQM---QLTESL--------KETDLLKGQLIKLQAELSELQEtseqaQSKFKSEKqsrrQ 717
Cdd:pfam05483 334 eAQMEELNKAKAAHSFVVTEFEAttcSLEELLrteqqrleKNEDQLKIITMELQKKSSELEE-----MTKFKNNK----E 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 718 LELkvtsleEELADLRAEKESLeknLSERKK--KSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAE 795
Cdd:pfam05483 405 VEL------EELKKILAEDEKL---LDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 796 LQTQWE-AKCEHL-LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ-HTKDLENKSHMSGVAA 872
Cdd:pfam05483 476 LKTELEkEKLKNIeLTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENlEEKEMNLRDELESVRE 555
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 961710479 873 AATDPSEKVKKIMNQVFQSLRG-EFELEESYNGRAVLGTIMNTIK 916
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSiEYEVLKKEKQMKILENKCNNLK 600
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
567-810 |
1.03e-06 |
|
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: 53.04 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL------------------IERNQRYVEQSNL----MMEKRNNSLQTAT 624
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKkatesleeqlaaaeaeqeLEESKRETETGIQnltaEIEQGQESLTENL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 625 ENTQARV--LHAEQEKAKVTEELTAATAQVS----RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK-LQAELSEL 697
Cdd:COG5185 357 EAIKEEIenIVGEVELSKSSEELDSFKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRqIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 698 QETSEQAQSKFKSEKQSRRQLElkvtslEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:COG5185 437 EEVSKLLNELISELNKVMREAD------EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
250 260 270
....*....|....*....|....*....|...
gi 961710479 778 LLKKARVSTDQAAAEQAELQTqwEAKCEHLLAS 810
Cdd:COG5185 511 QLEGVRSKLDQVAESLKDFMR--ARGYAHILAL 541
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
511-888 |
1.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMIMGNIQRIIQENERLKQEILEKSS---R 587
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeekK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 588 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQ-LKVTAHQKKE 666
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 667 AELQMQLTESLKETDLLKGQliklqAElsELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSER 746
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKK-----AE--EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 747 KKKSAQ----ERCRAEEEIDEIRKSYQEELDKLRQLLK--------KARV--------STDQAAAEQAELQTQWEAKCEH 806
Cdd:PTZ00121 1545 KKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakkaeEARIeevmklyeEEKKMKAEEAKKAEEAKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 807 LlasAKDEHLLQYQEVCAQRDASQ----QELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMSGVAAAATDPSEKVK 882
Cdd:PTZ00121 1625 L---KKAEEEKKKVEQLKKKEAEEkkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
....*.
gi 961710479 883 KIMNQV 888
Cdd:PTZ00121 1702 KKAEEL 1707
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-864 |
1.25e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENER---LKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSlqtatENTQARVlhaEQEKAKVTE 643
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL-----EVELNKL---EKQKKENKK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 644 ELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQE---TSEQAQSKFKSEKQSRRQLEL 720
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNkllKLELLLSNLKKKIQKNKSLES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKESLEKNLSERKK--KSAQERC-RAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTeiSNTQTQLnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 798 TQWEAKCEHLLASAKDEhlL-----QYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENK 864
Cdd:TIGR04523 299 DLNNQKEQDWNKELKSE--LknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
641-853 |
1.57e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 641 VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKEslEKNLSERKKKSAQERCRAEE------------------EIDEIRKSYQ------EELDKLR 776
Cdd:COG1340 86 KLNELREELDELRKELA--ELNKAGGSIDKLRKEIERLEwrqqtevlspeeekelveKIKELEKELEkakkalEKNEKLK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 777 QLLKKARVSTDQAAAEQAELQTqweakcehlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 853
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKE---------LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-796 |
1.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 625 ENTQARVLHAEQEKAKVTEELTAATAQVSRLQlkvtaHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQA 704
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 705 QSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARV 784
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170
....*....|..
gi 961710479 785 STDQAAAEQAEL 796
Cdd:COG4717 239 AALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
633-875 |
1.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK 712
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 713 QSRRQLELKVTSLE-----EELADLrAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTD 787
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 788 QAAAEQAELQTqweakcehllasakdehllQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHM 867
Cdd:COG3883 172 ELEAQQAEQEA-------------------LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....*...
gi 961710479 868 SGVAAAAT 875
Cdd:COG3883 233 AAAAAAAA 240
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
502-749 |
2.07e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 502 SDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNSLLLPSMSVTMetsmiMGNIQRIIQEN 574
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSSRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVTEEL 645
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 646 TAATAQVSRLQLKVTAHQKKE---AELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKqsrrqlelkv 722
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA---------- 378
|
250 260
....*....|....*....|....*..
gi 961710479 723 tsleEELADLRAEKESLEKNLSERKKK 749
Cdd:PHA02562 379 ----EELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
566-778 |
2.48e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIERN-----QRYVEQSNLMMEKRNNSLQTATENTQarvlhaeqekak 640
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 641 vtEELTAATAQVS-------RLQLKVTAHQKKEAELQMQL-TESLKETDLLKGQLIKLQAELS------ELQETSEQAQS 706
Cdd:PRK11281 142 --NDLAEYNSQLVslqtqpeRAQAALYANSQRLQQIRNLLkGGKVGGKALRPSQRVLLQAEQAllnaqnDLQRKSLEGNT 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 707 KFKSEKQSRRQL-ELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcraeEEIDEIRKS--YQEELDKLRQL 778
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ----DEAARIQANplVAQELEINLQL 290
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
573-862 |
2.90e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 51.57 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSnlmMEKRNNSLQTATENTQ--ARVLHAEQEKAKVTEELTAATA 650
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSA---ALAGTEATSGASRSAQdlAELLSSFSGSSTTDTGLTKGSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLlkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQQ------QREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 731 DLRAEKESLEKNLsERKKKSAQERCRAEEEIdeirksyqeelDKLRQLLkkarvstDQAAAEQAELQTQWEAKCEHLLas 810
Cdd:pfam05667 374 ELKEQNEELEKQY-KVKKKTLDLLPDAEENI-----------AKLQALV-------DASAQRLVELAGQWEKHRVPLI-- 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 811 akdEHLLQYQEVCAQR--DASQQ--ELLRLQEKCLalqaQVTALTEQNEQHTKDLE 862
Cdd:pfam05667 433 ---EEYRALKEAKSNKedESQRKleEIKELREKIK----EVAEEAKQKEELYKQLV 481
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
689-856 |
2.98e-06 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 49.95 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 689 KLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKEsleknlSERKKKSAQ----ERcraeeEIDEI 764
Cdd:pfam15397 64 QLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQianlVR-----QLQQL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 765 RKSYQEELDKLRQLLKKarvstdqaaaEQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLR--------- 835
Cdd:pfam15397 133 KDSQQDELDELEEMRRM----------VLESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVMLKeieqfrefi 202
|
170 180
....*....|....*....|...
gi 961710479 836 --LQEKCLALQAQVTALTEQNEQ 856
Cdd:pfam15397 203 deLEEEIPKLKAEVQQLQAQRQE 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
565-865 |
3.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 565 GNIQRIIQENERLKQEILEKSSRIEEQNDKISE---------------------LIERN--------------------- 602
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeevrdlrerleeLEEERddllaeaglddadaeavearr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 603 ----------QRYVEQSNLMMEKRNNSLQTATEN------------TQARVLHAEQEKAKVT-----EELTAATAQVSRL 655
Cdd:PRK02224 317 eeledrdeelRDRLEECRVAAQAHNEEAESLREDaddleeraeelrEEAAELESELEEAREAvedrrEEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK-----------------QSRRQl 718
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRE- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 719 elKVTSLEEELADLRAEKESLEKNLSE---------RKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQA 789
Cdd:PRK02224 476 --RVEELEAELEDLEEEVEEVEERLERaedlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 790 AAEQAELQTQWE---------AKCEHLLASAKD--EHLLQYQEVCAQRDASQQELLRLQEKclalqaqVTALTEQNEQHT 858
Cdd:PRK02224 554 EEKREAAAEAEEeaeeareevAELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREK-------REALAELNDERR 626
|
....*..
gi 961710479 859 KDLENKS 865
Cdd:PRK02224 627 ERLAEKR 633
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
567-803 |
3.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSR-IEEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQArvlhaEQEKAKVTEEL 645
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEE----FRQKNGLVDLSEEAKLL-----LQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDL--LKGQLIKLQAELSELQET-SEQAQskfksekqsrrqlelKV 722
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSARyTPNHP---------------DV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 723 TSLEEELADLRAEkesLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLlkkarvstDQAAAEQAELQTQWEA 802
Cdd:COG3206 294 IALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEV 362
|
.
gi 961710479 803 K 803
Cdd:COG3206 363 A 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
573-782 |
5.75e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEkssRIEEQNDKISELIERN--QRYV---------EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:COG4913 245 EDAREQIELLE---PIRELAERYAAARERLaeLEYLraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQ--------VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK- 712
Cdd:COG4913 322 REELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELe 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961710479 713 ---QSRRQLELKVTSLEEELADLRAEKESLEKNlserkkksaqercraeeeideiRKSYQEELDKLRQLLKKA 782
Cdd:COG4913 402 aleEALAEAEAALRDLRRELRELEAEIASLERR----------------------KSNIPARLLALRDALAEA 452
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
631-869 |
5.76e-06 |
|
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: 50.53 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 631 VLHAEQEKAKVTE--ELTAATAQVSRLQLKvtahqKKEAELQMQLTE-SLKETDLLKGQLIKLQAELSELQEtsEQAQSK 707
Cdd:pfam09731 235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 708 FKSEKQSRRQLELKVTSLEEELADLRAEKESleknlsERKKKSAQERCRAEEEIDEIRKSYQEELDKlrQLLKKARVSTD 787
Cdd:pfam09731 308 KREEKHIERALEKQKEELDKLAEELSARLEE------VRAADEAQLRLEFEREREEIRESYEEKLRT--ELERQAEAHEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 788 ---QAAAEQA-ELQTQWEAKCEHLLASAKDEHLLQYQEVCAQ-RDASQQELLRLQEKCLALQAQVTALTEQNEQHTkdLE 862
Cdd:pfam09731 380 hlkDVLVEQEiELQREFLQDIKEKVEEERAGRLLKLNELLANlKGLEKATSSHSEVEDENRKAQQLWLAVEALRST--LE 457
|
....*..
gi 961710479 863 NKSHMSG 869
Cdd:pfam09731 458 DGSADSR 464
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
575-812 |
6.01e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSS-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELTA 647
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 648 ATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 728 ELADL-------RAEKESLEKNLSE-----RKKKSAQERCraEEEIDEIRKSYQ---EELDKLRQLLKKARVSTDQAAAE 792
Cdd:PRK02224 350 DADDLeeraeelREEAAELESELEEareavEDRREEIEEL--EEEIEELRERFGdapVDLGNAEDFLEELREERDELRER 427
|
250 260
....*....|....*....|....*.
gi 961710479 793 QAELQTQWE------AKCEHLLASAK 812
Cdd:PRK02224 428 EAELEATLRtarervEEAEALLEAGK 453
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
515-801 |
6.02e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 515 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMI---------MGNIQRIIQENERLKQEILEKS 585
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILllnqarlqaLEDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 586 SRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKK 665
Cdd:PLN02939 177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 666 EAELQMQLTE-SLKETDL--LKGQLIKLQAELSELQ--------ETSEQAQ-----SKFKSEK-----QSRRQLELKVTS 724
Cdd:PLN02939 256 EERVFKLEKErSLLDASLreLESKFIVAQEDVSKLSplqydcwwEKVENLQdlldrATNQVEKaalvlDQNQDLRDKVDK 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 725 LEEELADLRAEKESLEK-NLSERKKKSAQERC-RAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWE 801
Cdd:PLN02939 336 LEASLKEANVSKFSSYKvELLQQKLKLLEERLqASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSE 414
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
634-865 |
6.05e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.84 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVSRLQlkvtAHQKKEAELQMQLTESLKETDLLKGQLIKLQAelselqetSEQAQSKFKSEKQ 713
Cdd:pfam12795 11 DEAAKKKLLQDLQQALSLLDKID----ASKQRAAAYQKALDDAPAELRELRQELAALQA--------KAEAAPKEILASL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 714 SRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercRAEEEIDEIRKsyqeELDKLRQLLKKARVS-TDQAAAE 792
Cdd:pfam12795 79 SLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPE----RAQQQLSEARQ----RLQQIRNRLNGPAPPgEPLSEAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 793 QAELQTQweakcehlLASAKDEHLLQYQEVC----------AQRDASQQELLRLQEKCLALQAQVT----ALTEQNEQHT 858
Cdd:pfam12795 151 RWALQAE--------LAALKAQIDMLEQELLsnnnrqdllkARRDLLTLRIQRLEQQLQALQELLNekrlQEAEQAVAQT 222
|
....*..
