|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
193-286 |
9.24e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 102.27 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 193 AVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPACAAGSEGVTGW 272
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 961710477 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 961710477 184 QDLVVVEGPAVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPACA 263
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|..
gi 961710477 264 AGSEGVTGwTQSPDSILVYEVE 285
Cdd:COG0545 80 YGERGAGG-VIPPNSTLVFEVE 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
567-839 |
1.96e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntqarvlhAEQEKAKVTEELT 646
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--------LEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 727 EELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWE 806
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
250 260 270
....*....|....*....|....*....|...
gi 961710477 807 akcEHLLASAKDEHLLQYQEVCAQRDASQQELL 839
Cdd:COG1196 493 ---LLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-867 |
6.24e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 620 LQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQE 699
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 700 TSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLL 779
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 780 -KKARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQyqevcAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:COG1196 397 eLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-----EALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*....
gi 961710477 859 NEQHTKDLE 867
Cdd:COG1196 472 AALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-878 |
8.06e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 569 RIIQENERLKQ------EILEKSSRIEEQNDKISELIERNQRYVEQSNLmmekrnnsLQTATENTQARVLHAEQEKAKVT 642
Cdd:COG1196 216 RELKEELKELEaellllKLRELEAELEELEAELEELEAELEELEAELAE--------LEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKV 722
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 723 TSLEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 802
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 803 TQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLA---LQAQVTALTEQNEQHTKDLENKSHMSGVAAA 878
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
566-859 |
3.25e-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: 87.80 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 645
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELADLRAEKESLEKNLSE----RKKKSAQ------ERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLS 795
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 796 LVQAELQ-TQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQN 859
Cdd:TIGR02168 924 LAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
572-870 |
7.48e-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: 86.65 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QEN-ERLkQEILEKssrIEEQNDKISELIERNQRYVEQSNlmmEKRN----------NSLQTATENTQARVLHAEQEKAK 640
Cdd:TIGR02168 185 RENlDRL-EDILNE---LERQLKSLERQAEKAERYKELKA---ELRElelallvlrlEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 641 VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 721 KVTSLEEELADLRAEKESLEKNLSERKKKsAQERCRAEEEIDEIRKSYQEELDKLRQLLKK--ARVSTDQAAAEQLSLVQ 798
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAE-LEELESRLEELEEQLETLRSKVAQLELQIASlnNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 799 AELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKS 870
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
573-858 |
4.19e-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: 80.88 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSN-------LMMEKRN----------NSLQTATENTQARVLHAE 635
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREyegyellkekEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 636 QEKAKVTEE--------------LTAATAQVS--------RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAE 693
Cdd:TIGR02169 251 EELEKLTEEiselekrleeieqlLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 694 LSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEiRKSYQEELD 773
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-INELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 774 KLRQLLKK--ARVSTDQAAAEQLSLVQAELQTQWEAKCEHLlasAKDEHLLqyQEVCAQRDASQQELLRLQEKCLALQAQ 851
Cdd:TIGR02169 410 RLQEELQRlsEELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL--EQLAADLSKYEQELYDLKEEYDRVEKE 484
|
....*..
gi 961710477 852 VTALTEQ 858
Cdd:TIGR02169 485 LSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
565-882 |
2.24e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 565 GNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVLHAEQEKAKVTEE 644
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 645 LTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 725 LEEELADLRAEKESLEKNLSERKKKSAQercrAEEEIDEIRKSyQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQT- 803
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAAL----LEAALAELLEE-LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRg 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 804 ---------QWEAKCEHLLASAKDEhLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMSG 874
Cdd:COG1196 522 lagavavliGVEAAYEAALEAALAA-ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
....*...
gi 961710477 875 VAAAATDP 882
Cdd:COG1196 601 VDLVASDL 608
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-868 |
2.75e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 QLKVTAHQKKEAELQMQLTESLKETD--LLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLR 733
Cdd:COG1196 201 QLEPLERQAEKAERYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 734 AEKESL---EKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLlkKARVSTDQAAAEQLSLVQAELQTQWEAKCE 810
Cdd:COG1196 281 LELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 811 HL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLEN 868
Cdd:COG1196 359 ELaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
571-837 |
3.98e-13 |
|
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: 74.33 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARV------LHAEQEKAKVT-- 642
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeLEAEIASLERSia 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 ---EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQsrrqle 719
Cdd:TIGR02169 312 ekeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 720 lKVTSLEEELADLRAEKESLEKNLS---ERKKKSAQERCRAEEEIDEIR---KSYQEELDKLRQLLKKARVSTDQaAAEQ 793
Cdd:TIGR02169 386 -ELKDYREKLEKLKREINELKRELDrlqEELQRLSEELADLNAAIAGIEakiNELEEEKEDKALEIKKQEWKLEQ-LAAD 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 961710477 794 LSLVQAELQ--TQWEAKCEHLLASAKDEhllqYQEVCAQRDASQQE 837
Cdd:TIGR02169 464 LSKYEQELYdlKEEYDRVEKELSKLQRE----LAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-905 |
7.36e-13 |
|
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: 73.55 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 623 ATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE 702
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 703 QAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKK--SAQERCRA-EEEIDEIRKSYQEELDKLRQLL 779
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieQLKEELKAlREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 780 KKARVSTDQAAAEQLSLVqaELQTQWEAKCEHLLASAK---------DEHLLQYQEVCAQRDASQQELLRLQEKCLALQA 850
Cdd:TIGR02168 824 ERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAeieeleeliEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 851 QVTALTEQNEQHTKDLENKSHMsgVAAAATDpSEKVKKIMNQVFQSLRGEFELEE 905
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREK--LAQLELR-LEGLEVRIDNLQERLSEEYSLTL 953
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
673-880 |
2.08e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 673 LTESLKE--TDLLKGQLIKLQAELSELQETSEQAQSKfKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSE-RKKK 749
Cdd:COG4717 47 LLERLEKeaDELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 750 SAQERCRAEEEIDEIRKSYQEELDKLRQllKKARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDE---HLLQYQE 826
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 961710477 827 VCAQRDASQQELLRLQEKCLALQAQVTALtEQNEQHTKDLENKSHMSGVAAAAT 880
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-866 |
2.74e-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: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 626 NTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQM-------------------QLTESLKETDLLKGQ 686
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaereiaELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 687 LIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRA---EEEIDE 763
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 764 IRKSYQEELDKLRQLLKKARvstdqaaaEQLSLVQAELQTQWEAKCEHLLASAKDEHllQYQEVCAQRDASqqELLRLQE 843
Cdd:COG4913 767 LRENLEERIDALRARLNRAE--------EELERAMRAFNREWPAETADLDADLESLP--EYLALLDRLEED--GLPEYEE 834
|
250 260
....*....|....*....|...
gi 961710477 844 KCLALqaqvtaLTEQNEQHTKDL 866
Cdd:COG4913 835 RFKEL------LNENSIEFVADL 851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-741 |
6.61e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 517 TEIRMAVSKVADKMDHLMTKVEELQKhsagnslllpsmsvtmETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKIS 596
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 597 ELIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQ 656
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 657 LKVTAHQKKEAELQMQLTEslKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEK 736
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
....*
gi 961710477 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 ... |
509-935 |
1.12e-11 |
|
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: 69.37 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMET--SMIMGNIQRIIQENERLK---QEILE 583
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 584 KSSRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELTAATAQVSRLQLKV 659
Cdd:pfam05483 389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 660 TA-------HQKKEAELQMQL-TESLKETDLlKGQLIKLQAELSEL-QETSE-------QAQSKFKSEKQSRRQLElKVT 723
Cdd:pfam05483 460 TAiktseehYLKEVEDLKTELeKEKLKNIEL-TAHCDKLLLENKELtQEASDmtlelkkHQEDIINCKKQEERMLK-QIE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 724 SLEEELADLRAEKESLEKnlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLK--------KARVSTDQAAAEQLS 795
Cdd:pfam05483 538 NLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnlKKQIENKNKNIEELH 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 796 LVQAELQTQWEAKCEHL-------------LASAK---DEHLLQYQEVCAQRDASQQELLRLQEKclalqAQVTALTEQN 859
Cdd:pfam05483 615 QENKALKKKGSAENKQLnayeikvnkleleLASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEK-----AKAIADEAVK 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 860 EQHTKDLENKSHMSGVAAAAtdpsEKVKKIMNQVFQSLRGEFEL-----EESYNGRAVLGTIMNTIKMVTLQLLNQHEQD 934
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALM----EKHKHQYDKIIEERDSELGLyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIE 765
|
.
gi 961710477 935 K 935
Cdd:pfam05483 766 K 766
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-860 |
1.88e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLK------QEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 641
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 642 TEELTAATAQVSRLQLKVTAHQKKE--AELQMQL------------TESLKETDLLKGQLIKLQAELSELQETSEQAQSK 707
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEErlKEARLLLliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 708 FKSEKQSRRQLELKVTSLE-EELADLRAE---KESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEE--LDKLRQLLKK 781
Cdd:COG4717 299 SLGKEAEELQALPALEELEeEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 782 ARVSTD-------------QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLAL 848
Cdd:COG4717 379 AGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
330
....*....|..
gi 961710477 849 QAQVTALTEQNE 860
Cdd:COG4717 459 EAELEQLEEDGE 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
508-782 |
6.42e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 508 LMTEARQHNTEIRMaVSKVADKMDHLMTKVEELQKhsagnslllpsmsvtmETSMIMGNIQRI---IQENERLKQEILEK 584
Cdd:PRK03918 212 ISSELPELREELEK-LEKEVKELEELKEEIEELEK----------------ELESLEGSKRKLeekIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 585 SSRIEEQNDKISELIERNQRYVEQSNLM---------MEKRNNSLQTATENTQARVLHAEQEKAKVtEELTaataqvsrl 655
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEERIKELEEKEERL-EELK--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 qlkvtahqKKEAELQ---MQLTESLKETDL---LKGQLIKLQAELSELqeTSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:PRK03918 345 --------KKLKELEkrlEELEERHELYEEakaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 730 ADLRAEKESLEKNLSERKKksAQERCR------AEEEIDEIRKSYQEELDKLRQLLKKA 782
Cdd:PRK03918 415 GELKKEIKELKKAIEELKK--AKGKCPvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
575-802 |
1.21e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.92 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 652 VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD 731
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 732 LRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 802
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-801 |
1.45e-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: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 563 IMGNIQRIIQENERLKqEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtaTENTQARVLHAEQEKAKVT 642
Cdd:COG4913 223 TFEAADALVEHFDDLE-RAHEALEDAREQIELLEPIRELAERYAAARERLAELE-------YLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK-LQAELSELQETSEQAQSKFKSEKQSRRQLELK 721
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 722 VTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLlkKARVST----DQAA----AEQ 793
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--ERRKSNiparLLALrdalAEA 452
|
....*...
gi 961710477 794 LSLVQAEL 801
Cdd:COG4913 453 LGLDEAEL 460
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-778 |
1.82e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 506 SFLMTEARqhntEIRMAVSKVADKMDHLMTKVEELQKHsaGNSLLLPSMSVTMETSMIMGNIQRIIQENERLKQEILEKS 585
Cdd:TIGR02169 691 SSLQSELR----RIENRLDELSQELSDASRKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 586 SRIEEQNDKISEL------IER--NQRYVEQSNLMMEKRNN---SLQTATENTQARVLHAEQEKAKVTEELTAATAQVSR 654
Cdd:TIGR02169 765 ARIEELEEDLHKLeealndLEArlSHSRIPEIQAELSKLEEevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 655 LQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRA 734
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 961710477 735 EKESLEKNLS--ERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQL 778
Cdd:TIGR02169 925 KLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
579-806 |
2.66e-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: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 579 QEILEK-SSRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvteeltaATAQVSRLQL 657
Cdd:pfam01576 348 QEMRQKhTQALEELTEQL-EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK-------LEGQLQELQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 658 KVTAHQKKEAELQMQLTESLKETDLL-------KGQLIKLQAEL----SELQETSE--QAQSKFKSEKQSR-RQLELKVT 723
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVssllneaEGKNIKLSKDVssleSQLQDTQEllQEETRQKLNLSTRlRQLEDERN 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 724 SLEEELADLRAEKESLEKN-------LSERKKKsAQERCRAEEEIDEIRKSYQEELDKLRQLLKKarvstDQAAAEQLSL 796
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQlstlqaqLSDMKKK-LEEDAGTLEALEEGKKRLQRELEALTQQLEE-----KAAAYDKLEK 573
|
250
....*....|
gi 961710477 797 VQAELQTQWE 806
Cdd:pfam01576 574 TKNRLQQELD 583
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
635-856 |
5.65e-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: 64.04 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 635 EQEKAK--VTEELTAATAQVSRLQLKVT----AHQKKEAELQMQLT----ESLKETDLLKgQLIKLQAELSELQETSEqa 704
Cdd:pfam01576 205 ELEKAKrkLEGESTDLQEQIAELQAQIAelraQLAKKEEELQAALArleeETAQKNNALK-KIRELEAQISELQEDLE-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 705 qskfkSEKQSRRQLELKVTSLEEELADLRAEKESL--------------EKNLSERKKKSAQERCRAEEEIDEIRKSYQE 770
Cdd:pfam01576 282 -----SERAARNKAEKQRRDLGEELEALKTELEDTldttaaqqelrskrEQEVTELKKALEEETRSHEAQLQEMRQKHTQ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 771 ELDKLRQLL---KKARVS---TDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHllQYQEVCAQRDASQQELLRLQEK 844
Cdd:pfam01576 357 ALEELTEQLeqaKRNKANlekAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG--QLQELQARLSESERQRAELAEK 434
|
250
....*....|..
gi 961710477 845 CLALQAQVTALT 856
Cdd:pfam01576 435 LSKLQSELESVS 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
655-861 |
6.21e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 655 LQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRA 734
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 735 EKESLEKNLSERKK------------------------KSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAA 790
Cdd:COG4942 91 EIAELRAELEAQKEelaellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961710477 791 AE--QLSLVQAELQTQWEAkcehlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ 861
Cdd:COG4942 171 AEraELEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-781 |
6.89e-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: 63.50 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIER------------NQRYVEQSNL-MMEKRNNSLQTATENTQARVL 632
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldNTRESLETQLkVLSRSINKIKQNLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 633 HAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTE-----SLKETDL-----------LKGQLIKLQAELSE 696
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskiSDLEDELnkddfelkkenLEKEIDEKNKEIEE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 697 LQET---SEQAQSKFK-------SEKQS-RRQLELK---VTSLEEELADLRAEKESLE---KNLSERKKKSAQERCRAEE 759
Cdd:TIGR04523 573 LKQTqksLKKKQEEKQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKE 652
|
250 260
....*....|....*....|..
gi 961710477 760 EIDEIRKSYQEELDKLRQLLKK 781
Cdd:TIGR04523 653 TIKEIRNKWPEIIKKIKESKTK 674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-888 |
9.97e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvTEELTAATaQV 652
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAE-EL 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 653 SRLQLKVTAHQKKEAE----LQMQLTESLK--------ETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEedknMALRKAEEAKkaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 721 KVTSLEEEladlRAEKESLEKNLSERKKKSAQERCRAEEE---IDEIRKSYQEELDKLRQLLKKARvstDQAAAEQLSLV 797
Cdd:PTZ00121 1638 LKKKEAEE----KKKAEELKKAEEENKIKAAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAE---EAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 798 QAElqtqwEAKCEHLLASAKDEHLLQYQEvcAQRDASqqellrlQEKCLALQAQVTALTEQNEQHTKDLENKSHMSGVAA 877
Cdd:PTZ00121 1711 EAE-----EKKKAEELKKAEEENKIKAEE--AKKEAE-------EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
330
....*....|.
gi 961710477 878 AATDPSEKVKK 888
Cdd:PTZ00121 1777 KEAVIEEELDE 1787
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
660-832 |
1.03e-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: 60.32 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 660 TAHQKKEAELQMQLTESlkETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESL 739
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 740 EKNLSE-------------------RKKKSAQERCRAEEEIDEIRKSY---QEELDKLRQLLKKARVSTDQAAAEqlslV 797
Cdd:COG1579 79 EEQLGNvrnnkeyealqkeieslkrRISDLEDEILELMERIEELEEELaelEAELAELEAELEEKKAELDEELAE----L 154
|
170 180 190
....*....|....*....|....*....|....*
gi 961710477 798 QAELQTQwEAKCEHLLASAKDEHLLQYQEVCAQRD 832
Cdd:COG1579 155 EAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
636-807 |
1.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 636 QEKAKVTEELTAATAQVSRL--QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFksekQ 713
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL----E 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 714 SRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170
....*....|....
gi 961710477 794 LSLVQAELQTQWEA 807
Cdd:COG4717 237 EAAALEERLKEARL 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-869 |
1.46e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIE---EQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEkakvt 642
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKE----- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTaataqvSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAEL-------SELQETSEQAQS---KFKSEK 712
Cdd:TIGR04523 306 QDWN------KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNeieKLKKEN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 713 QSRRQ----LELKVTSLE--------------EELADLRAEKESLEK---NLSERKKKSAQERCRAEEEIDEIRKSYqEE 771
Cdd:TIGR04523 380 QSYKQeiknLESQINDLEskiqnqeklnqqkdEQIKKLQQEKELLEKeieRLKETIIKNNSEIKDLTNQDSVKELII-KN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 772 LDKLRQLLKKarvstdqaaaeQLSLVQAE---LQTQWEAKCEHLlaSAKDEHLLQYQEVCAQRDASQQELLRLQEKCLAL 848
Cdd:TIGR04523 459 LDNTRESLET-----------QLKVLSRSinkIKQNLEQKQKEL--KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
330 340
....*....|....*....|.