gi 961710479 859 KDLENKS 865
Cdd:pfam12795 223 EQLAEEA 229
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
579-929 |
6.65e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 579 QEILEKSSRIEEQNDKISElIERNQRyveqsnlmMEKRNNSLQTATEntQARVLHAEQEKAKVTEELTAaTAQVSRLQLK 658
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLAC-IIKLQK--------TIKREKKLRETEE--VEFSLKAEVLIQKFGRSLKA-KKRFSLLKKE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 659 VTAHQ--KKEAELQMQLTE---SLKETDLLKGQLIKLQAELSEL---QETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:COG5022 868 TIYLQsaQRVELAERQLQElkiDVKSISSLKLVNLELESEIIELkksLSSDLIENLEFKTELIARLKKLLNNIDLEEGPS 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 731 DLRAEKESLEKNLSERK--KKSAQERCRA----EEEIDEIRKSyQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKC 804
Cdd:COG5022 948 IEYVKLPELNKLHEVESklKETSEEYEDLlkksTILVREGNKA-NSELKNFKKELAELSKQYGALQESTKQLKELPVEVA 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 805 EHLLASAKDEH----LLQYQEVCAQRDASQQELLRLQEKCLALQAQ-----VTALTEQNEQHTKDLENKSHMSGVAAAAT 875
Cdd:COG5022 1027 ELQSASKIISSesteLSILKPLQKLKGLLLLENNQLQARYKALKLRrenslLDDKQLYQLESTENLLKTINVKDLEVTNR 1106
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 876 DPSEKVKKIMNQVFQSLRGEFELEESYNGRAVLgtimNTIKMVTLQL-LNQHEQD 929
Cdd:COG5022 1107 NLVKPANVLQFIVAQMIKLNLLQEISKFLSQLV----NTLEPVFQKLsVLQLELD 1157
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
571-900 |
6.81e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.82 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 571 IQENE-RLKQEILEKSSRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAAT 649
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 650 AQVSRlqlKVTAHQKKEAELQmQLTESLKETDLLKGQLIKLQAELSELQETS--EQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:TIGR00606 447 EILEK---KQEELKFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 728 ELADLRAEKESLEKNLSERKKKSAqercrAEEEIDEIRKSYQEEL--------------DKLRQLLKKARVSTDQAAAEQ 793
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKMD-----KDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 794 AELQTqweakcehllaSAKDEHLLQYQEvcaqrDASQQELLRLQEK------CLALQAQVTALTEQNEQHTKDLENKSHM 867
Cdd:TIGR00606 598 KELAS-----------LEQNKNHINNEL-----ESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
330 340 350
....*....|....*....|....*....|....*..
gi 961710479 868 SGVAAA----ATDPSEKVKKIMNQVFQSlrgEFELEE 900
Cdd:TIGR00606 662 TAVYSQfitqLTDENQSCCPVCQRVFQT---EAELQE 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-735 |
7.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELieRNQRyveqsnlmmekRNNSLQtATENTQARVLHAEQEKAKVTEELT 646
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDEL--EAQI-----------RGNGGD-RLEQLEREIERLERELEERERRRA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
....*....
gi 961710479 727 EELADLRAE 735
Cdd:COG4913 440 ARLLALRDA 448
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
686-864 |
9.92e-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: 48.38 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 686 QLIKLQAELSELQETseqaqskfkseKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercRAEEEIDEIR 765
Cdd:COG1579 8 ALLDLQELDSELDRL-----------EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK----RLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 766 ksyqEELDKLRQLLKKARvSTDQAAAEQAELqtqweakcehllASAKDEhllqyqevcaqRDASQQELLRLQEKCLALQA 845
Cdd:COG1579 73 ----ARIKKYEEQLGNVR-NNKEYEALQKEI------------ESLKRR-----------ISDLEDEILELMERIEELEE 124
|
170
....*....|....*....
gi 961710479 846 QVTALTEQNEQHTKDLENK 864
Cdd:COG1579 125 ELAELEAELAELEAELEEK 143
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
574-780 |
1.00e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 574 NErLKQEIlEKSSRIEEQNDKISELIERNQRYVEQ-----------------SNLMMEKRNNSLQTATENTQAR---VLH 633
Cdd:TIGR01612 1486 NE-LKEHI-DKSKGCKDEADKNAKAIEKNKELFEQykkdvtellnkysalaiKNKFAKTKKDSEIIIKEIKDAHkkfILE 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTE--------ELTAATAQVSR-----LQLKVTAHQKKE---AELQMQLTESLKETDLLKGQLIKL-----QA 692
Cdd:TIGR01612 1564 AEKSEQKIKEikkekfriEDDAAKNDKSNkaaidIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFsidsqDT 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 693 ELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEeladLRAEKESLEKNLSERKKKSaqeRCRAEEEIDEIRKSYQEEL 772
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE----LDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEI 1716
|
....*...
gi 961710479 773 DKLRQLLK 780
Cdd:TIGR01612 1717 ESIKELIE 1724
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
572-776 |
1.23e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEILEKSSRIEEQNDKISELIERNQR-----YvEQSNLMMEKrNNSLQtatENTQARVLHAEQEKAKVTEELT 646
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRrahfsY-EDAAEMLAK-NSDLN---EKLRQRLEQAEQERTRAREQLR 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVS-----RLQLKvTAHQKKEAELQmqltESLKETDLL-----KGQLIKLQAELSELQETSEQAQSKfksekqsRR 716
Cdd:PRK04863 1010 QAQAQLAqynqvLASLK-SSYDAKRQMLQ----ELKQELQDLgvpadSGAEERARARRDELHARLSANRSR-------RN 1077
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 717 QLELKVTSLEEELadlraekESLEKNLSERKKKSAQERcraeEEIDEIRKSYQEELDKLR 776
Cdd:PRK04863 1078 QLEKQLTFCEAEM-------DNLTKKLRKLERDYHEMR----EQVVNAKAGWCAVLRLVK 1126
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
689-801 |
1.33e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 689 KLQAELSELQETSEQAQSKFKSEKQSR-RQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRK- 766
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREi 467
|
90 100 110
....*....|....*....|....*....|....*.
gi 961710479 767 -SYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWE 801
Cdd:COG2433 468 sRLDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
656-863 |
1.34e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFkseKQSRRQLE---------------- 719
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEalkddndeetretlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 720 LKVTSLEEELADLRAEKESLEKNLSERKKK--SAQERC-RAEEEIDEirksYQEELDKLRQLLKKARVS-TDQAAAEQAE 795
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQPeRAQAALYA----NSQRLQQIRNLLKGGKVGgKALRPSQRVL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710479 796 LQTQW---EAKCEHLLASAKDEHLLQ--YQevcAQRDASQQELLRLQEKCLALQAQVTA-LTEQNEQHTKDLEN 863
Cdd:PRK11281 197 LQAEQallNAQNDLQRKSLEGNTQLQdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSkRLTLSEKTVQEAQS 267
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
576-861 |
1.45e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.36 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 576 RLKQEILEKSSRIEEQNDKISELIER-NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAE------------QEKAKVT 642
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAELQEQvTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsraqearrrqqQQTASAE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQKKEAE-------LQMQLTESLKETDLLKG------QLIKLQAELSELQETSEQAQSKFK 709
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLETTMTRVEQavaripsLSNRLSYAVRKVHTIKGlmarkvALAQLRQESCPPPPPAPPVDADLS 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 710 SEKQSRRQ--------LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEE-------EIDEIRKSYQE---E 771
Cdd:pfam07111 481 LELEQLREernrldaeLQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQEslasvgqQLEVARQGQQEsteE 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 772 LDKLRQLLKKARVSTDQAAAEQ-AELQTQWEAK---CEHLLASAKDEH------LLQYQEVCAQRDASQQELLRLQEKCL 841
Cdd:pfam07111 561 AASLRQELTQQQEIYGQALQEKvAEVETRLREQlsdTKRRLNEARREQakavvsLRQIQHRATQEKERNQELRRLQDEAR 640
|
330 340
....*....|....*....|
gi 961710479 842 ALQAQVTALTEQNEQHTKDL 861
Cdd:pfam07111 641 KEEGQRLARRVQELERDKNL 660
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
578-855 |
1.45e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 578 KQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEkrnnslqtATENTQARVLHAEQEKAKVTEELTAATAQV-SRLQ 656
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE--------SSERTVSDLTASLQEKERAIEATNAEITKLrSRVD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 657 LKVT--AHQKKEAE-----------LQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQ-SKFKSEKQ-SRRQLEL- 720
Cdd:pfam15921 528 LKLQelQHLKNEGDhlrnvqteceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELq 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 -----------KVTSLEEELADLRAEKESLEKNLSER---KKKSAQER---------CRAE------------------- 758
Cdd:pfam15921 608 efkilkdkkdaKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERdqllnevktSRNElnslsedyevlkrnfrnks 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 759 EEIDEIR-------KSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDEHLLQYqevcAQRDASQQ 831
Cdd:pfam15921 688 EEMETTTnklkmqlKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE----AMTNANKE 763
|
330 340
....*....|....*....|....
gi 961710479 832 ELLRLQEKCLALQAQVTALTEQNE 855
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVATEKNK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
567-884 |
1.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEkssRIEEQNDKISELIERNQRYVEQSNL------MMEKRNNSLQTATENTQARVLHAEQEKAK 640
Cdd:PRK02224 263 LRETIAETEREREELAE---EVRDLRERLEELEEERDDLLAEAGLddadaeAVEARREELEDRDEELRDRLEECRVAAQA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 641 VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESlketdllKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKESLEKNL-SERKKKSAQERCRAE----------------EEIDEIRksyqEELDKLRQLLKKAR 783
Cdd:PRK02224 413 FLEELREERDELREREAELEATLrTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDR----ERVEELEAELEDLE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 784 VSTDQAAA--EQAELQTQWEAKCEHLLASAKD-EHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVT--ALTEQNEQHT 858
Cdd:PRK02224 489 EEVEEVEErlERAEDLVEAEDRIERLEERREDlEELIAERRETIEEKRERAEELRERAAELEAEAEEKreAAAEAEEEAE 568
|
330 340
....*....|....*....|....*.
gi 961710479 859 KDLENKSHMSGVAAAATDPSEKVKKI 884
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERI 594
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
588-855 |
1.52e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 588 IEEQNDKISELIERnQRYVEQSNLMMEkrnnslqtatentqarvlhaeqekAKVTEELTAATAQVSRLQLkvtAHQKKEA 667
Cdd:pfam00038 6 LQELNDRLASYIDK-VRFLEQQNKLLE------------------------TKISELRQKKGAEPSRLYS---LYEKEIE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 668 ELQMQLteslketDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRqlelkvtSLEEELADLR--AEKESLEKNLSE 745
Cdd:pfam00038 58 DLRRQL-------DTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRT-------SAENDLVGLRkdLDEATLARVDLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 746 RKKKSAQErcraeeEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQ-------AELQTQWEAKCEHLLASAKDEHLLQ 818
Cdd:pfam00038 124 AKIESLKE------ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKldltsalAEIRAQYEEIAAKNREEAEEWYQSK 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 961710479 819 YQEVCAQRD-------ASQQELLRLQEKCLALQAQVTALTEQNE 855
Cdd:pfam00038 198 LEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
558-862 |
1.52e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 558 METSMImgniqriiqENERLKQEILEKSSrieeQNDKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAEQE 637
Cdd:PRK04863 235 MEAALR---------ENRMTLEAIRVTQS----DRDLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELRRE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 638 KAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLtESLK-------ETDLLKGQLIKLQAELSELQETSEQAQSkfks 710
Cdd:PRK04863 295 LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDY-QAASdhlnlvqTALRQQEKIERYQADLEELEERLEEQNE---- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 711 ekqsrrqlelKVTSLEEELADLRAEKEsleknlserkkksaqercRAEEEIDEIRKS---YQEELDKLR----------Q 777
Cdd:PRK04863 370 ----------VVEEADEQQEENEARAE------------------AAEEEVDELKSQladYQQALDVQQtraiqyqqavQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 778 LLKKAR-------VSTDQAAAEQAELQTQWEAKCEHLLA---------SAKDEHLLQYQEVCA------QRDASQ--QEL 833
Cdd:PRK04863 422 ALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSleqklsvaqAAHSQFEQAYQLVRKiagevsRSEAWDvaREL 501
|
330 340
....*....|....*....|....*....