gi 961710477 849 QAQVTALTEQNEQHTKDLENK 869
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDE 546
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
600-863 |
1.52e-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: 61.23 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 600 ERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVtahqkKEAELQM-QLTESLK 678
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI-----RELELEVlKQAQSIK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 679 ETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRrqlelkvtsleeeLADLRAekesLEKNLSERKKKSAQErcrae 758
Cdd:pfam15742 108 SQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVC-------------LTDTCI----LEKKQLEERIKEASE----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 759 eEIDEIRKSYQEE------LDKLRQLLKKaRVSTDQAAAEQLSLVQAELQT---QWEAKCEHLLA--SAKDEHLLQYQEV 827
Cdd:pfam15742 166 -NEAKLKQQYQEEqqkrklLDQNVNELQQ-QVRSLQDKEAQLEMTNSQQQLriqQQEAQLKQLENekRKSDEHLKSNQEL 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 961710477 828 CAQRDASQQELLRLQEKCLALQAQVTA-LTEQNEQHT 863
Cdd:pfam15742 244 SEKLSSLQQEKEALQEELQQVLKQLDVhVRKYNEKHH 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
567-820 |
2.14e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEliernqryveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQN---------------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVSRLQLKVTAHQKKEAELQmQLTESLKE-TDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLD-NTRESLETqLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELA-------DLRAEKESLEKNLSERKKK-----SAQERCRAEEEIDEirksYQEELDKLRQ----LLKK---ARVST 786
Cdd:TIGR04523 516 TKKISslkekieKLESEKKEKESKISDLEDElnkddFELKKENLEKEIDE----KNKEIEELKQtqksLKKKqeeKQELI 591
|
250 260 270
....*....|....*....|....*....|....*
gi 961710477 787 DQAAAEQLSLV-QAELQTQWEAKCEHLLASAKDEH 820
Cdd:TIGR04523 592 DQKEKEKKDLIkEIEEKEKKISSLEKELEKAKKEN 626
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
567-746 |
4.34e-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: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIErnqryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKT------ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQEtseqaqskfksekqsrrQLELKVTSLE 726
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------------ELDEELAELE 155
|
170 180
....*....|....*....|
gi 961710477 727 EELADLRAEKESLEKNLSER 746
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-869 |
4.53e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLK----QEILEKSSRIEEQNDKISELIERNQRYveqsnlmmEKRNNSLqtatentqarvlhaEQEKAKV 641
Cdd:TIGR04523 128 KLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEEL--------ENELNLL--------------EKEKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 642 TEELTAATAQVSRLQLKVTAHQKKEA---ELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQS---- 714
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnki 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 715 -----RRQLEL-----KVTSLEE-------ELADLRAEKES-LEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLR 776
Cdd:TIGR04523 266 kkqlsEKQKELeqnnkKIKELEKqlnqlksEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 777 QLLK--KARVSTDQAAAEQLSLVQAELQT---QWEAKCEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQ 849
Cdd:TIGR04523 346 QLKKelTNSESENSEKQRELEEKQNEIEKlkkENQSYKQEIknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
330 340
....*....|....*....|...
gi 961710477 850 AQVTALTEQNEQHT---KDLENK 869
Cdd:TIGR04523 426 KEIERLKETIIKNNseiKDLTNQ 448
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
571-871 |
4.74e-09 |
|
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: 60.36 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 641
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 642 TEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQS--KFKSEKQsrrQLE 719
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKD---TIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 720 LKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKkarvSTDQAAAEQLSLVQA 799
Cdd:COG5185 388 STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS----ELNKVMREADEESQS 463
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 800 ELQtqweakcehllaSAKDEHllqYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSH 871
Cdd:COG5185 464 RLE------------EAYDEI---NRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLD 520
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-842 |
5.02e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQK-KEAELQMQLTESLKET----------DLLKGQLIKLQAELSELQETSEQAQSKFKSE 711
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRAAlrlwfaqrrlELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 712 KQSRRQLELKVTSLE-EELADLRAEKESLEKNLSERKKKSAQercraeeeideirksYQEELDKLrqllkKARVSTDQAA 790
Cdd:COG4913 322 REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRAR---------------LEALLAAL-----GLPLPASAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 961710477 791 AEQLSLVQAELQTQWEAKcEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQ 842
Cdd:COG4913 382 FAALRAEAAALLEALEEE-LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
578-864 |
6.96e-09 |
|
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: 60.35 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 578 KQEILEKSSRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATentqarvlhAEQEK-AKVTEELTAATAQVSRLQ 656
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTAL---------RQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 657 LKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQL---ELKVTSLEEELADLR 733
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 734 AEKESLEKNLSERKKKSAQercrAEEEIDEIRKSYQ------------EELDKLRQLLKKARVSTDQAA----------- 790
Cdd:COG3096 448 AKEQQATEEVLELEQKLSV----ADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQrlqqlraqlae 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710477 791 AEQLSLVQAELQTQWEAKCEHL---LASAKD-EHLLQYQEvcAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTK 864
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
575-870 |
7.06e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSSRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQArvlhaeqEKAKVTEELtaataQVSR 654
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 655 LQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ------------AQSKFKSEKQSRRQLELKV 722
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkikaAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 723 TSLEEELADLRAEKESLEKNLSER-KKKSAQERCRAEeeidEIRKSYQEELDKLRQLLKKARvsTDQAAAEQLSLVQAEl 801
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE- 1755
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 802 qtqwEAKCEHLlasaKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAqvtalteqnEQHTKDLENKS 870
Cdd:PTZ00121 1756 ----KKKIAHL----KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV---------DKKIKDIFDNF 1807
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-901 |
7.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 564 MGNIQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENT-------QARVLH 633
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAKKEELERLKKRLTgltpeklEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRL------------QLK------------VTAHQKKE--AELQMQLTESLKETDLLKGQL 687
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKEllEEYTAELKRIEKELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 688 IKLQAELSELqETSEQAQSKFKSEKQSRRQL-----ELKVTSLE-------------EELADLRAEKESLEKNLS----- 744
Cdd:PRK03918 476 RKLRKELREL-EKVLKKESELIKLKELAEQLkeleeKLKKYNLEelekkaeeyeklkEKLIKLKGEIKSLKKELEkleel 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 745 -------ERKKKSAQERCRA----------------EEEIDEIRKSYQE---------ELDKLRQLLKKARVSTDQAAAE 792
Cdd:PRK03918 555 kkklaelEKKLDELEEELAEllkeleelgfesveelEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 793 qLSLVQAELQtQWEAKCEHLLASAKDEhllQYQEVcaqrdasQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHM 872
Cdd:PRK03918 635 -LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
410 420
....*....|....*....|....*....
gi 961710477 873 SGVAAAATDPSEKVKKIMNQVfQSLRGEF 901
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERV-EELREKV 730
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
555-793 |
8.02e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.38 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 555 SVTMETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 634
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 635 EQ--EKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQ-MQLTESL---KETDL------LKGQLIKLQAEL---SELQE 699
Cdd:COG1340 85 EKlnELREELDELRKELAELNKAGGSIDKLRKEIERLEwRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 700 TSEQAQSKFKSEKQSRRQLE----------LKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcraeEEIDEIRKS-- 767
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELH----EEIIELQKElr 240
|
250 260
....*....|....*....|....*..
gi 961710477 768 -YQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:COG1340 241 eLRKELKKLRKKQRALKREKEKEELEE 267
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
565-781 |
8.59e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 565 GNIQRIIQENE----RLKQEILEKSSRIEEQNDKISELIERNQRY------VEQSNLMMEKRNNSLQTATE---NTQARV 631
Cdd:PRK03918 189 ENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELeelkeeIEELEKELESLEGSKRKLEEkirELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 632 lhaeQEKAKVTEELTAATAQVSRLQLKVTAHQKKEaELQMQLTESLKETDLLKG---QLIK-LQAELSELQETSEQAQSK 707
Cdd:PRK03918 269 ----EELKKEIEELEEKVKELKELKEKAEEYIKLS-EFYEEYLDELREIEKRLSrleEEINgIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 708 FKSEKQSRRQLElKVTSLEEELADLRAEKESLEKnlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKK 781
Cdd:PRK03918 344 KKKLKELEKRLE-ELEERHELYEEAKAKKEELER---LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
572-913 |
9.96e-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: 59.99 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKS--SRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENtqarvLHAEQEKAKVTEELTaaT 649
Cdd:pfam02463 649 RKGVSLEEGLAEKSevKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-----QREKEELKKLKLEAE--E 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 650 AQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSE-LQETSEQAQSKFKSEKQS-RRQLELKVTSLEE 727
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKELAEEREKTEKLKvEEEKEEKLKAQEE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 728 ELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDklRQLLKKARVSTDQAAAEQLSLVQAELQTQWEA 807
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 808 KCEHLLASAKDEHLLQYQEvcaqrdasQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKS----HMSGVAAAATDPS 883
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEE--------KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEeepeELLLEEADEKEKE 951
|
330 340 350
....*....|....*....|....*....|
gi 961710477 884 EKVKKIMNQVFQSLRGEFELEESYNGRAVL 913
Cdd:pfam02463 952 ENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-777 |
1.26e-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: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 614 EKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTES---------LKETDLLK 684
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 685 GQLIKLQAELSELQETSEQAQSKFKsekqsrrQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDE- 763
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELA-------ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPe 175
|
170
....*....|....