gi 961710479 834 LRLQEKCLALQAQVTALteqnEQHTKDLE 862
Cdd:PRK04863 502 LRRLREQRHLAEQLQQL----RMRLSELE 526
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
572-754 |
1.70e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEILEKSSRIEEQNDKI---SELIERNQRYVEQSNLMMEKRNNSLqtaTENTQARVLHAEQEKAKVTEELTAA 648
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARREAREQLRQA 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 649 TAQVS----RLQLKVTAHQKKEAELQmQLTESLKEtdllkgqlIKLQAElselQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG3096 1011 QAQYSqynqVLASLKSSRDAKQQTLQ-ELEQELEE--------LGVQAD----AEAEERARIRRDELHEELSQNRSRRSQ 1077
|
170 180 190
....*....|....*....|....*....|
gi 961710479 725 LEEELADLRAEKESLEKNLSERKKKSAQER 754
Cdd:COG3096 1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
588-754 |
2.03e-05 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 48.68 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 588 IEEQNDKISELIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARVLHAEQEKAKVTEELTAATAQVSRLQLK-VTA 661
Cdd:pfam15066 365 INKLKENVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVNYVHLQERyITE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 662 HQKKEAE----LQMQLTESLKEtdllkGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELkvtSLEEELAdlRAEKE 737
Cdd:pfam15066 439 MQQKNKSvsqcLEMDKTLSKKE-----EEVERLQQLKGELEKATTSALDLLKREKETREQEFL---SLQEEFQ--KHEKE 508
|
170
....*....|....*...
gi 961710479 738 SLEknlsERKK-KSAQER 754
Cdd:pfam15066 509 NLE----ERQKlKSRLEK 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
587-785 |
2.25e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 587 RIEEQNDKISEL------IERNQRYVEQsnlmMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELTAATAQVSRLql 657
Cdd:PRK04863 895 RVEEIREQLDEAeeakrfVQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRR-- 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 658 kvtAHQKKEAELQMqLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKF----------KSEKQSRRQLelkVTSLEE 727
Cdd:PRK04863 969 ---AHFSYEDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqvlaslKSSYDAKRQM---LQELKQ 1041
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 728 ELADL------------RAEKESLEKNLSE-RKKKSAQERCRA--EEEIDEIRK---SYQEELDKLRQLLKKARVS 785
Cdd:PRK04863 1042 ELQDLgvpadsgaeeraRARRDELHARLSAnRSRRNQLEKQLTfcEAEMDNLTKklrKLERDYHEMREQVVNAKAG 1117
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
631-810 |
2.35e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 48.33 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 631 VLHAEQEKAKVTEELTAATAQvsrlQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIkLQAElSELQETSEQAQSKFKS 710
Cdd:PRK00106 21 LISIKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 711 EKQSRRQLELKVT----SL---EEELADLRAEKESLEKNLSErKKKSAQERcraEEEIDEIRKSYQEELDKLRQLlkkar 783
Cdd:PRK00106 95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
|
170 180
....*....|....*....|....*..
gi 961710479 784 vstDQAAAEQAELqTQWEAKCEHLLAS 810
Cdd:PRK00106 166 ---SQAEAREIIL-AETENKLTHEIAT 188
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
671-800 |
2.36e-05 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 47.80 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 671 MQLTESLKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKS 750
Cdd:COG4026 131 NELREELLE---LKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKR 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 751 AQERCRAEEEIDEIrksYQEELDKLRQLL--------KKARVSTDQAAAEQAELQTQW 800
Cdd:COG4026 208 LLEVFSLEELWKEL---FPEELPEEDFIYfatenlkpGKIIVGQGYIAAESKEDAEEW 262
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
577-735 |
2.55e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 577 LKQEILEKSSRIEEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRL 655
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKsEKQSR-----RQLELKVTSLEEELA 730
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAKiadlgRRLNVALAQRVQELN 193
|
....*
gi 961710479 731 DLRAE 735
Cdd:PRK09039 194 RYRSE 198
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
523-862 |
2.71e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 523 VSKVADKMDHLMTKVEELQKHSAGNSLLLPSM-SVTMETSmimgNIQRIIQENERLKQEILEKSSRIEEQNDKISELIER 601
Cdd:PRK01156 144 ISGDPAQRKKILDEILEINSLERNYDKLKDVIdMLRAEIS----NIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 602 NQRYVEQSNLMMEKRNNSlqtatENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELqMQLTES----- 676
Cdd:PRK01156 220 IERLSIEYNNAMDDYNNL-----KSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDpvykn 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 677 ---LKETDLLKGQLIKLQAELSEL--QETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKE-------SLEKNLS 744
Cdd:PRK01156 294 rnyINDYFKYKNDIENKKQILSNIdaEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 745 ERKKKSAQERCRAEE---EIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDEHLLQYQE 821
Cdd:PRK01156 374 SLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 961710479 822 VCAQ-------------RDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLE 862
Cdd:PRK01156 454 VCPVcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE 507
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
518-787 |
2.80e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 518 EIRMAVSKVADKMDHLMTKV----EELQKHSAgnslllpsmsvtmETSMIMGNIQRIIQENERLKQEILEKSSRIEEQN- 592
Cdd:COG1340 33 ELNEELKELAEKRDELNAQVkelrEEAQELRE-------------KRDELNEKVKELKEERDELNEKLNELREELDELRk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 593 ------------DKISELIERNQRYVEQSNLMMEKRNNSLQTATEntQARVLHAEQEKAKVTEELTAATAQVSRLQLKVT 660
Cdd:COG1340 100 elaelnkaggsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKE--LEKELEKAKKALEKNEKLKELRAELKELRKEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 661 AHQKKEAELQMQLTEslketdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLe 740
Cdd:COG1340 178 EIHKKIKELAEEAQE-------LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 961710479 741 knlseRKKKSAQERCRAEEEIDEIRKsyqEELDKLRqllKKARVSTD 787
Cdd:COG1340 250 -----RKKQRALKREKEKEELEEKAE---EIFEKLK---KGEKLTTE 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-883 |
3.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERLKQEILEKSS---RIEE-QNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHaEQEKAKVTEELTAA 648
Cdd:PTZ00121 1112 EEARKAEEAKKKAEdarKAEEaRKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK-KAEAARKAEEVRKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 649 TaQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQsKFKSEKQSRRQLELKVTSLEEE 728
Cdd:PTZ00121 1191 E-ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 729 LADLRAE--------------KESLEKNLSERKKKSAQERCRAEE--EIDEIRKSYQEELDKLRQLLKKARVSTDQAAAE 792
Cdd:PTZ00121 1269 QAAIKAEearkadelkkaeekKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 793 QAELqtqwEAKCEHLLASAKDEHLLQYQEVCAQRDASQQElLRLQEKCLALQAQVTAltEQNEQHTKDLENKSHMSGVAA 872
Cdd:PTZ00121 1349 KAEA----EAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKA--EEDKKKADELKKAAAAKKKAD 1421
|
330
....*....|.
gi 961710479 873 AATDPSEKVKK 883
Cdd:PTZ00121 1422 EAKKKAEEKKK 1432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
606-784 |
3.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 606 VEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvtEELTAATAQVSRLQLKVTAHQKKE--AELQMQLTESLKETDLL 683
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQ--ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 684 KGQLIKLQAELSELQETSEQAQSKFK--SEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERkkKSAQERCRAEEEI 761
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEelLEALDEEELEEELEELEEELEELEEELEELREELAEL--EAELEQLEEDGEL 471
|
170 180
....*....|....*....|...
gi 961710479 762 DEIRKSYQEELDKLRQLLKKARV 784
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAA 494
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
575-853 |
3.41e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSL-------QTATENTQARVLHAEQ-----EKAKV- 641
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEA-AEEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARAl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 --TEELTAATA----QVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSR 715
Cdd:COG3096 429 cgLPDLTPENAedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 716 RQLElKVTSLEEELADLR---AEKESLEKNLSERKKKSAQERcRAEEEIDEirksYQEELDKLRQLLkkarvstDQAAAE 792
Cdd:COG3096 509 ALAQ-RLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQL-DAAEELEE----LLAELEAQLEEL-------EEQAAE 575
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 793 QAELQTQWEAKCEHLLAsakdehllQYQEVCAQRDA---SQQELLRLQEKC---LALQAQVTALTEQ 853
Cdd:COG3096 576 AVEQRSELRQQLEQLRA--------RIKELAARAPAwlaAQDALERLREQSgeaLADSQEVTAAMQQ 634
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-777 |
3.52e-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: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNL-MMEKRNNSLQTATENTQAR----------VLHAE 635
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYsWDEIDVASAEREIAELEAElerldassddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 636 QEKAKVTEELTAATAQVSRLqlkvtahQKKEAELQMQLTESLKETDLLKGQLikLQAELSELQETSEQAQSKFKSEKQSR 715
Cdd:COG4913 692 EQLEELEAELEELEEELDEL-------KGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 716 RQLELKvTSLEEELADLRAEKESLEKNLsERKKKSAQERCRAE-----EEIDEIRkSYQEELDKLRQ 777
Cdd:COG4913 763 VERELR-ENLEERIDALRARLNRAEEEL-ERAMRAFNREWPAEtadldADLESLP-EYLALLDRLEE 826
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
687-807 |
4.11e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 44.60 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 687 LIKLQAELSELQETSEQAQSKFKsekqsrrQLELKVTSLEEELADL-------RAEKESLEKNLSERKKK---SAQERCR 756
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKVK-------ELEQENLEKEQEIKSLthknqqlEEEVEKLEEQLKEAKEKaeeSEKLKTN 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710479 757 A----------EEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQtQWEAKCEHL 807
Cdd:pfam12718 75 NenltrkiqllEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERD-EWEKKYEEL 134
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
652-868 |
4.12e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.66 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 652 VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKgQLIKLQaelselqetsEQAQSKFKSekqSRRQLELKVTSLEEELAD 731
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELRKENRLLK-RLQKRQ----------EKALGKYEG---TESELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 732 LRAEKESL---EKNLSERKKKSAQERCRAeeeideirksyQEELDKLRQLLKkarvstDQAAAEQAELQTQWEAKCEHLL 808
Cdd:pfam15619 72 LRERLRRLqekERDLERKLKEKEAELLRL-----------RDQLKRLEKLSE------DKNLAEREELQKKLEQLEAKLE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 809 ASAKDEHLLQYQEVCAQRdASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMS 868
Cdd:pfam15619 135 DKDEKIQDLERKLELENK-SFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
634-799 |
4.14e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLK--ETDLLK---GQLIKLQAELSELQETSEQAQskf 708
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEkgREDLARealERKAELEAQAEALEAQLAQLE--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 709 ksekQSRRQLELKVTSLEEELADLRAEKESLeknlserkkKSAQERCRAEEEIDEIRKSYQEE--LDKLRQLlkKARVST 786
Cdd:COG1842 112 ----EQVEKLKEALRQLESKLEELKAKKDTL---------KARAKAAKAQEKVNEALSGIDSDdaTSALERM--EEKIEE 176
|
170
....*....|....