gi 961710477 764 IRKSYqeelDKLRQ 777
Cdd:COG1579 176 LLALY----ERIRK 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
566-808 |
1.39e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQArvlhAEQEKAKVT 642
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE-----QAQSKFKSEKQSRRQ 717
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 718 LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLV 797
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250
....*....|.
gi 961710477 798 QAELQTQWEAK 808
Cdd:COG4372 275 EEELEIAALEL 285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
567-778 |
1.46e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSR-IEEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQArvlhaEQEKAKVTEEL 645
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEE----FRQKNGLVDLSEEAKLL-----LQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDL--LKGQLIKLQAELSELQETS-------EQAQSKFKS-EKQSR 715
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSARYtpnhpdvIALRAQIAAlRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 716 RQLELKVTSLEEELADLRAEKESLEKNLSERKKKSA------QERCRAEEEIDEIRKSYQEELDKLRQL 778
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpeleAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-870 |
1.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 582 LEKSSRIEEQNDKISELIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQaRVLHAEQEKA 639
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLG-EVIKEIKRRI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 640 KVTEELTAATAQVSRLqlkvtahqKKEAElqMQLTESLKETDLLKGQLIKLQAELS----------ELQETSEQAQSKFK 709
Cdd:PRK03918 179 ERLEKFIKRTENIEEL--------IKEKE--KELEEVLREINEISSELPELREELEklekevkeleELKEEIEELEKELE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 710 SEKQSRRQLELKVTSLEEELADLRAEKESLEKNlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARvstdqa 789
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 790 aaEQLSLVQAELQTqweakcehllASAKDEHLlqyQEVCAQRDASQQELLRLQEKCLALQaQVTALTEQNEQHTKDLENK 869
Cdd:PRK03918 321 --EEINGIEERIKE----------LEEKEERL---EELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGL 384
|
.
gi 961710477 870 S 870
Cdd:PRK03918 385 T 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-805 |
2.75e-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: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENER----LKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 642
Cdd:COG4942 32 LQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAA--TAQVSRLQLKVTAHQKKEAELQMQLTESLKETDllKGQLIKLQAELSELQETseqaqskfksekqsRRQLEL 720
Cdd:COG4942 108 ELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAAL--------------RAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 721 KVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEElDKLRQLLKKARVSTDQAAAEQLSLVQAE 800
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 961710477 801 LQTQW 805
Cdd:COG4942 251 LKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
566-789 |
3.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELiernqryveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEel 645
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEI---------------SSELPELREELEKLEKEVKELEELKEEIEE-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 646 taataqVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ--AQSKFKSEKQSRRQlelkvt 723
Cdd:PRK03918 243 ------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELR------ 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 724 SLEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYqEELDKLRQLLKKARVSTDQA 789
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRL-EELEERHELYEEAKAKKEEL 374
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
568-864 |
5.88e-08 |
|
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: 57.22 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELta 647
Cdd:pfam15964 381 EKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEK----VTREKNSLVSQLEEAQKQLASQEMDVTKVCGEM-- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 648 ataqvsRLQLKVTAHQKKEAELQMQ--LTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSL 725
Cdd:pfam15964 455 ------RYQLNQTKMKKDEAEKEHReyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGES 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELADLRAEKESLEKNLSERKKKSAQERCRAEEEideirksyqeeldkLRQLLKKARVSTDQAAAEQLSLV--QAELQT 803
Cdd:pfam15964 529 EHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE--------------LTQKMQQMEAQHDKTVNEQYSLLtsQNTFIA 594
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 804 QWEAKCeHLLASAKDEHLLQYQEVCAQRDasqQELLRLQEKCLALQAQVTALTEQNEQHTK 864
Cdd:pfam15964 595 KLKEEC-CTLAKKLEEITQKSRSEVEQLS---QEKEYLQDRLEKLQKRNEELEEQCVQHGR 651
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-783 |
5.95e-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: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERnqryvEQSNLMMEKRNNSLQTATENTQARVLHAEQ--EKAKVTEE 644
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKL-----EKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKDEL 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 645 LTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK--LQAELSELQETSEQAQ-SKFKSEKQSRRQLELK 721
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYeeEPEELLLEEADEKEKEeNNKEEEEERNKRLLLA 968
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 722 VTSLEEELADLRAEKESLEknlsERKKKSAQERCRAEEEIDEIRksyQEELDKLRQLLKKAR 783
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKE----ERYNKDELEKERLEEEKKKLI---RAIIEETCQRLKEFL 1023
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
625-804 |
7.84e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 625 ENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKE--AELQMQLTESLKETDLLKGQLIKLQAELSELQETSE 702
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 703 QAQSKFKSEKQSRRQL--ELKVTSLEEELADLRAEKESLEKNLSERkkksAQERCRAEEEIDEIRKSYQEELDKLRQLLK 780
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180
....*....|....*....|....
gi 961710477 781 KARvstdQAAAEQLSLVQAELQTQ 804
Cdd:COG3206 320 AEL----EALQAREASLQAQLAQL 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
575-765 |
9.22e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEqsnlmMEKRNNSLQTATENTQARVLHAEQEKA--KVTEELTAATAQV 652
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 653 SRLQLKVTAHQKKEAELQmQLTESLKEtdlLKGQLIKLQAELSEL-QETSEQAQSKFKSEKQSRRQLELKVTSLEEELAD 731
Cdd:COG4717 142 AELPERLEELEERLEELR-ELEEELEE---LEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|....
gi 961710477 732 LRAEKESLEKNLSERKKKsaQERCRAEEEIDEIR 765
Cdd:COG4717 218 AQEELEELEEELEQLENE--LEAAALEERLKEAR 249
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
618-741 |
1.17e-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: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 618 NSLQTATENTQARVLHAEQEKAKVTEELTAataQVSRLQlkvTAHQKKEAELQMQlTESLKETDLLKGQLIKLQAELSEL 697
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEK---QAEIAR---EAQQNYERELVLH-AEDIKALQALREELNELKAEIAEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 961710477 698 QETSEQAQSKFKSEKQSrrqLELKVTSLEEELADLRAEKESLEK 741
Cdd:pfam07926 77 KAEAESAKAELEESEES---WEEQKKELEKELSELEKRIEDLNE 117
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-783 |
1.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaeqEKAKVT--EELTAATA 650
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL----AEAGVEdeEELRAALE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 651 QVSRLQlkvtAHQKKEAELQMQLTESLKE--TDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE- 727
Cdd:COG4717 393 QAEEYQ----ELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEd 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 728 -ELADLRAEKESLEKNLSERKKKsAQERCRAEEEIDEIRKSYQEEldKLRQLLKKAR 783
Cdd:COG4717 469 gELAELLQELEELKAELRELAEE-WAALKLALELLEEAREEYREE--RLPPVLERAS 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-942 |
1.90e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEeltaataqv 652
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA--------- 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 653 srlqLKVTAHQKKEA-ELQMQLTESLKETDLLKgqliKLQAELSELQETSEQAQSKFKSEK------QSRRQLELKVTSL 725
Cdd:PTZ00121 1383 ----AKKKAEEKKKAdEAKKKAEEDKKKADELK----KAAAAKKKADEAKKKAEEKKKADEakkkaeEAKKADEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELADlRAEKESLEKNLSERKKKSAQERCRAEE--EIDEIRKSYQEELDKLRQLLKKA---RVSTDQAAAEQLSLVQAE 800
Cdd:PTZ00121 1455 EAKKAE-EAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 801 LQTQWEAKCEHLLAS---AKDEHLLQYQEVCA---QRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMSG 874
Cdd:PTZ00121 1534 KKADEAKKAEEKKKAdelKKAEELKKAEEKKKaeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 875 VAAAATDPSEKVKKI--MNQVFQSLRGEFELEESYNGRAVLGTIMNTIKMVTLQLLNQHEQDKGQSSSEE 942
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAeeEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
191-309 |
2.14e-07 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 53.61 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 191 GPAVEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLRLKLGSgkVIKAWEDGMLGMKKGGKRLLVIPPACAAGSEGVT 270
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLID----GKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 961710477 271 GWtqSPDSILVYEVEMRRVKFARDSGSDGHSVSSRDSAA 309
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-781 |
2.25e-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: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELE 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVSRLQLKVTAHQKKEAELQMQLTESLK---------------ETDLLKGQLIKLQAELSELQETSEQAQSKFKSE 711
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaealenkiedDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL 998
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 712 KQsRRQLelkvtsLEEELADLRAEKESLEKnlserkkksaqercrAEEEID-EIRKSYQEELDKLRQLLKK 781
Cdd:TIGR02168 999 KE-RYDF------LTAQKEDLTEAKETLEE---------------AIEEIDrEARERFKDTFDQVNENFQR 1047
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-895 |
2.59e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELT--A 647
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKkkA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 648 ATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE-----------QAQSKFKSEKQSR- 715
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkkaeelkKAEEKKKAEEAKKa 1572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 716 --------------RQLELK----VTSLEEELADLRAEK-----------ESLEKNLSERKKKSAQERCRAEE--EIDEI 764
Cdd:PTZ00121 1573 eedknmalrkaeeaKKAEEArieeVMKLYEEEKKMKAEEakkaeeakikaEELKKAEEEKKKVEQLKKKEAEEkkKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 765 RKsyQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEvcaqRDASQQELLRLQEK 844
Cdd:PTZ00121 1653 KK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA----EEKKKAEELKKAEE 1726
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 845 CLALQAQVTALTEQN-----EQHTKDLENKSHMSGVAAAATDPSEKVKKIMNQVFQ 895
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEdkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
658-803 |
2.78e-07 |
|
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: 52.22 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 658 KVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQaqskFKSEKQSRRQLELKVTSLEEELADLRAEKE 737
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 738 SLEknlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKaRVstdQAAAEQLSLVQAELQT 803
Cdd:pfam13851 110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
664-779 |
2.98e-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: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSE--KQSR-----RQLELKVTSLEEELADLRAEK 736
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvLHAEdikalQALREELNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 961710477 737 ESLEKNLSERKKKSAQERCRAEEEIDEIRKSYqEELDKLRQLL 779
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
566-805 |
3.03e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIERN-----QRYVEQSNLMMEKRNNSLQTATENTQarvlhaeqekak 640
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 641 vtEELTAATAQVS-------RLQLKVTAHQKKEAELQMQL-TESLKETDLLKGQLIKLQAELS------ELQETSEQAQS 706
Cdd:PRK11281 142 --NDLAEYNSQLVslqtqpeRAQAALYANSQRLQQIRNLLkGGKVGGKALRPSQRVLLQAEQAllnaqnDLQRKSLEGNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 707 KFKSEKQSRRQL-ELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcraeEEIDEIRKS--YQEELDKLRQLLKKAR 783
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ----DEAARIQANplVAQELEINLQLSQRLL 295
|
250 260
....*....|....*....|...
gi 961710477 784 VSTDQAAaeqlSLVQAELQT-QW 805
Cdd:PRK11281 296 KATEKLN----TLTQQNLRVkNW 314
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
557-904 |
3.31e-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: 54.74 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 557 TMETSMIMGNIQRIIQE----NERLKQEILEK--SSRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQAr 630
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHqkavSERQQQEKFEKmeQERLRQEKEEKAREVERRRK--------LEEAEKARQAEMDRQAA- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 631 vLHAEQEKAKVTEEltaatAQVSRLQLKvtaHQKKEAElQMQLTESLKETDLLKgQLIKLQAELSELQETSEQAQSKFKS 710
Cdd:pfam17380 335 -IYAEQERMAMERE-----RELERIRQE---ERKRELE-RIRQEEIAMEISRMR-ELERLQMERQQKNERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 711 EKQSRRQLELKVTSLEEELADLRAEKESLEKnlsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQ--------LLKKA 782
Cdd:pfam17380 404 VKILEEERQRKIQQQKVEMEQIRAEQEEARQ---REVRRLEEERAREMERVRLEEQERQQQVERLRQqeeerkrkKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 783 RVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQH 862
Cdd:pfam17380 481 KEKRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 961710477 863 TKDLENKSHMsgvaaaatDPSEKVKKIMNQVFQSLRGEFELE 904
Cdd:pfam17380 559 RKATEERSRL--------EAMEREREMMRQIVESEKARAEYE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
566-861 |
3.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRN---NSLQTATENTQARVLHAEQEKAKVT 642
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEeleELLEQLSLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLtESLKETDLLKGQLIKLQAeLSELQETSEQAQSKFKSEKQSRRQLELKV 722
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLI-AAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 723 TSLEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYQ-------EELDKLRQLLKKARVSTDQAAAEQLS 795
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAEELEEE 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 796 LVQAELQTQWEAkcehLLASAKDEHLLQYQEVCAQrdasQQELLRLQEKCLALQAQVTALTEQNEQ 861
Cdd:COG4717 363 LQLEELEQEIAA----LLAEAGVEDEEELRAALEQ----AEEYQELKEELEELEEQLEELLGELEE 420
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
636-870 |
3.52e-07 |
|
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: 54.97 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 636 QEKAKVTEELTAaTAQVSRLQLKVTAHQK----------KEAELQMQLTESLKET---------DLLKgQLIKLQAE--- 693
Cdd:TIGR00618 163 KEKKELLMNLFP-LDQYTQLALMEFAKKKslhgkaelltLRSQLLTLCTPCMPDTyherkqvleKELK-HLREALQQtqq 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 694 ----LSELQETSEQAQSKFKSEKQSRRQLElKVTSLEEELADLRAEKEsleknlSERKKKSAQERCRAEEEIDEIRKSYQ 769
Cdd:TIGR00618 241 shayLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERIN------RARKAAPLAAHIKAVTQIEQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 770 EELDKLRQLLKKARVSTDQAAAEQLSL-VQAELQTQWEAKCEHlLASAKDEHLLQYQEVCAQRdASQQELLRLQEKCLAL 848
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSIeEQRRLLQTLHSQEIH-IRDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTL 391
|
250 260
....*....|....*....|....*..
gi 961710477 849 QAQVTAL-----TEQNEQHTKDLENKS 870
Cdd:TIGR00618 392 TQKLQSLckeldILQREQATIDTRTSA 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
572-808 |
3.73e-07 |
|
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: 54.00 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKISELiernqryveqsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAL---------------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 652 VSRLQlkvtahqKKEAELQMQLTEslkETDLLKGQLIKLQ-----AELSEL--QETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG4942 85 LAELE-------KEIAELRAELEA---QKEELAELLRALYrlgrqPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 725 LEEELADLRAEKESLEKNLsERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKK--ARVSTDQAAAEQLSLVQAELQ 802
Cdd:COG4942 155 LRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAElaAELAELQQEAEELEALIARLE 233
|
....*.
gi 961710477 803 TQWEAK 808
Cdd:COG4942 234 AEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
511-781 |
3.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQK-----HSAGNSLLLPSMSVTMETSM-IMGNIQRIIQENERLKQEILEK 584
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEKELKEIEEK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 585 SSRIEEQNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARVLHAEQEKA-KVTEELTAATAQVSRLQLKVtahq 663
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKEL---- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ---------------------AQSKFKSEKQSRRQLELKV 722
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeleerlkelepfyneylelkdAEKELEREEKELKKLEEEL 628
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 723 TSLEEELADLRAEKESLEKNLSERKKKSAQERCR-AEEEIDEIRKSYQ------EELDKLRQLLKK 781
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAglraelEELEKRREEIKK 694
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
588-860 |
6.29e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.62 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 588 IEEQNDKISELIERnQRYVEQSNLMMEkrnnslqtatentqarvlhaeqekAKVTEELTAATAQVSRLQLkvtAHQKKEA 667
Cdd:pfam00038 6 LQELNDRLASYIDK-VRFLEQQNKLLE------------------------TKISELRQKKGAEPSRLYS---LYEKEIE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 668 ELQMQLteslketDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRqlelkvtSLEEELADLR--AEKESLEKNLSE 745
Cdd:pfam00038 58 DLRRQL-------DTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRT-------SAENDLVGLRkdLDEATLARVDLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 746 RKKKSAQErcraeeEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQA--ELQTQWEAKCEHLLASAKDEHLLQ 823
Cdd:pfam00038 124 AKIESLKE------ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEIRAQYEEIAAKNREEAEEWYQSK 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 961710477 824 YQEVCAQRD-------ASQQELLRLQEKCLALQAQVTALTEQNE 860
Cdd:pfam00038 198 LEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
530-849 |
6.40e-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: 53.36 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 530 MDHLMTKVEELQKHSAGNSLLLPSMSVTMetsmimgnIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQS 609
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 610 NLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQmQLTESLKETDLLKgqlik 689
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 690 lQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQercraeeeideirksYQ 769
Cdd:pfam07888 149 -ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ---------------LQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 770 EELDKLRQLLKKA--RVSTDQAAAEQLSLVQaelqtqweakcEHLLASAKDEHLL--QYQEVCAQRDASQQEL--LRLQE 843
Cdd:pfam07888 213 DTITTLTQKLTTAhrKEAENEALLEELRSLQ-----------ERLNASERKVEGLgeELSSMAAQRDRTQAELhqARLQA 281
|
....*.