gi 961710479 787 DQAAAE-QAELQTQ 799
Cdd:COG1842 177 MEARAEaAAELAAG 190
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
663-784 |
4.35e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQLTESLKETDLL-KGQLIKLQAELSELQETSEQAQSKFKSEKQsrrqLELKVTSLEEELADLRAEKESLEK 741
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 742 NLSERKKKSAQERCRAEEEIDE--------------IRKSYQEELDKLRQL---LKKaRV 784
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
568-857 |
5.70e-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: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVE--------QSNLM----MEK-------RNNSLQTATENTQ 628
Cdd:pfam05557 145 KAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknsKSELAripeLEKelerlreHNKHLNENIENKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 629 ARVLHAEQEKAKVtEELTAATAQVSRLQLKVTahqKKEAELQ------MQLTESLKETDLLKGQLIKLQaelselQETSE 702
Cdd:pfam05557 225 LLKEEVEDLKRKL-EREEKYREEAATLELEKE---KLEQELQswvklaQDTGLNLRSPEDLSRRIEQLQ------QREIV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 703 QAQSKFKSEKQSRrQLELKVTSLEEELADLRAEKESLEKnlsERKKKSAQERcRAEEEIDEIRKsyqeELDKLRQLLKKA 782
Cdd:pfam05557 295 LKEENSSLTSSAR-QLEKARRELEQELAQYLKKIEDLNK---KLKRHKALVR-RLQRRVLLLTK----ERDGYRAILESY 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 783 RVSTDQAAAEQAELQTQWEAkcehllASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQH 857
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEA------EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLA 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
643-866 |
5.74e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLtESLKETDLLKGQLI---------KLQAELSELQETSEQAQSKFKSEKQ 713
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL-EQAKEGLSALNRLLprlnlladeTLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 714 SRRQLELkvtsLEEELADLRAEKESLEK-----NLSERKKKSAQERCRAEEEIDEIR----------------------- 765
Cdd:PRK04863 916 HGNALAQ----LEPIVSVLQSDPEQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRahfsyedaaemlaknsdlneklr 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 766 ---KSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDEHLLQYQ-----EVCA--QRDASQQELLR 835
Cdd:PRK04863 992 qrlEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsgaEERAraRRDELHARLSA 1071
|
250 260 270
....*....|....*....|....*....|....*
gi 961710479 836 LQEKCLALQAQVT----ALTEQNEQHTKdLENKSH 866
Cdd:PRK04863 1072 NRSRRNQLEKQLTfceaEMDNLTKKLRK-LERDYH 1105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
634-865 |
6.94e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVS------RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSK 707
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIidleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 708 fksekQSRRQLELKVTSLEEELADLraEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTD 787
Cdd:pfam02463 250 -----QEEIESSKQEIEKEEEKLAQ--VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 788 QAAAEQAELQTQWE-AKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQE----KCLALQAQVTALTEQNEQHTKDLE 862
Cdd:pfam02463 323 KKKAEKELKKEKEEiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllakKKLESERLSSAAKLKEEELELKSE 402
|
...
gi 961710479 863 NKS 865
Cdd:pfam02463 403 EEK 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
571-776 |
7.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATA 650
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAE------LSELQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERieslerIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 961710479 725 LEEELADLRAEKESLEKNLSERKKKSAQE-RCRAEEEIDEIrksyQEELDKLR 776
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEAREdKERAEEYLEQV----EEKLDELR 673
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
568-894 |
7.51e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEKSSRIEEQNDKISELiERNQRYVEQSNLMMEKRNNSLQTATE---------------NTQARVL 632
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKL-DNEIKALKSRKKQMEKDNSELELKMEkvfqgtdeqlndlyhNHQRTVR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKAKVTEEL--------------TAATAQVSRLQLKVTAHQkkeaelqmqltESLKETDLLKgQLIKLQAELSELQ 698
Cdd:TIGR00606 316 EKERELVDCQRELeklnkerrllnqekTELLVEQGRLQLQADRHQ-----------EHIRARDSLI-QSLATRLELDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 699 ETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLrAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQL 778
Cdd:TIGR00606 384 RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADL-QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 779 LKKARVSTDQAAAEQAELQtqweakcehllasaKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHT 858
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELR--------------KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN 528
|
330 340 350
....*....|....*....|....*....|....*.
gi 961710479 859 KDLENKSHMSGVAAAATDPSEKVKKIMNQVFQSLRG 894
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
586-802 |
7.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 586 SRIEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQ--LKVTAHQ 663
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 664 KKEAELQMQLTESLKE----TDLLKGQLI---------KLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfSDFLDRLSAlskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 731 DLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEA 802
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
517-777 |
7.73e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 517 TEIRMAVSKVADKMDHLMTKVEEL-QKHSAGNSLllpsmsVTMETsmimgNIQRIIQENERLKQEILEKSSRIEEQNDKI 595
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeERLERAEDL------VEAED-----RIERLEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 596 SELIERNQRYVEQsnlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELTA-------------ATAQVSRLQLKvt 660
Cdd:PRK02224 540 EELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKERIESlerirtllaaiadAEDEIERLREK-- 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 661 ahQKKEAELQMQLTESLKETDLLKGQLiklQAELSElqETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLE 740
Cdd:PRK02224 615 --REALAELNDERRERLAEKRERKREL---EAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 961710479 741 KNLSER-----KKKSAQERCRAEE----EIDEIRKSYQEELDKLRQ 777
Cdd:PRK02224 688 NELEELeelreRREALENRVEALEalydEAEELESMYGDLRAELRQ 733
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
643-796 |
7.89e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 45.05 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQsrrQLELKV 722
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKD---QALADL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 723 TSLEEELADL--RAE--KESLE--KNLSERKKKSAQERC----------------------RAEEEIDEIRKSYQEELDK 774
Cdd:pfam05010 85 NSVEKSFSDLfkRYEkqKEVISgyKKNEESLKKCAQDYLarikkeeqryqalkahaeekldQANEEIAQVRSKAKAETAA 164
|
170 180
....*....|....*....|....*....
gi 961710479 775 LRQLLKKARVST-------DQAAAEQAEL 796
Cdd:pfam05010 165 LQASLRKEQMKVqslerqlEQKTKENEEL 193
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
664-797 |
8.39e-05 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 43.82 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQ----------SKFKSEKQSRRQlelKVTSLEEELADLR 733
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAIleaenskaevETLKAEIEEMAQ---NLRDLELDLVTLR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 734 AEKESLEKNLSERkkksaQERCRAEEEIDE-IRKSYQEELDKLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:pfam10473 80 SEKENLTKELQKK-----QERVSELESLNSsLENLLEEKEQEKVQMKEESKTAVEMLQTQLKELN 139
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
528-901 |
8.58e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 528 DKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSM-IMGNIQR----IIQENERLKQEILEKSSRIEE-------QNDKI 595
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTqLVGQHGRtagaMQVEKAQLEKEINDRRLELQEfkilkdkKDAKI 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 596 SELIERnqryveQSNLMMEKRNnSLQTATENTQArVLHAEQEKAKVTEELTAATAQVSRLQ-----LKVTAHQKKEA--- 667
Cdd:pfam15921 621 RELEAR------VSDLELEKVK-LVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSedyevLKRNFRNKSEEmet 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 668 ---ELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESL--EKN 742
Cdd:pfam15921 693 ttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLkeEKN 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 743 -LSERKKKSAQERCRAEEEIDEIRKsyQEEldKLRQLLKKARVSTDQAAAEQAELQTQWEAKcEHLLASAKDEHLLQYQE 821
Cdd:pfam15921 773 kLSQELSTVATEKNKMAGELEVLRS--QER--RLKEKVANMEVALDKASLQFAECQDIIQRQ-EQESVRLKLQHTLDVKE 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 822 VCAQRDASQQELlrlqeKCLALQAQVTALTEQNEQHTKDLEN--KSHMSGVAAAATDPSEKVKkimnQVFQSLRGEFELE 899
Cdd:pfam15921 848 LQGPGYTSNSSM-----KPRLLQPASFTRTHSNVPSSQSTASflSHHSRKTNALKEDPTRDLK----QLLQELRSVINEE 918
|
..
gi 961710479 900 ES 901
Cdd:pfam15921 919 PT 920
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
561-798 |
9.35e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 45.48 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 561 SMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKI-------SELIERNQRYVEQSNLMM---EKRNNSLQTATENTQAR 630
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIeilekelSSLAQETEELQKKATQTLakaQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 631 VLHAEQEKAKVTEeltaATAQVSRL-----QLKVTAHQKKEAELQMQLTEsLKETDLLKgQLIKLQAELSELQETSEQAQ 705
Cdd:pfam06008 88 AEAIKNLIDNIKE----INEKVATLgendfALPSSDLSRMLAEAQRMLGE-IRSRDFGT-QLQNAEAELKAAQDLLSRIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 706 SKFKSEKQSRRQLElkvTSLEEELADLRAEKESLEKNLSERKKKSAQ------ERCRAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:pfam06008 162 TWFQSPQEENKALA---NALRDSLAEYEAKLSDLRELLREAAAKTRDanrlnlANQANLREFQRKKEEVSEQKNQLEETL 238
|
250
....*....|....*....
gi 961710479 780 KKARVSTDQAAAEQAELQT 798
Cdd:pfam06008 239 KTARDSLDAANLLLQEIDD 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-798 |
9.43e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 517 TEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMIM--GNIQRIiQENERLKQEILEKSSRIEEQNDK 594
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQraAHEARI-RELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 595 ISELIER--NQRYVEQSnlmmEKRNnsLQTATENTQA--RVLHAEQEKAKVTEELTAATAQ-----VSRLQLKVTAHQKK 665
Cdd:pfam07888 155 MKERAKKagAQRKEEEA----ERKQ--LQAKLQQTEEelRSLSKEFQELRNSLAQRDTQVLqlqdtITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 666 EAE----------LQMQLTESLKETDLLKGQL----------------IKLQA-----ELSELQETSEQAQSKFKSEKQS 714
Cdd:pfam07888 229 EAEnealleelrsLQERLNASERKVEGLGEELssmaaqrdrtqaelhqARLQAaqltlQLADASLALREGRARWAQERET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 715 RRQ-----------LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSY--------------Q 769
Cdd:pfam07888 309 LQQsaeadkdriekLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaqkekeqlqaekQ 388
|
330 340
....*....|....*....|....*....
gi 961710479 770 EELDKLRQLLKKARVSTDQAAAEQAELQT 798
Cdd:pfam07888 389 ELLEYIRQLEQRLETVADAKWSEAALTST 417
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
686-857 |
1.00e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 686 QLIKLQAELSELQEtsEQAQSKFKSEKQSR--RQLELKVTSL---------EEELADLRAEKESLEKNLSERKKKSAQER 754
Cdd:COG3096 786 RLEELRAERDELAE--QYAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 755 craeEEIDEIRksyqEELDKLRQLLKKARVSTDQAAAEQAE-LQTQWEAKCE-------HLLASAKDEHLLQY-QEVCAQ 825
Cdd:COG3096 864 ----QQLDQLK----EQLQLLNKLLPQANLLADETLADRLEeLREELDAAQEaqafiqqHGKALAQLEPLVAVlQSDPEQ 935
|
170 180 190
....*....|....*....|....*....|....
gi 961710479 826 RDASQQELLRLQEKCLALQAQVTALTE--QNEQH 857
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEvvQRRPH 969
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
632-897 |
1.06e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 632 LHAEQEKAKVTEELTAATAQVSRLqlkVTAHQKKEAELQMQL-TESLKETDllkgqliKLQAELSELQETSEQ------- 703
Cdd:NF041483 83 IQADQLRADAERELRDARAQTQRI---LQEHAEHQARLQAELhTEAVQRRQ-------QLDQELAERRQTVEShvnenva 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 704 --AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqERCRAEEEideirksyqeeldklrQLLKK 781
Cdd:NF041483 153 waEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEA-ESARAEAE----------------AILRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 782 ARVSTDQ---AAAEQAELQTQWEAKCEHLLASAKDEHLLQYQEV---CAQRDASQQELLR---------LQEKCLALQAQ 846
Cdd:NF041483 216 ARKDAERllnAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraAEQRMQEAEEALRearaeaekvVAEAKEAAAKQ 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 961710479 847 VTALTEQNEQHTKdlENKSHMSGVAAAATDPSEKVKKIMNQVFQSLRGEFE 897
Cdd:NF041483 296 LASAESANEQRTR--TAKEEIARLVGEATKEAEALKAEAEQALADARAEAE 344
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
726-862 |
1.35e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 726 EEELADLRAEKESLEKNLSErkkksAQERCraeEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAeQAELQtQWEAKCE 805
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-----AEERL---EALEAELDALQERREALQRLAEYSWDEIDVASA-EREIA-ELEAELE 678
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 806 HLLASAKDehLLQYQEvcaQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLE 862
Cdd:COG4913 679 RLDASSDD--LAALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
589-906 |
1.36e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 589 EEQNDKISEL--IERNQRYVEQSNLMMEKRNNSLqTATENTQARVLHAEQEKAKVTEELTAataqvsRLqlkvtAHQKKE 666
Cdd:pfam01576 5 EEMQAKEEELqkVKERQQKAESELKELEKKHQQL-CEEKNALQEQLQAETELCAEAEEMRA------RL-----AARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 667 AELQMQLTESLKETDLLKGQliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEknlsER 746
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQ--QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE----DQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 747 KKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKkarvstdqaaaeqaeLQTQWEAKCEHLLASAKDEHLLQyQEVCAQR 826
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKSLSK---------------LKNKHEAMISDLEERLKKEEKGR-QELEKAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 827 DASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLEN-KSHMSGVAAAATDPSEKVKKIMNQVFQsLRGEFELEESYNGR 905
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAaLARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNK 289
|
.