gi 961710477 844 KCLALQ 849
Cdd:pfam07888 282 AQLTLQ 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
633-869 |
7.49e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 633 HAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTEslketdlLKGQLIKLQAELselqetsEQAQSKFKSEK 712
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------LNEQLQAAQAEL-------AQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQercrAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAE 792
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----REEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 793 QLslvqAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENK 869
Cdd:COG4372 184 AL----DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
471-866 |
8.29e-07 |
|
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: 53.43 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 471 YPHASAVTSQLQPARPLYPTPLSQSPHFQGSSDMASFLM------TEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHS 544
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIReiscqqHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 545 AGNSLLLPSMSVTMETSMIMGNIQRIIQENERLKQEILEKSSRIEEQndKISELIERNQRYVEQSNLMMEKRNNSLQ--- 621
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL--EKIHLQESAQSLKEREQQLQTKEQIHLQetr 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 622 TATENTQARVLHAEQE------------KAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK 689
Cdd:TIGR00618 488 KKAVVLARLLELQEEPcplcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 690 LQAELSEL----QETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIR 765
Cdd:TIGR00618 568 IQQSFSILtqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 766 KS-YQEELDKLRQLLKKARVSTDQaaAEQLSLVQAELQtqwEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRL-QE 843
Cdd:TIGR00618 648 LHaLQLTLTQERVREHALSIRVLP--KELLASRQLALQ---KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREfNE 722
|
410 420
....*....|....*....|...
gi 961710477 844 KCLALQAQVTALTEQNEQHTKDL 866
Cdd:TIGR00618 723 IENASSSLGSDLAAREDALNQSL 745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
511-808 |
8.44e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 511 EARQHNTEIRM-AVSKV--ADKMDHLMTKVEELQKHSAGNSLLLPSMSVtmetsmiMGNIQRIIQENERLKQEILEKSsr 587
Cdd:PTZ00121 1216 EARKAEDAKKAeAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAH-------FARRQAAIKAEEARKADELKKA-- 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 588 ieEQNDKISELIERNQ-RYVEQSNLMME--KRNNSLQTATENTQ--ARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAH 662
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEkKKADEAKKKAEeaKKADEAKKKAEEAKkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 663 QKKEAELQMQltESLKETDLLK--GQLIKLQAELSE-LQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADlRAEKESL 739
Cdd:PTZ00121 1365 KAEAAEKKKE--EAKKKADAAKkkAEEKKKADEAKKkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD-EAKKKAE 1441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 740 EKNLSERKKKSAQERCRAEE---EIDEIRKSyqEELDKLRQLLKKARVSTDQaaAEQLSLVQAELQTQWEAK 808
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEakkKAEEAKKA--DEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEAK 1509
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
656-868 |
8.58e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFkseKQSRRQLE---------------- 719
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEalkddndeetretlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 720 LKVTSLEEELADLRAEKESLEKNLSERKKK--SAQERC-RAEEEIDEirksYQEELDKLRQLLKKARVSTDQAAAEQLSL 796
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQPeRAQAALYA----NSQRLQQIRNLLKGGKVGGKALRPSQRVL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 797 VQAELQtQWEAKCEHLLASAKDEHLLQ--YQevcAQRDASQQELLRLQEKCLALQAQVTA-LTEQNEQHTKDLEN 868
Cdd:PRK11281 197 LQAEQA-LLNAQNDLQRKSLEGNTQLQdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSkRLTLSEKTVQEAQS 267
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
576-866 |
9.25e-07 |
|
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: 53.22 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 576 RLKQEILEKSSRIEEQNDKISELIER-NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAE------------QEKAKVT 642
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAELQEQvTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsraqearrrqqQQTASAE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAE-------LQMQLTESLKETDLLKG------QLIKLQAELSELQETSEQAQSKFK 709
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLETTMTRVEQavaripsLSNRLSYAVRKVHTIKGlmarkvALAQLRQESCPPPPPAPPVDADLS 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 710 SEKQSRRQ--------LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEE-------EIDEIRKSYQE---E 771
Cdd:pfam07111 481 LELEQLREernrldaeLQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQEslasvgqQLEVARQGQQEsteE 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 772 LDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWeAKCEHLLASAKDEH------LLQYQEVCAQRDASQQELLRLQEKC 845
Cdd:pfam07111 561 AASLRQELTQQQEIYGQALQEKVAEVETRLREQL-SDTKRRLNEARREQakavvsLRQIQHRATQEKERNQELRRLQDEA 639
|
330 340
....*....|....*....|.
gi 961710477 846 LALQAQVTALTEQNEQHTKDL 866
Cdd:pfam07111 640 RKEEGQRLARRVQELERDKNL 660
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
634-807 |
1.32e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQET------------- 700
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraralyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 701 ---------------------------SEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQE 753
Cdd:COG3883 101 svsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 961710477 754 RcRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEA 807
Cdd:COG3883 181 E-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
576-843 |
1.58e-06 |
|
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: 51.74 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 576 RLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAkvteELTAATAQVSRl 655
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKT----SLSASVASLEK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 qlkvtahqkkeaelqmQLTESLKETDLLK------GQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:pfam15905 130 ----------------QLLELTRVNELLKakfsedGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 730 ADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRK--SYQEELDKLRQLLKKARVSTDQAAAEQLSLVQA------EL 801
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITElsCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSleekeqEL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 961710477 802 QTQWE---AKCEhLLASAKDEHLLQYQEVCAQRDASQQEL---LRLQE 843
Cdd:pfam15905 274 SKQIKdlnEKCK-LLESEKEELLREYEEKEQTLNAELEELkekLTLEE 320
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
571-898 |
1.60e-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: 52.74 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 571 IQENE-RLKQEILEKSSRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAAT 649
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 650 AQVSRlqlKVTAHQKKEAELQmQLTESLKETDLLKGQLIKLQAELSELQETS--EQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:TIGR00606 447 EILEK---KQEELKFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 728 ELADLRAEKESLEKNLSERKKKSAqercrAEEEIDEIRKSYQEEL--------------DKLRQLLKKARVSTDQAAAEQ 793
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKMD-----KDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 794 LSLVQAE-LQTQWEAKCEhllasAKDEHLLQYQ----EVCAQRDaSQQELLRLQEKCLALQAQVTALTEQNEQHTKDLEN 868
Cdd:TIGR00606 598 KELASLEqNKNHINNELE-----SKEEQLSSYEdklfDVCGSQD-EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
330 340 350
....*....|....*....|....*....|
gi 961710477 869 KSHMSGVAAAATDPSEKVKKIMNQVFQSLR 898
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAELQEFISDLQ 701
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
631-874 |
1.84e-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: 52.07 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 631 VLHAEQEKAKVTE--ELTAATAQVSRLQLKvtahqKKEAELQMQLTE-SLKETDLLKGQLIKLQAELSELQEtsEQAQSK 707
Cdd:pfam09731 235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 708 FKSEKQSRRQLELKVTSLEEELADLRAEKESleknlsERKKKSAQERCRAEEEIDEIRKSYQEeldKLRQLLKKARVSTD 787
Cdd:pfam09731 308 KREEKHIERALEKQKEELDKLAEELSARLEE------VRAADEAQLRLEFEREREEIRESYEE---KLRTELERQAEAHE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 788 QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQ-RDASQQELLRLQEKCLALQAQVTALTEQNEQHTkdL 866
Cdd:pfam09731 379 EHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANlKGLEKATSSHSEVEDENRKAQQLWLAVEALRST--L 456
|
....*...
gi 961710477 867 ENKSHMSG 874
Cdd:pfam09731 457 EDGSADSR 464
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
650-821 |
1.87e-06 |
|
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: 52.16 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 650 AQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKvtsLEEEl 729
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 730 ADLRAekeSLEKNLSERKKKSAQERCRAEE----------EIDEIRKSYQEELD-KLRQLLKKARVSTDQAAaeQLSLVQ 798
Cdd:pfam09726 478 QEARA---SAEKQLAEEKKRKKEEEATAARavalaaasrgECTESLKQRKRELEsEIKKLTHDIKLKEEQIR--ELEIKV 552
|
170 180 190
....*....|....*....|....*....|
gi 961710477 799 AELQTQWE-AKCEHLLASA------KDEHL 821
Cdd:pfam09726 553 QELRKYKEsEKDTEVLMSAlsamqdKNQHL 582
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
643-871 |
1.92e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLtESLKETDLLKGQLI---------KLQAELSELQETSEQAQSKFKSEKQ 713
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL-EQAKEGLSALNRLLprlnlladeTLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 714 SRRQLELkvtsLEEELADLRAEKESLEK-----NLSERKKKSAQERCRAEEEIDEIRK--SYQEEL----------DKLR 776
Cdd:PRK04863 916 HGNALAQ----LEPIVSVLQSDPEQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaknsdlnEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 777 QLLKKARVSTDQA------AAEQL---SLVQAELQTQWEAKCEHLLASAKDEHLLQYQ-----EVCA--QRDASQQELLR 840
Cdd:PRK04863 992 QRLEQAEQERTRAreqlrqAQAQLaqyNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsgaEERAraRRDELHARLSA 1071
|
250 260 270
....*....|....*....|....*....|....*
gi 961710477 841 LQEKCLALQAQVT----ALTEQNEQHTKdLENKSH 871
Cdd:PRK04863 1072 NRSRRNQLEKQLTfceaEMDNLTKKLRK-LERDYH 1105
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
567-791 |
2.00e-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: 51.88 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL------------------IERNQRYVEQSNL----MMEKRNNSLQTAT 624
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKkatesleeqlaaaeaeqeLEESKRETETGIQnltaEIEQGQESLTENL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 625 ENTQARV--LHAEQEKAKVTEELTAATAQVS----RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK-LQAELSEL 697
Cdd:COG5185 357 EAIKEEIenIVGEVELSKSSEELDSFKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRqIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 698 QETSEQAQSKFKSEKQSRRQLElkvtslEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:COG5185 437 EEVSKLLNELISELNKVMREAD------EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
250
....*....|....
gi 961710477 778 LLKKARVSTDQAAA 791
Cdd:COG5185 511 QLEGVRSKLDQVAE 524
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
502-749 |
2.08e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 502 SDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNSLLLPSMSVTMetsmiMGNIQRIIQEN 574
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSSRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVTEEL 645
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 646 TAATAQVSRLQLKVTAHQKKE---AELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKqsrrqlelkv 722
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA---------- 378
|
250 260
....*....|....*....|....*..
gi 961710477 723 tsleEELADLRAEKESLEKNLSERKKK 749
Cdd:PHA02562 379 ----EELAKLQDELDKIVKTKSELVKE 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-795 |
2.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 625 ENTQARVLHAEQEKAKVTEELTAATAQVSRLQlkvtaHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQA 704
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 705 QSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIrksyQEELDKLRQLLKKARV 784
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA----QEELEELEEELEQLEN 234
|
170
....*....|..
gi 961710477 785 S-TDQAAAEQLS 795
Cdd:COG4717 235 ElEAAALEERLK 246
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
588-852 |
2.34e-06 |
|
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: 50.74 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 588 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtatentqarvlhaEQEKaKVTEELTAATAQVSRLQLKVTAHQKKEA 667
Cdd:pfam09311 14 IQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKK-------------ELED-KMNQLSEETSNQVSTLAKRNQKSETLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 668 ELQMQLTESLKET----DLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRR-----------QLELKVTSLEEELADL 732
Cdd:pfam09311 80 ELQQAFSQAKRNFqdqlAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQaekfdmpdtvqELQELVLKYREELIEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 733 RAEKESLEKNLSER----KKKSAQERCRAEeeidEIRKSYQEELDKLRQLLkkARVSTDQAAAEQLSLVQAELQTQWEAK 808
Cdd:pfam09311 160 RTAADHMEEKLKAEilflKEQIQAEQCLKE----NLEETLQAEIENCKEEI--ASISSLKVELERIKAEKEQLENGLTEK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 961710477 809 CEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQV 852
Cdd:pfam09311 234 IRQLedLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
634-870 |
2.82e-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: 49.99 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRLQlkvtAHQKKEAELQMQLTESLKETDLLKGQLIKLQAelselqetSEQAQSKFKSEKQ 713
Cdd:pfam12795 11 DEAAKKKLLQDLQQALSLLDKID----ASKQRAAAYQKALDDAPAELRELRQELAALQA--------KAEAAPKEILASL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 714 SRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercRAEEEIDEIRKsyqeELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:pfam12795 79 SLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPE----RAQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 794 LSLVQAELQTQW----EAKCEHLLASAKDEhLLQyqevcAQRDASQQELLRLQEKCLALQAQVT----ALTEQNEQHTKD 865
Cdd:pfam12795 151 RWALQAELAALKaqidMLEQELLSNNNRQD-LLK-----ARRDLLTLRIQRLEQQLQALQELLNekrlQEAEQAVAQTEQ 224
|
....*
gi 961710477 866 LENKS 870
Cdd:pfam12795 225 LAEEA 229
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
641-858 |
3.20e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 641 VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 721 KVTSLEEELADLRAEKEslEKNLSERKKKSAQERCRAEEE---------------IDEIRKsYQEELDKLRQLLKKAR-V 784
Cdd:COG1340 86 KLNELREELDELRKELA--ELNKAGGSIDKLRKEIERLEWrqqtevlspeeekelVEKIKE-LEKELEKAKKALEKNEkL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 785 STDQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKE-----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
565-870 |
3.25e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 565 GNIQRIIQENERLKQEILEKSSRIEEQNDKISE---------------------LIERN--------------------- 602
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeevrdlrerleeLEEERddllaeaglddadaeavearr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 603 ----------QRYVEQSNLMMEKRNNSLQTATEN------------TQARVLHAEQEKAKVT-----EELTAATAQVSRL 655
Cdd:PRK02224 317 eeledrdeelRDRLEECRVAAQAHNEEAESLREDaddleeraeelrEEAAELESELEEAREAvedrrEEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK-----------------QSRRQl 718
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRE- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 719 elKVTSLEEELADLRAEKESLEKNLSE---------RKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKAR------ 783
Cdd:PRK02224 476 --RVEELEAELEDLEEEVEEVEERLERaedlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAeleaea 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 784 VSTDQAAAEQLSLVQAELQTQweAKCEHLLASAKD--EHLLQYQEVCAQRDASQQELLRLQEKclalqaqVTALTEQNEQ 861
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEV--AELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREK-------REALAELNDE 624
|
....*....
gi 961710477 862 HTKDLENKS 870
Cdd:PRK02224 625 RRERLAEKR 633
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
575-817 |
3.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSS-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELTA 647
Cdd:PRK02224 190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 648 ATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 728 ELADL-------RAEKESLEKNLSE-----RKKKSAQERCraEEEIDEIRKSYQ---EELDKLRQLLKKARvSTDQAAAE 792
Cdd:PRK02224 350 DADDLeeraeelREEAAELESELEEareavEDRREEIEEL--EEEIEELRERFGdapVDLGNAEDFLEELR-EERDELRE 426
|
250 260
....*....|....*....|....*..
gi 961710477 793 QLSLVQAELQTQWE--AKCEHLLASAK 817
Cdd:PRK02224 427 REAELEATLRTARErvEEAEALLEAGK 453
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
518-921 |
4.97e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 518 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSLLlpSMSVTMETSMimGNIQRIIQE-----NERLKQ------EILEKSS 586
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 587 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTEELTAAT---------- 649
Cdd:pfam05483 255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEDLQIATkticqlteek 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 650 -AQVSRLQLKVTAHQKKEAELQM---QLTESL--------KETDLLKGQLIKLQAELSELQEtseqaQSKFKSEKqsrrQ 717
Cdd:pfam05483 334 eAQMEELNKAKAAHSFVVTEFEAttcSLEELLrteqqrleKNEDQLKIITMELQKKSSELEE-----MTKFKNNK----E 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 718 LELkvtsleEELADLRAEKESLeknLSERKK--KSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVStDQAAAEQLS 795
Cdd:pfam05483 405 VEL------EELKKILAEDEKL---LDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 796 LVQAELQTQWEAKCEhlLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ-HTKDLENKSHMSG 874
Cdd:pfam05483 475 DLKTELEKEKLKNIE--LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENlEEKEMNLRDELES 552
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 961710477 875 VAAAATDPSEKVKKIMNQVFQSLRG-EFELEESYNGRAVLGTIMNTIK 921
Cdd:pfam05483 553 VREEFIQKGDEVKCKLDKSEENARSiEYEVLKKEKQMKILENKCNNLK 600
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
579-934 |
5.55e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 579 QEILEKSSRIEEQNDKISElIERNQRyveqsnlmMEKRNNSLQTATEntQARVLHAEQEKAKVTEELTAaTAQVSRLQLK 658
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLAC-IIKLQK--------TIKREKKLRETEE--VEFSLKAEVLIQKFGRSLKA-KKRFSLLKKE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 659 VTAHQ--KKEAELQMQLTE---SLKETDLLKGQLIKLQAELSEL---QETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:COG5022 868 TIYLQsaQRVELAERQLQElkiDVKSISSLKLVNLELESEIIELkksLSSDLIENLEFKTELIARLKKLLNNIDLEEGPS 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 731 DLRAEKESLEKNLSERK--KKSAQERCRA----EEEIDEIRKSyQEELDKLRQLLKKARVSTD--QAAAEQLSLVQAELQ 802
Cdd:COG5022 948 IEYVKLPELNKLHEVESklKETSEEYEDLlkksTILVREGNKA-NSELKNFKKELAELSKQYGalQESTKQLKELPVEVA 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 803 TQWEAkcEHLLASAKDEhLLQYQEVCAQRDASQQELLRLQEKCLALQAQ-----VTALTEQNEQHTKDLENKSHMSGVAA 877
Cdd:COG5022 1027 ELQSA--SKIISSESTE-LSILKPLQKLKGLLLLENNQLQARYKALKLRrenslLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 961710477 878 AATDPSEKVKKIMNQVFQSLRGEFELEESYNGRAVLgtimNTIKMVTLQL-LNQHEQD 934
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLV----NTLEPVFQKLsVLQLELD 1157
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
686-902 |
5.81e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 686 QLIKLQAELSELQEtsEQAQSKFKSEKQSR--RQLELKVTSL---------EEELADLRAEKESLEKNLSERKKKSAQER 754
Cdd:COG3096 786 RLEELRAERDELAE--QYAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 755 craeEEIDEIRksyqEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKC---EHLLASAKDEHLLQY-QEVCAQ 830
Cdd:COG3096 864 ----QQLDQLK----EQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAfiqQHGKALAQLEPLVAVlQSDPEQ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 831 RDASQQELLRLQEKCLALQAQVTALTE--QNEQH------------TKDLENK--SHMSGVAAAATDPSEKVKKI----- 889
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEvvQRRPHfsyedavgllgeNSDLNEKlrARLEQAEEARREAREQLRQAqaqys 1015
|
250
....*....|....