gi 961710479 906 A 906
Cdd:pfam01576 290 A 290
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
514-740 |
1.39e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 514 QHNTEIRMAVSKVADkmdhlmTKVEELQKHSAGNSLLLPSMSVTMETSMIMGNIQ-------RIIQENERLKQEILEKSS 586
Cdd:pfam15921 615 KKDAKIRELEARVSD------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKtsrnelnSLSEDYEVLKRNFRNKSE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 587 RIEEQNDKISELIERNQRYVEQSNlmmekrnNSLQTaTENTQArvlHAEQEKAKVTEELTAATAQVSRLQLKVTAhqkke 666
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTR-------NTLKS-MEGSDG---HAMKVAMGMQKQITAKRGQIDALQSKIQF----- 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710479 667 aeLQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELadlraEKESLE 740
Cdd:pfam15921 753 --LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL-----DKASLQ 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
623-783 |
1.42e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 623 ATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE 702
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 703 QAQSKfksEKQSRRQLELKVTSLEEELADLRAEKESLEK-NLserkkksaqercRAEEEIDEIRKSYqEELDKLRQLLKK 781
Cdd:COG1196 746 ELLEE---EALEELPEPPDLEELERELERLEREIEALGPvNL------------LAIEEYEELEERY-DFLSEQREDLEE 809
|
..
gi 961710479 782 AR 783
Cdd:COG1196 810 AR 811
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
567-835 |
1.42e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRyvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ--AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVtahQKKEAELQMQLTESLKETDLLKGQL---IKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVT 723
Cdd:pfam13868 156 RILEYLKEKAERE---EEREAEREEIEEEKEREIARLRAQQekaQDEKAERDELRAKLYQEEQERKERQKEREEAEKKAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 724 SLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARvstdqaaaeqAELQTQWEAK 803
Cdd:pfam13868 233 QRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR----------RELEKQIEER 302
|
250 260 270
....*....|....*....|....*....|..
gi 961710479 804 CEHLLASAKDEhlLQYQEVCAQRDASQQELLR 835
Cdd:pfam13868 303 EEQRAAEREEE--LEEGERLREEEAERRERIE 332
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
628-776 |
1.43e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.77 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 628 QARVLHAEQEKakvteeLTAATAQVSRLQLKVTAHQKKEAELQMQLTESlketdllkgQLIKLQAELSELQETSEQAQSK 707
Cdd:pfam08614 15 RTALLEAENAK------LQSEPESVLPSTSSSKLSKASPQSASIQSLEQ---------LLAQLREELAELYRSRGELAQR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 708 FKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERkkksaqercraEEEIDEIRKSY---QEELDKLR 776
Cdd:pfam08614 80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR-----------EEELREKRKLNqdlQDELVALQ 140
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
567-754 |
1.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQT--ATENTQARVLHAeqekakv 641
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRsgGSVSYLDVLLGS------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 tEELTAATAQVSRLQlKVTAHQKKEAELQMQLTESLKET-DLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:COG3883 112 -ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190
....*....|....*....|....*....|....
gi 961710479 721 KVTSLEEELADLRAEKESLEKNLSERKKKSAQER 754
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
559-777 |
1.47e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 559 ETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISEL-IERNQRYVEQS---NLMMEKRNNSLQTATENTQARVLHA 634
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEqAEWKELEKEEEreeDERILEYLKEKAEREEEREAEREEI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 635 EQEKAKVTEELTAATAQVS---------RLQLKVTAHQKKEAELQMQLTESLKEtdllkgQLIKLQAELSELQETSEQAQ 705
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQdekaerdelRAKLYQEEQERKERQKEREEAEKKAR------QRQELQQAREEQIELKERRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 706 SKFKSEKQSRRQLELKVTSLEEELADLRAEK---------ESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLR 776
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmkrlehrRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIE 332
|
.
gi 961710479 777 Q 777
Cdd:pfam13868 333 E 333
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
567-855 |
1.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELieRNQRYVEQSNLMMEKRNNSLQTAT-----ENTQARVLHAEQEKAKV 641
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEEL--EEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKgqliKLQAElsELQETSEQAQSKFKSEKQSRRQLELK 721
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE----ELEEE--ELEELLAALGLPPDLSPEELLELLDR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 722 VTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEiDEIRKSYqEELDKLRQLLKKARVSTDQaaaeqaeLQTQWE 801
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE-EELRAAL-EQAEEYQELKEELEELEEQ-------LEELLG 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 961710479 802 AKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNE 855
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
194-261 |
1.55e-04 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 42.78 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 194 VEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLrLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPA 261
Cdd:COG1047 1 IEKGDVVTLHYTLKLED----GEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPE 63
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
669-853 |
1.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 669 LQMQLTESLKETDLLKGQLIKLQAELSElqetSEQAQSKFKSEKQS------RRQLELKVTSLEEELADLRAEKESLEKN 742
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLvdlseeAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 743 LSERKKKSAQERCRAEE-----EIDEIRKSYQE---ELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKde 814
Cdd:COG3206 242 LAALRAQLGSGPDALPEllqspVIQQLRAQLAEleaELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE-- 319
|
170 180 190
....*....|....*....|....*....|....*....
gi 961710479 815 hllqyqevcaqrdaSQQELLRLQEKclALQAQVTALTEQ 853
Cdd:COG3206 320 --------------AELEALQAREA--SLQAQLAQLEAR 342
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-781 |
1.60e-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: 45.78 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISEL------------IERNQRYVEQsnlmMEKRNNSLQTATENTQARVLH 633
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkenlekeIDEKNKEIEE----LKQTQKSLKKKQEEKQELIDQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVSrlqlkvtahqkkeaELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQ 713
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKIS--------------SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 714 SRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRA--EEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:TIGR04523 660 KWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIkdLPKLEEKYKEIEKELKKLDEFSKE 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
582-860 |
2.11e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 582 LEKSSR-----IEEQNDKISELiERNQRYVEQSNLMMEKRNNSLQTATE-NTQARVLHAEQEKAKVTEELTAATAQV--S 653
Cdd:pfam01576 683 LERSKRaleqqVEEMKTQLEEL-EDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELedE 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 654 RLQ--LKVTAHQKKEAELQ---MQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEE 728
Cdd:pfam01576 762 RKQraQAVAAKKKLELDLKeleAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 729 LADLRAEKESleknlSERKKKSAQ-ERCRAEEEIDEIRKSYQEELDKLRQLlkKARVStdQAAAEQAELQTQWEAKCEHL 807
Cdd:pfam01576 842 LLQLQEDLAA-----SERARRQAQqERDELADEIASGASGKSALQDEKRRL--EARIA--QLEEELEEEQSNTELLNDRL 912
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 808 LASAKDEHLLQyQEVCAQRDASQ-------------QEL-LRLQE-----------KCLALQAQVTALTEQNEQHTKD 860
Cdd:pfam01576 913 RKSTLQVEQLT-TELAAERSTSQksesarqqlerqnKELkAKLQEmegtvkskfksSIAALEAKIAQLEEQLEQESRE 989
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
726-807 |
2.64e-04 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 43.50 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 726 EEELADLRAEKEslEKNLSERKKKSAQERCRAEEEiDEIRKsyqEELDKLRQLLKKARVSTDQAAAEqAELQTQWE--AK 803
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERKEALEKLRAE-AREEAEWEryMR 77
|
....
gi 961710479 804 CEHL 807
Cdd:pfam15927 78 CDGL 81
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
567-772 |
2.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKS-SRIEEQNDKISELIERNQRYVEQSNLMMEKRNNslqtatentqarvlhaEQEKAKVTEEL 645
Cdd:PRK03918 565 LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELERE----------------EKELKKLEEEL 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTEslKETDLLKGQLIKLQAELSELQEtseqaqsKFKSEKQSRRQLELKVTSL 725
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKL 699
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 726 EEELADLRAEKESLEK---------NLSER-KKKSAQERCRAEEEIDEIRKSYQEEL 772
Cdd:PRK03918 700 KEELEEREKAKKELEKlekalerveELREKvKKYKALLKERALSKVGEIASEIFEEL 756
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
631-853 |
2.90e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 631 VLHAEQEKAKVTEELTAATAQVSRLQLK--VTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQEtSEQAQSKF 708
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWErqRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE-EKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 709 KSEKQSR-RQLELKVTSLEEELADLRAEKESLEknlsERKKKSAQERCRAEEEideiRKSYQ-------EELDKLRQLLK 780
Cdd:pfam07888 124 RAAHEARiRELEEDIKTLTQRVLERETELERMK----ERAKKAGAQRKEEEAE----RKQLQaklqqteEELRSLSKEFQ 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961710479 781 KARVSTDQAAAEQAELQTQWeAKCEHLLASAkdehllqyQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 853
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTI-TTLTQKLTTA--------HRKEAENEALLEELRSLQERLNASERKVEGLGEE 259
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
580-754 |
3.00e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 580 EILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELtaATAQVSrlq 656
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlesTKSQLQESEQLIAELRSEL--ASLKES--- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 657 lkvtahqKKEAELQMQ-LTESLKETDLlkgQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAdlRAE 735
Cdd:pfam05911 739 -------NSLAETQLKcMAESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNE 806
|
170 180
....*....|....*....|
gi 961710479 736 KESLEKNL-SERKKKSAQER 754
Cdd:pfam05911 807 KKESSNCDaDQEDKKLQQEK 826
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
567-869 |
3.05e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA---------EQE 637
Cdd:pfam15921 269 IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyedkieELE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 638 KAKV--TEELTAATAQV-----------SRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQA 704
Cdd:pfam15921 349 KQLVlaNSELTEARTERdqfsqesgnldDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 705 Q------SKFKSEKQSRrqlelkvtsLEEELADLRAEKESLEKNLSerkkKSAQercrAEEEIDEIRKSYQEELDKLRQL 778
Cdd:pfam15921 429 QrleallKAMKSECQGQ---------MERQMAAIQGKNESLEKVSS----LTAQ----LESTKEMLRKVVEELTAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 779 LKKARVSTDQAAAEQaELQTQWEAKCEHL--LASAKDEHLLQYQEVCAQRDasqqELLRLQEKCLALQAQVTALTEQNEQ 856
Cdd:pfam15921 492 ESSERTVSDLTASLQ-EKERAIEATNAEItkLRSRVDLKLQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEI 566
|
330
....*....|...
gi 961710479 857 HTKDLENKSHMSG 869
Cdd:pfam15921 567 LRQQIENMTQLVG 579
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
647-812 |
3.50e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEE---LQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 727 E------ELADLRAEKES-----LEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLK-KARVSTDQAAAEQA 794
Cdd:PRK09510 136 EaaakaaAAAKAKAEAEAkraaaAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKkKAEAEAKKKAAAEA 215
|
170
....*....|....*...
gi 961710479 795 ELQTQWEAKCEHLLASAK 812
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
656-820 |
3.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 656 QLKVTAHQKKEAELQMQLTESLKETD-LLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLra 734
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 735 EKESLEKNLSERKKKSAqercRAEEEIDEIRKSYQEELDKLRQLLKKARVST-----DQAAAEQAELQTQWEAK--CEHL 807
Cdd:COG4717 426 DEEELEEELEELEEELE----ELEEELEELREELAELEAELEQLEEDGELAEllqelEELKAELRELAEEWAALklALEL 501
|
170
....*....|...
gi 961710479 808 LASAKDEHLLQYQ 820
Cdd:COG4717 502 LEEAREEYREERL 514
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
720-849 |
3.86e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 720 LKVTSLEEELADLRAEKESLEKnlserkkksaqERCRAEEEIDEirkSYQEELDKLRQLLKKARvstdqaaAEQAELQTQ 799
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE-------EELEALKAR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 961710479 800 WEAKCEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTA 849
Cdd:COG0542 463 WEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
514-710 |
4.04e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.11 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 514 QHNTEIRMAVSKVADKMDHLMTKVEE---LQKHSAgnslllpsmsvTMETSmimgniqriIQENERLKQEILEK----SS 586
Cdd:pfam15665 22 AHEEEIQQILAETREKILQYKSKIGEeldLKRRIQ-----------TLEES---------LEQHERMKRQALTEfeqyKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 587 RIEEQNDKISEliERNQRYVEQSNLMMEKRNNSLQTATENTQARVlHAEQEKAKVTEELTAATAQ-VSRLQLKVTAHQKK 665
Cdd:pfam15665 82 RVEERELKAEA--EHRQRVVELSREVEEAKRAFEEKLESFEQLQA-QFEQEKRKALEELRAKHRQeIQELLTTQRAQSAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 961710479 666 EAELQMQLTESLK-ETDLLKGQLIKLQAELSELQETSEQAQSKFKS 710
Cdd:pfam15665 159 SLAEQEKLEELHKaELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
573-853 |
5.03e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 573 ENERlkQEILEKSSRIE-EQNDKISELIERNQRYVEQSNLM--MEKRNNSLQTATENT---QARVLHAE--QEK-AKVTE 643
Cdd:PRK04863 278 ANER--RVHLEEALELRrELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQAAsdhLNLVQTALrqQEKiERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 644 ELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETS---EQAQSKFKSEKQSRRQLEL 720
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyQQAVQALERAKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 721 KVTSLEEELADLRAEKE-------SLEKNLS-------------------------ERKKKSAQERCRAEEE-------- 760
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQeateellSLEQKLSvaqaahsqfeqayqlvrkiagevsrSEAWDVARELLRRLREqrhlaeql 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 761 ------IDEIRKSYQEE--LDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDEHlLQYQEVCAQRDASQQE 832
Cdd:PRK04863 516 qqlrmrLSELEQRLRQQqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR-ERRMALRQQLEQLQAR 594
|
330 340
....*....|....*....|....
gi 961710479 833 LLRLQEKC---LALQAQVTALTEQ 853
Cdd:PRK04863 595 IQRLAARApawLAAQDALARLREQ 618
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
652-803 |
5.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 652 VSRLQLKVTAHQK-KEAElqmQLTESLKETDLLKGQLIKLQAELsELQETSEQAQSKFKSEKQSRR--------QLELKV 722
Cdd:PRK12704 20 IGYFVRKKIAEAKiKEAE---EEAKRILEEAKKEAEAIKKEALL-EAKEEIHKLRNEFEKELRERRnelqklekRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 723 TSLEEELADLRAEKESLEKNLS--ERKKKSAQERcraEEEIDEIrksYQEELDKL------------RQLLKKARvstDQ 788
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKelEQKQQELEKK---EEELEEL---IEEQLQELerisgltaeeakEILLEKVE---EE 166
|
170
....*....|....*
gi 961710479 789 AAAEQAELQTQWEAK 803
Cdd:PRK12704 167 ARHEAAVLIKEIEEE 181
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
635-778 |
5.64e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 635 EQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTE--SLKETDLLKgqlikLQAELSELQETSEQAQSKFKSEK 712
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEleDCDPTELDR-----AKEKLKKLLQEIMIKVKKLEELE 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercraeeeiDEIRKsYQEELDKLRQL 778
Cdd:smart00787 232 EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTF----------KEIEK-LKEQLKLLQSL 286
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
598-752 |
6.60e-04 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 41.44 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 598 LIERNQRYVEQSNlMMEKRNNSLQTATENTQAR--VLHAEQEKAKVTEEltaataqvsrlQLKVTAHQKKEAELQ--MQL 673
Cdd:cd12923 10 LKEINKEYLDKSR-EYDELYEKYNKLSQEIQLKrqALEAFEEAVKMFEE-----------QLRTQEKFQKEAQPHekQRL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 674 TESLKetdllkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQ 752
Cdd:cd12923 78 MENNE----------LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQKDQYLRWLKRKGVSQEE 146
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
514-764 |
7.68e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 514 QHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMEtsMIMGNIQRIIQE-------NERLKQEILEKSS 586
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP--GRQSIIDLKEKEipelrnkLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 587 RIEEQNDKISEL----------------IERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEKAKVTEELTAATA 650
Cdd:TIGR00606 766 DIEEQETLLGTImpeeesakvcltdvtiMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQlelkVTSLEEELA 730
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLE 919
|
250 260 270
....*....|....*....|....*....|....
gi 961710479 731 DLRAEKESLEKNLSERKKKSAQERCRAEEEIDEI 764
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
669-856 |
7.93e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 42.06 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 669 LQMQLTESLKETDLLKGQLIKlqaELSELQETSEQAQSKFKSEKQS-RRQLELKvtslEEELADLRAEKESLEkNLSERK 747
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQ---ECEEIERRRQELASRYTQQTAElQTQLLQK----EKEQASLKKELQALR-PFAKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 748 KKSAQERCRAEEEIDEIRKSYQEELDKLR-QLLK-KARV---STDQAAAEQAELQT-QWEAKCEHLLASAKDEHLLQYQE 821
Cdd:pfam14988 81 ESQEREIQDLEEEKEKVRAETAEKDREAHlQFLKeKALLekqLQELRILELGERATrELKRKAQALKLAAKQALSEFCRS 160
|
170 180 190
....*....|....*....|....*....|....*
gi 961710479 822 VCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ 856
Cdd:pfam14988 161 IKRENRQLQKELLQLIQETQALEAIKSKLENRKQR 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-795 |
8.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqTATENTQARVLHAEQEKAKVTEELT 646
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAAE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 647 AATAQVSRLQLKvtahQKKEAELQMQLTESLKETdlLKGQLIKLQAELSELQETSEQAQSKFKSE-----------KQSR 715
Cdd:COG4913 741 DLARLELRALLE----ERFAAALGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 716 RQLELKVTSLEEE-LADLRAEKESLEKNLSERKK-----KSAQERCRAEEEIDEI-------------------RKSYQE 770
Cdd:COG4913 815 PEYLALLDRLEEDgLPEYEERFKELLNENSIEFVadllsKLRRAIREIKERIDPLndslkripfgpgrylrleaRPRPDP 894
|
250 260
....*....|....*....|....*
gi 961710479 771 ELDKLRQLLKKARVSTDQAAAEQAE 795
Cdd:COG4913 895 EVREFRQELRAVTSGASLFDEELSE 919
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
572-756 |
8.95e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 572 QENERLKQEILEKSSRIEEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEELTAAT 649
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQEEFRRK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 650 AQVSRLQLKVTAHQKKEAELQMQlteslKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:pfam15709 432 LQELQRKKQQEEAERAEAEKQRQ-----KE---LEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
170 180
....*....|....*....|....*..
gi 961710479 730 ADLRAEKESleknlserkKKSAQERCR 756
Cdd:pfam15709 504 AARLALEEA---------MKQAQEQAR 521
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
568-835 |
9.67e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEKSSRieeqndkiseliernqryveqsnlmmekrnNSLQTATENTqARVLHAEQEKAKVTEELTA 647
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGV------------------------------EGLDSSTALT-LELEELRQERDLLREEIQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 648 ATAQVSRLQlkvtahqkkeaeLQMQLTESlketdllkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:pfam09787 66 LRGQIQQLR------------TELQELEA------------QQQEEAESSREQLQELEEQLATERSARREAEAELERLQE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 728 EladLRAEKESLeknlsERKKKSAQERCRAEEeideirksyqEELDKLR-QLLKKARVSTDQAAAEQ---------AELQ 797
Cdd:pfam09787 122 E---LRYLEEEL-----RRSKATLQSRIKDRE----------AEIEKLRnQLTSKSQSSSSQSELENrlhqltetlIQKQ 183
|
250 260 270
....*....|....*....|....*....|....*...
gi 961710479 798 TQWEAkcehlLASAKDEHLLQYQEVCAQRDASQQELLR 835
Cdd:pfam09787 184 TMLEA-----LSTEKNSLVLQLERMEQQIKELQGEGSN 216
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
689-777 |
9.85e-04 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 41.06 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 689 KLQAELSELQETSEQAQSKFKSEKQSRRQ----LELKVTSLEEELADLRAEKESLEK-----------NLSERKKKSAQE 753
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKE 126
|
90 100
....*....|....*....|....
gi 961710479 754 RCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam09744 127 YSKLHERETEVLRKLKEVVDRQRD 150
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
654-807 |
1.02e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 41.44 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 654 RLQLKVTAHQKKEAELQM----QLTESLKETDLLKgqlikLQAELSELQETSEQaqskfKSEKQSRrqLELKVTSLEEEL 729
Cdd:pfam13870 12 RLELITLKHTLAKIQEKLeqkeELGEGLTMIDFLQ-----LQIENQALNEKIEE-----RNKELKR--LKLKVTNTVHAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 730 ADLRaEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVST------------DQAAAEQAELQ 797
Cdd:pfam13870 80 THLK-EKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGgllhvpallhdyDKTKAEVEEKR 158
|
170
....*....|...
gi 961710479 798 ---TQWEAKCEHL 807
Cdd:pfam13870 159 ksvKKLRRKVKIL 171
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
663-849 |
1.08e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQLTESLKETDLLKGQL-----IKLQA----ELSE----------LQETSEQAQSKFKSE--------KQSR 715
Cdd:COG0497 171 KKELEELRADEAERARELDLLRFQLeeleaAALQPgeeeELEEerrrlsnaekLREALQEALEALSGGeggaldllGQAL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 716 RQLElKVTSLEEELADLRAEKESLEKNLSErkkkSAQE--RCRAEEEIDEIRKSYQEE-LDKLRQLLKKARVSTDQAAAE 792
Cdd:COG0497 251 RALE-RLAEYDPSLAELAERLESALIELEE----AASElrRYLDSLEFDPERLEEVEErLALLRRLARKYGVTVEELLAY 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 793 QAELQTQWEAkcehLLASakDEHLLQYQevcAQRDASQQELLRL--------QEKCLALQAQVTA 849
Cdd:COG0497 326 AEELRAELAE----LENS--DERLEELE---AELAEAEAELLEAaeklsaarKKAAKKLEKAVTA 381
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
695-932 |
1.31e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 695 SELQETSEQAQSKFKSEKQSRRQLELKvtsLEEELADLRAEKESlEKNLSERKKKSAQERCRAEEEI-DEIRKSYQEELD 773
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIID---LEELKLQELKLKEQ-AKKALEYYQLKEKLELEEEYLLyLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 774 KLRQLLKKARVSTDQAAAEQAelqtqweakcehlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 853
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIE-------------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 854 NEQHTKDLENKSHmsgvaaaaTDPSEKVKKIMNQVFQSLRGEFELEESYNGRAVLGTIM-NTIKMVTLQLLNQHEQDKGQ 932
Cdd:pfam02463 308 RKVDDEEKLKESE--------KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeELEKLQEKLEQLEEELLAKK 379
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
628-800 |
1.40e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 40.84 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 628 QARVLHAE-QEKAKVTEELTAATAQVSRlqlkvtahqkkeaELQMQLT--ESLKETdllkgqlIKLQAELSELQET-SEQ 703
Cdd:cd12926 9 QLKVYHQQyQDKSREYDQLYEEYTRTSQ-------------ELQMKRTaiEAFNET-------IKIFEEQGQTQEKcSKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 704 AQSKFKSEKQSR--RQLELKVTSLEEELADLRAEKESLEKNLserKKKSAQERcraeeEIDEIRKSYQEELDKLRQLLKK 781
Cdd:cd12926 69 YLERFRREGNEKemQRILLNSERLKSRIAEIHESRTKLEQDL---RAQASDNR-----EIDKRMNSLKPDLMQLRKIRDQ 140
|
170
....*....|....*....
gi 961710479 782 ARVSTDQAAAEQAELQtQW 800
Cdd:cd12926 141 YLVWLTQKGARQKKIN-EW 158
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
307-499 |
1.48e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.83 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 307 SAAPSPIPGADSLSADPVVSPPTSVPFKSGEPALRIKSnslneqlTVNTNPDTVKAKLISRMAKMgQPMLPILPPQLDSN 386
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPSQVSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 387 DSEIEEVntVRGAGQPVATP-SMQPSLQPaHPVLPQMTSQAPQPSVSglQAPsaalmqvasLDSHSAVSGNAQSFQpyag 465
Cdd:pfam03154 264 QPLPQPS--LHGQMPPMPHSlQTGPSHMQ-HPVPPQPFPLTPQSSQS--QVP---------PGPSPAAPGQSQQRI---- 325
|
170 180 190
....*....|....*....|....*....|....*.
gi 961710479 466 mqayAYPHASAVTSQLQPAR--PLYPTPLSQsPHFQ 499
Cdd:pfam03154 326 ----HTPPSQSQLQSQQPPReqPLPPAPLSM-PHIK 356
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
713-799 |
1.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDklrQLLKKARVSTDQAAAE 792
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD---EIIKELRQLQKGGYAS 603
|
....*..
gi 961710479 793 QAELQTQ 799
Cdd:PRK00409 604 VKAHELI 610
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
663-862 |
1.70e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQaqsKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEK- 741
Cdd:pfam03528 7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE---DLKRQNAVLQEAQVELDALQNQLALARAEMENIKAv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 742 -NLSERKKksaqercraEEEIDEIRKSYQEELDKLRQLLKKA--------RVSTDQAAAEQAELQTQWE---AKCEHLLA 809
Cdd:pfam03528 84 aTVSENTK---------QEAIDEVKSQWQEEVASLQAIMKETvreyevqfHRRLEQERAQWNQYRESAEreiADLRRRLS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 961710479 810 SAKDEHLLQYQEVCAQRDASqqellRLQEKCLALQAQVTALTE---QNEQHTKDLE 862
Cdd:pfam03528 155 EGQEEENLEDEMKKAQEDAE-----KLRSVVMPMEKEIAALKAkltEAEDKIKELE 205
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
693-863 |
1.81e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 693 ELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEE---IDEIRKSYQ 769
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEreqMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 770 EELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKcEHLLASAKDEHLLQYQEVCAQRDAS-QQELLRLQEKCLALQAQVT 848
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEErEAEREEIEEEKEREIARLR 190
|
170
....*....|....*
gi 961710479 849 ALTEQNEQHTKDLEN 863
Cdd:pfam13868 191 AQQEKAQDEKAERDE 205
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
566-771 |
1.82e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERL------KQEILEKSSRIEEQNDKISELIERNQRYV-------EQSNLMMEKRNNSLQTATENTQARVL 632
Cdd:PTZ00440 2378 KLLKNIKRNNTLcnnnniKDFISNIGKSVETIKQRFSSNLPEKEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDI 2457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKAKVTEELTAataqVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK 712
Cdd:PTZ00440 2458 DNEKNKENNNMNAEK----IDDLIENVTSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNS 2533
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 713 QS-RRQLELKVTSLEE-------ELADLRAEKESLEKNL---SERKKKSAQERCRAEEEIDEIRKSYQEE 771
Cdd:PTZ00440 2534 TYiINELESHVSKLNEllsyidnEIKELENEKLKLLEKAkieESRKERERIESETQEDNTDEEQINRQQQ 2603
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
706-799 |
1.89e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 706 SKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKsYQEELDKLRQLLKKARVS 785
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
90
....*....|....
gi 961710479 786 TDQAAAEQAELQTQ 799
Cdd:COG1340 80 RDELNEKLNELREE 93
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
663-849 |
2.03e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQLTESLKETDLLKGQL-------IKLQAELSELQETSEQAQSKFKSEKQSRRQLElkvtSLEEELADLRAE 735
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNrlanqriLELQQQVEELQKALQEQGSKAEDSSLLKQKLE----EHLEKLHEAQSE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 736 KESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEEL----DKLRQLLKKAR------------VSTDQAAAEQAELQTQ 799
Cdd:pfam05622 379 LQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMkameERYKKYVEKAKsviktldpkqnpASPPEIQALKNQLLEK 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710479 800 wEAKCEHLLASAKDEHLLQYQE------------VCAQRDASQQELLRLQ---EKCLALQAQVTA 849
Cdd:pfam05622 459 -DKKIEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
615-764 |
2.06e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.89 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 615 KRNNSLQTATEntqarvlHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETdLLKGQLIKLQAEL 694
Cdd:COG2882 2 KRSFRLQTLLD-------LAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQG-LSAAQLRNYQQFI 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710479 695 SELQETSEQAQSKfksEKQSRRQLELKvtslEEELADLRAEKESLEKnLSERKKKSAQERCRAEE--EIDEI 764
Cdd:COG2882 74 ARLDEAIEQQQQQ---VAQAEQQVEQA----RQAWLEARQERKALEK-LKERRREEERQEENRREqkELDEL 137
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
663-816 |
2.14e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 663 QKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQ---SRRQLE----LKVTSLEEELADLRAE 735
Cdd:pfam05701 285 KKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAelaSLRQREgmasIAVSSLEAELNRTKSE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 736 KESL---EKNLSERKKKSAQERCRAEEEIDEIRKSYQeeldKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAK 812
Cdd:pfam05701 365 IALVqakEKEAREKMVELPKQLQQAAQEAEEAKSLAQ----AAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKA 440
|
....
gi 961710479 813 DEHL 816
Cdd:pfam05701 441 SEKL 444
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
694-799 |
2.18e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.57 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 694 LSELQETSEQAQSKfksekqsRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEirksYQEELD 773
Cdd:pfam06785 85 FKILEETLEELQSE-------EERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAE----KQLLIN 153
|
90 100
....*....|....*....|....*.
gi 961710479 774 KLRQLLKKARVSTDQAAAEQAELQTQ 799
Cdd:pfam06785 154 EYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
517-858 |
2.51e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 517 TEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMimgniQRIIQENERL--KQEILEKSSRIEEQND 593
Cdd:PRK10246 179 TEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTDEEKQLltAQQQQQQSLNWLTRLD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 594 KISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLH------AEQEKA---------KVTEELTAATAQVSRL-QL 657
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRphweriQEQSAAlahtrqqieEVNTRLQSTMALRARIrHH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 658 KVTAHQKKEAELQmQLTESLKETDLL--------------------KGQLIKLQAELSELQE------------TSEQAQ 705
Cdd:PRK10246 334 AAKQSAELQAQQQ-SLNTWLAEHDRFrqwnnelagwraqfsqqtsdREQLRQWQQQLTHAEQklnalpaitltlTADEVA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 706 SKFKSEKQSRrQLELKVTSLEEELADLRAEKESLEKNLSerkkKSAQERCRAEEEIDEIRKSYQEEldklRQLLKKARVS 785
Cdd:PRK10246 413 AALAQHAEQR-PLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNEMRQRYKEK----TQQLADVKTI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 786 TDQAA------AEQAELQTqweAKCEHLLASAKDEHLLQYQEVC-----AQRDASQQELLRLQEKCLALQAQVTALTEQN 854
Cdd:PRK10246 484 CEQEArikdleAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
....
gi 961710479 855 EQHT 858
Cdd:PRK10246 561 QRDE 564
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
946-1124 |
2.85e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 946 PRQPSVSGSAGPPPVPlSGEMQGSPSLSPEQAVQEAVPPPPRVlsTPQEEVQGREGEPSEAEALSeieEGSLSPELTCGP 1025
Cdd:PHA03247 2878 PARPPVRRLARPAVSR-STESFALPPDQPERPPQPQAPPPPQP--QPQPPPPPQPQPPPPPPPRP---QPPLAPTTDPAG 2951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 1026 SQRALGPPTSVPPMPPGPVLVDSECEETLASAlenPCVEEPESTARlSLTSHLLKGDPLASGSESPGEEPQPP--ELKK- 1102
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA---PSREAPASSTP-PLTGHSLSRVSSWASSLALHEETDPPpvSLKQt 3027
|
170 180
....*....|....*....|....*...
gi 961710479 1103 ------DEDVTSSAIPYREPGGTEAGSP 1124
Cdd:PHA03247 3028 lwppddTEDSDADSLFDSDSERSDLEAL 3055
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-782 |
3.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 621 QTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQET 700
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 701 SEQAQSKFKSEkQSRRQLELKVTSLEEELADL-----RAEKESLEknLSERKKKSAQERCRAEEEIDEIRKSyQEELDKL 775
Cdd:COG1196 749 EEEALEELPEP-PDLEELERELERLEREIEALgpvnlLAIEEYEE--LEERYDFLSEQREDLEEARETLEEA-IEEIDRE 824
|
....*...
gi 961710479 776 -RQLLKKA 782
Cdd:COG1196 825 tRERFLET 832
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
580-799 |
3.64e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 580 EILEKSSRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQlkv 659
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDAS-KQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 660 tahqkKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD-------- 731
Cdd:pfam12795 79 -----SLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPlseaqrwa 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710479 732 LRAEKESLEKNLSERKKKSA-----QERCRAEEEIDEIRksyQEELDKLRQLLK-----KARVSTDQAAAEQAELQTQ 799
Cdd:pfam12795 154 LQAELAALKAQIDMLEQELLsnnnrQDLLKARRDLLTLR---IQRLEQQLQALQellneKRLQEAEQAVAQTEQLAEE 228
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
602-796 |
3.66e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 602 NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKvtahQKKEAELQMQLTESLK-ET 680
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKAAAAAKaKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 681 DLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEe 760
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAA- 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 961710479 761 ideirKSYQEELDKLRQLLKKARVSTDQAAAEQAEL 796
Cdd:PRK09510 229 -----KAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
717-864 |
3.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 717 QLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIR---KSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710479 794 AELQTQWEAKCEHLLASAKdehllQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENK 864
Cdd:COG4372 83 EELNEQLQAAQAELAQAQE-----ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
597-777 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 597 ELIE-RNQRYVEQSNLM-----MEKRNNSLQTATENTQARVLHAEqEKAKVTEeltaataqvsrlqlKVTAHQKKEAElq 670
Cdd:pfam15905 160 ELMKlRNKLEAKMKEVMakqegMEGKLQVTQKNLEHSKGKVAQLE-EKLVSTE--------------KEKIEEKSETE-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 671 mQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSrrqLELKVTSLEEELADLRAEKESLEknlSERKKKS 750
Cdd:pfam15905 223 -KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLE---SEKEELL 295
|
170 180 190
....*....|....*....|....*....|...
gi 961710479 751 AQERCRAE------EEIDEIRKSYQEELDKLRQ 777
Cdd:pfam15905 296 REYEEKEQtlnaelEELKEKLTLEEQEHQKLQQ 328
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
666-865 |
3.98e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 666 EAELQMQLtESLKETDLLKGQLIKLQAELSELQETSEQAQSkfksEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSE 745
Cdd:PRK11281 38 EADVQAQL-DALNKQKLLEAEDKLVQQDLEQTLALLDKIDR----QKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 746 RKKKSAqercrAEEEIDEIrksyQEELDKLRQLLKKARVSTDQAAAEQAELQTQWE-AKcehllaSAKDEHLLQYQEVCA 824
Cdd:PRK11281 113 ETRETL-----STLSLRQL----ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPErAQ------AALYANSQRLQQIRN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 961710479 825 QRDASQ--QELLRLQEKCLaLQAQVTALTEQNEQHTKDLENKS 865
Cdd:PRK11281 178 LLKGGKvgGKALRPSQRVL-LQAEQALLNAQNDLQRKSLEGNT 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
568-932 |
4.44e-03 |
|
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: 41.36 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEKSSRIEEQNDKIS------ELIERNQRYVEQSNLmmEKRNNSLQTAtENTQARVLHAEQEKAKV 641
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNGELSAADAAVAkdrselEALEDQHGAFLDADI--ETAAADQEQL-PSWQSELENLEERLKAL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 642 TEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK--LQAELSELQETSEQAQSKFKSEKQ--SRRQ 717
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEddLQALESELREQLEAGKLEFNEEEYrlKSRL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 718 LELK-----VTSLEEELADLRAEKESLEKnLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLlkKARVSTDQAAAE 792
Cdd:pfam12128 447 GELKlrlnqATATPELLLQLENFDERIER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQA--SRRLEERQSALD 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 793 QAELQ----------------TQWEAKCEHLLASakdEHLLQYQEVCAQRDASQQELLRLQEKCLALQAqvtalTEQNEQ 856
Cdd:pfam12128 524 ELELQlfpqagtllhflrkeaPDWEQSIGKVISP---ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKR-----IDVPEW 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 857 HTKDLENKSHMSGVAAAATDPSEKVKKIMNQVFQsLRGEFE---LEESYNGRAVLGTIMNTIKMVTLQllnQHEQDKGQ 932
Cdd:pfam12128 596 AASEEELRERLDKAEEALQSAREKQAAAEEQLVQ-ANGELEkasREETFARTALKNARLDLRRLFDEK---QSEKDKKN 670
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
628-781 |
4.77e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 628 QARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSK 707
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710479 708 FKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIrksyQEELDKLRQLLKK 781
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL----ERELERLEREIEA 778
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
558-733 |
4.83e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 558 METSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtatENTQArvlhaEQE 637
Cdd:pfam15294 98 FEEREFTSSNKKPNFELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQATQALD---EKSKL-----EKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 638 KAKVTEELTAATAQVSRLQlKVTAHQKKEAELQMQLTESLKETDL----LKGQLIKLQAELSELQETSEQAQS----KFk 709
Cdd:pfam15294 170 LKDLQKEQGAKKDVKSNLK-EISDLEEKMAALKSDLEKTLNASTAlqksLEEDLASTKHELLKVQEQLEMAEKelekKF- 247
|
170 180
....*....|....*....|....
gi 961710479 710 SEKQSRRQLELKVTSLEEELADLR 733
Cdd:pfam15294 248 QQTAAYRNMKEMLTKKNEQIKELR 271
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
689-795 |
5.11e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 689 KLQAELSELQETSEQAQSKFkseKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcraEEEIDEIRKSY 768
Cdd:smart00935 8 KILQESPAGKAAQKQLEKEF---KKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKK---VQEFQRKQQKL 81
|
90 100
....*....|....*....|....*...
gi 961710479 769 QEELDKLRQ-LLKKARVSTDQAAAEQAE 795
Cdd:smart00935 82 QQDLQKRQQeELQKILDKINKAIKEVAK 109
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
569-864 |
5.39e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 569 RIIQ-ENERLKQEILEKSSRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQarvlhaEQEKAKvtEELTA 647
Cdd:pfam05557 10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLE------KREAEA--EEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 648 ATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDL-LKGQLIKLQ--------------AELSELQETSEQAQSKFKSEK 712
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVIScLKNELSELRrqiqraelelqstnSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 713 QSRRQLELKVTSL---EEELADLRAEKESLEKNlSERKKKSAQERCRAEEEIDEIRKsYQEELDKLRQLLKKARVSTDQA 789
Cdd:pfam05557 153 QLRQNLEKQQSSLaeaEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 790 AAEQAELQTQWEAKCEHLLASAKDEHL---LQYQEVCAQR--------DASQQELLRLQEKCLALQAQVTALTEQNEQHT 858
Cdd:pfam05557 231 EDLKRKLEREEKYREEAATLELEKEKLeqeLQSWVKLAQDtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
....*....
gi 961710479 859 K---DLENK 864
Cdd:pfam05557 311 KarrELEQE 319
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-862 |
5.50e-03 |
|
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: 41.21 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 669 LQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEK--NLSER 746
Cdd:TIGR02169 140 LQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 747 KKKSAQ-----ERCRAEEEIDEIRK---SYQEELDKLRQLLKKARVSTDQAAAEQAELQTQWEAKCEHLLASAKDE-HLL 817
Cdd:TIGR02169 220 KREYEGyellkEKEALERQKEAIERqlaSLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGEL 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 961710479 818 QYQEVCAQR--DASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLE 862
Cdd:TIGR02169 300 EAEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
716-812 |
5.55e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 716 RQLELKVTSLEEELADLRAEKESLEKnlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQlLKKARVSTDQAAAEQAE 795
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASF---ERLAELRDELAELEEELEALKARWEAEKELIEE-IQELKEELEQRYGKIPE 489
|
90
....*....|....*..
gi 961710479 796 LQTQWEAKCEHLLASAK 812
Cdd:COG0542 490 LEKELAELEEELAELAP 506
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
566-888 |
6.33e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 566 NIQRIIQENERLKQEILEKSsrIEEQNDKISEL---------IER-NQRYVEQSNLMMEKRNNSLQTATE-NTQARVLHA 634
Cdd:PRK04778 26 RNYKRIDELEERKQELENLP--VNDELEKVKKLnltgqseekFEEwRQKWDEIVTNSLPDIEEQLFEAEElNDKFRFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 635 EQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAElQMQLTESLKET------DLL------------------------- 683
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEK-NREEVEQLKDLyrelrkSLLanrfsfgpaldelekqlenleeefs 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 684 --------------KGQLIKLQAELSELQETSEQ-------AQSKFKSE----KQSRRQLE-----LKVTSLEEELADLR 733
Cdd:PRK04778 183 qfveltesgdyveaREILDQLEEELAALEQIMEEipellkeLQTELPDQlqelKAGYRELVeegyhLDHLDIEKEIQDLK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 734 AEKESLEKNLSERKKKsaqercRAEEEIDEIrksyQEELDKLRQLLKKarvstdqaaaeqaelqtqwEAKCEHLLASAKD 813
Cdd:PRK04778 263 EQIDENLALLEELDLD------EAEEKNEEI----QERIDQLYDILER-------------------EVKARKYVEKNSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 814 EHLLQYQEVCAQRDASQQELLRLQ----------EKCLALQAQVTALTEQNEQHTKDLENKshmsgvAAAATDPSEKVKK 883
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDRVKqsytlneselESVRQLEKQLESLEKQYDEITERIAEQ------EIAYSELQEELEE 387
|
....*
gi 961710479 884 IMNQV 888
Cdd:PRK04778 388 ILKQL 392
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
649-777 |
6.74e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.56 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 649 TAQVSRLQLKVTAHQKKEAELQMQLtESLK--ETDLlkgqliklqAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKI-DALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKE 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 961710479 727 EELADLRAEKESLEKNLSerkkkSAQERC-RAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam18595 71 IELRELERREERLQRQLE-----NAQEKLeRLREQAEEKREAAQARLEELRE 117
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
697-794 |
6.75e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 697 LQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKES-LEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKL 775
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQE 108
|
90
....*....|....*....
gi 961710479 776 RQllkKARVSTDQAAAEQA 794
Cdd:COG0711 109 RA---KALAELRAEVADLA 124
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
673-749 |
6.88e-03 |
|
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.
Pssm-ID: 461756 [Multi-domain] Cd Length: 114 Bit Score: 37.56 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 673 LTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA------DLRAEKESLEKNLSER 746
Cdd:pfam05837 1 LLPLINRRDELSSAILKLSSELRELQEELTEVEKENLRLKRKNRELAAELLELAKEKEsrredpKLRAQLEKLEAELKKS 80
|
...
gi 961710479 747 KKK 749
Cdd:pfam05837 81 RRR 83
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
561-795 |
7.02e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 561 SMIMGNIqrIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKR--------NNSLQtATENTQARVL 632
Cdd:NF033838 28 SLFLGGV--VHAEEVRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRkhtqnvalNKKLS-DIKTEYLYEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 633 HAEQEKA------KVTEELTAATAQ----VSRLQLKVTAHQKKEAELQMQlTESLKETDLLKGQLI---KLQAELSELQE 699
Cdd:NF033838 105 NVLKEKSeaeltsKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEAEKK-AKDQKEEDRRNYPTNtykTLELEIAESDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 700 TSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKK--KSAQERCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:NF033838 184 EVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
250
....*....|....*...
gi 961710479 778 LLKKArVSTDQAAAEQAE 795
Cdd:NF033838 264 RAKRG-VLGEPATPDKKE 280
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
625-864 |
7.09e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 625 ENTQARVLHAEQEKA---KVTEELTAATAQVSRLQLKvtaHQKKEAELQMQLTESLKETdllkgQLIKLQAELSELQETS 701
Cdd:pfam13868 30 EKKRIKAEEKEEERRldeMMEEERERALEEEEEKEEE---RKEERKRYRQELEEQIEER-----EQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 702 ------------EQAQSKFKSEKQSRRQLELKVTSleEELADLRA-----EKESLEKNLSERKKKSAQERcRAEEEIDEI 764
Cdd:pfam13868 102 qmdeiveriqeeDQAEAEEKLEKQRQLREEIDEFN--EEQAEWKElekeeEREEDERILEYLKEKAEREE-EREAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 765 RKSYQEELDKLRQLLKKARVSTDQ-----AAAEQAELQTQWEAKcehllasAKDEhLLQYQEVCAQRDASQQELLRLQEK 839
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQK-------EREE-AEKKARQRQELQQAREEQIELKER 250
|
250 260 270
....*....|....*....|....*....|.
gi 961710479 840 CLALQAQ------VTALTEQNEQHTKDLENK 864
Cdd:pfam13868 251 RLAEEAEreeeefERMLRKQAEDEEIEQEEA 281
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
634-775 |
7.41e-03 |
|
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: 39.12 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQK-KEA---------ELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ 703
Cdd:pfam13851 52 IQQENKRLTEPLQKAQEEVEELRKQLENYEKdKQSlknlkarlkVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEA 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710479 704 AQS--KFKSEKQSrRQLELKVTSLEEELadlraekESLEKNLSERKKKS---AQERCRAEEEIDEIRKSYQEELDKL 775
Cdd:pfam13851 132 AIQdvQQKTGLKN-LLLEKKLQALGETL-------EKKEAQLNEVLAAAnldPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
567-797 |
7.52e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMME---KRNNSLQTATENTQARVLHAEQ---E 637
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLqkkIENLQEQLRDKDKQLAglkERVKSLQTDSSNTDTALTTLEEalsE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 638 KAKVTEeltaataqvsRLQLKvtaHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQ 717
Cdd:pfam10174 448 KERIIE----------RLKEQ---REREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 718 LELKVTSLEEELADLRAEKESLEKNLseRKKKSAQERCRAEEEIdeirksyqeeLDKLRQLLKKARVSTDQAAAEQAELQ 797
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQL--KKAHNAEEAVRTNPEI----------NDRIRLLEQEVARYKEESGKAQAEVE 582
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
690-797 |
7.90e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 690 LQA--ELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADlraEKESLEKNLSERKKKSAQERCRAEEEIDEIRKS 767
Cdd:cd16269 187 LQAdqALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLED---QERSYEEHLRQLKEKMEEERENLLKEQERALES 263
|
90 100 110
....*....|....*....|....*....|
gi 961710479 768 YQEELDKLRQllkkaRVSTDQAAAEQAELQ 797
Cdd:cd16269 264 KLKEQEALLE-----EGFKEQAELLQEEIR 288
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
568-888 |
8.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.22 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 568 QRIIQENERLKQEILEkssRIEEQNDKISELI---ERNQRYVEQSNLMMEKRNNSLQT-------ATENTQARVLHAEQE 637
Cdd:pfam06160 85 KKALDEIEELLDDIEE---DIKQILEELDELLeseEKNREEVEELKDKYRELRKTLLAnrfsygpAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 638 KAKVtEELT------AATAQVSRLQLKVTAHQKKEAELQmQLTESLKETdllkgqlikLQAELSELQETSEQAQSKfkse 711
Cdd:pfam06160 162 FSQF-EELTesgdylEAREVLEKLEEETDALEELMEDIP-PLYEELKTE---------LPDQLEELKEGYREMEEE---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 712 kqsrrQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRA-EEEIDEI----------RKSYQEELDKLRQLLK 780
Cdd:pfam06160 227 -----GYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 781 KARVSTDQAAAEQAELQtqweakcehllasakDEHLLQYQEVCAQRDasqqellrlqekclaLQAQVTALTEQNEQHTKD 860
Cdd:pfam06160 302 HAEEQNKELKEELERVQ---------------QSYTLNENELERVRG---------------LEKQLEELEKRYDEIVER 351
|
330 340
....*....|....*....|....*...
gi 961710479 861 LENKShmsgvaAAATDPSEKVKKIMNQV 888
Cdd:pfam06160 352 LEEKE------VAYSELQEELEEILEQL 373
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
630-803 |
8.87e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 630 RVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLI--KLQAELSE----LQETSEQ 703
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEeeRQRQEEEErkqrLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 704 AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKE---SLEKNLSERKKKSAQercRAEEEIDEIRKSYQEELDKLRQLLK 780
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLME---MAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*.
gi 961710479 781 KARVSTDQAAA---EQAELQTQWEAK 803
Cdd:pfam15709 496 ERRQKEEEAARlalEEAMKQAQEQAR 521
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
628-799 |
8.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 628 QARVLHAEQEKAK-VTEELTAATAQVSRLQLKVTAHQKKE---AELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ 703
Cdd:PRK04863 497 VARELLRRLREQRhLAEQLQQLRMRLSELEQRLRQQQRAErllAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 704 AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKnlserkkksAQERCRAE----EEIDEIRKSYQEEldklrqlL 779
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR---------LREQSGEEfedsQDVTEYMQQLLER-------E 640
|
170 180
....*....|....*....|
gi 961710479 780 KKARVSTDQAAAEQAELQTQ 799
Cdd:PRK04863 641 RELTVERDELAARKQALDEE 660
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
575-779 |
9.33e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 575 ERLKQEI-LEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVlhaEQEKAKVTEELTAATAQVS 653
Cdd:PRK05771 34 EDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV---EEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 654 RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQA------ELSELQETSEQAQSKFKSEKQSRR-----QLELKV 722
Cdd:PRK05771 111 ELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 961710479 723 TSLEEELADLRAEKESL--EKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:PRK05771 191 DEVEEELKKLGFERLELeeEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEEL 249
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
668-781 |
9.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710479 668 ELQMQLTESLKETDLLKGQLIKLQAELselQETSEQAQSKFKSEKQsrrQLELKVtslEEELADLRAEKESLEKNLSERK 747
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEEL---EEKKEKLQEEEDKLLE---EAEKEA---QQAIKEAKKEADEIIKELRQLQ 597
|
90 100 110
....*....|....*....|....*....|....
gi 961710479 748 KKsaQERCRAEEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:PRK00409 598 KG--GYASVKAHELIEARKRLNKANEKKEKKKKK 629
|
|
| |