gi 961710477 890 -MNQVFQSLRGEFE 902
Cdd:COG3096 1016 qYNQVLASLKSSRD 1029
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
558-867 |
6.47e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 558 METSMImgniqriiqENERLKQEILEKSSrieeQNDKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAEQE 637
Cdd:PRK04863 235 MEAALR---------ENRMTLEAIRVTQS----DRDLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELRRE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 638 KAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLtESLK-------ETDLLKGQLIKLQAELSELQETSEQAQSkfks 710
Cdd:PRK04863 295 LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDY-QAASdhlnlvqTALRQQEKIERYQADLEELEERLEEQNE---- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 711 ekqsrrqlelKVTSLEEELADLRAEKEsleknlserkkksaqercRAEEEIDEIRKS---YQEELDKLR----------Q 777
Cdd:PRK04863 370 ----------VVEEADEQQEENEARAE------------------AAEEEVDELKSQladYQQALDVQQtraiqyqqavQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 778 LLKKARVSTDQA--AAEQLSLVQAELQTQWEAKCEHLLA---------SAKDEHLLQYQEVCA------QRDASQ--QEL 838
Cdd:PRK04863 422 ALERAKQLCGLPdlTADNAEDWLEEFQAKEQEATEELLSleqklsvaqAAHSQFEQAYQLVRKiagevsRSEAWDvaREL 501
|
330 340
....*....|....*....|....*....
gi 961710477 839 LRLQEKCLALQAQVTALteqnEQHTKDLE 867
Cdd:PRK04863 502 LRRLREQRHLAEQLQQL----RMRLSELE 526
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
631-800 |
9.53e-06 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 49.87 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 631 VLHAEQEKAKVTEELTAATAQvsrlQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIkLQAElSELQETSEQAQSKFKS 710
Cdd:PRK00106 21 LISIKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 711 EKQSRRQLELKVT----SL---EEELADLRAEKESLEKNLSErKKKSAQERcraEEEIDEIRKSYQEELDKLRQLlkkar 783
Cdd:PRK00106 95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
|
170
....*....|....*..
gi 961710477 784 vstDQAAAEQLSLVQAE 800
Cdd:PRK00106 166 ---SQAEAREIILAETE 179
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
578-846 |
9.79e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 578 KQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEkrnnslqtATENTQARVLHAEQEKAKVTEELTAATAQV-SRLQ 656
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE--------SSERTVSDLTASLQEKERAIEATNAEITKLrSRVD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 657 LKVT--AHQKKEAE-----------LQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQ-SKFKSEKQ-SRRQLEL- 720
Cdd:pfam15921 528 LKLQelQHLKNEGDhlrnvqteceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELq 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 721 -----------KVTSLEEELADLRAEKESLEKNLSER---KKKSAQER---------CRAE-----EEIDEIRKSYQ--- 769
Cdd:pfam15921 608 efkilkdkkdaKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERdqllnevktSRNElnslsEDYEVLKRNFRnks 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 770 EELD----KLRQLLKKARVSTDQ---------------------------AAAEQLSLVQAELQTQWEA-----KCEHLL 813
Cdd:pfam15921 688 EEMEtttnKLKMQLKSAQSELEQtrntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQFLEEAmtnanKEKHFL 767
|
330 340 350
....*....|....*....|....*....|....*
gi 961710477 814 ASAKDEHLLQYQEVCAQRD--ASQQELLRLQEKCL 846
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNkmAGELEVLRSQERRL 802
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
574-780 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 574 NErLKQEIlEKSSRIEEQNDKISELIERNQRYVEQ-----------------SNLMMEKRNNSLQTATENTQAR---VLH 633
Cdd:TIGR01612 1486 NE-LKEHI-DKSKGCKDEADKNAKAIEKNKELFEQykkdvtellnkysalaiKNKFAKTKKDSEIIIKEIKDAHkkfILE 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTE--------ELTAATAQVSR-----LQLKVTAHQKKE---AELQMQLTESLKETDLLKGQLIKL-----QA 692
Cdd:TIGR01612 1564 AEKSEQKIKEikkekfriEDDAAKNDKSNkaaidIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFsidsqDT 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 693 ELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEeladLRAEKESLEKNLSERKKKSaqeRCRAEEEIDEIRKSYQEEL 772
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE----LDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEI 1716
|
....*...
gi 961710477 773 DKLRQLLK 780
Cdd:TIGR01612 1717 ESIKELIE 1724
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
573-867 |
1.14e-05 |
|
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: 49.64 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSnlmMEKRNNSLQTATENTQ--ARVLHAEQEKAKVTEELTAATA 650
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSA---ALAGTEATSGASRSAQdlAELLSSFSGSSTTDTGLTKGSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLlkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQQ------QREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 731 DLRAEKESLEKNLsERKKKSAQERCRAEEEIdeirksyqeelDKLRQLLkkarvstdQAAAEQLslvqAELQTQWEAKCE 810
Cdd:pfam05667 374 ELKEQNEELEKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKHRV 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 811 HLLasakdEHLLQYQEVCAQR--DASQQ--ELLRLQEKCLalqaQVTALTEQNEQHTKDLE 867
Cdd:pfam05667 430 PLI-----EEYRALKEAKSNKedESQRKleEIKELREKIK----EVAEEAKQKEELYKQLV 481
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
572-776 |
1.28e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKISELIERNQR-----YvEQSNLMMEKrNNSLQtatENTQARVLHAEQEKAKVTEELT 646
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRrahfsY-EDAAEMLAK-NSDLN---EKLRQRLEQAEQERTRAREQLR 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVS-----RLQLKvTAHQKKEAELQmqltESLKETDLL-----KGQLIKLQAELSELQETSEQAQSKfksekqsRR 716
Cdd:PRK04863 1010 QAQAQLAqynqvLASLK-SSYDAKRQMLQ----ELKQELQDLgvpadSGAEERARARRDELHARLSANRSR-------RN 1077
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 717 QLELKVTSLEEELadlraekESLEKNLSERKKKSAQERcraeEEIDEIRKSYQEELDKLR 776
Cdd:PRK04863 1078 QLEKQLTFCEAEM-------DNLTKKLRKLERDYHEMR----EQVVNAKAGWCAVLRLVK 1126
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
689-861 |
1.33e-05 |
|
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: 48.02 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 689 KLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKEsleknlSERKKKSAQ----ERcraeeEIDEI 764
Cdd:pfam15397 64 QLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQianlVR-----QLQQL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 765 RKSYQEELDKLRQLLKKarvstdqaaaeqlslVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLR---- 840
Cdd:pfam15397 133 KDSQQDELDELEEMRRM---------------VLESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVMLKeieq 197
|
170 180
....*....|....*....|....*...
gi 961710477 841 -------LQEKCLALQAQVTALTEQNEQ 861
Cdd:pfam15397 198 frefideLEEEIPKLKAEVQQLQAQRQE 225
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
652-804 |
1.47e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 652 VSRLQLKVTAHQK-KEAElqmQLTESLKETDLLKGQLIKLQAELsELQETSEQAQSKFKSEKQSRR--------QLELKV 722
Cdd:PRK12704 20 IGYFVRKKIAEAKiKEAE---EEAKRILEEAKKEAEAIKKEALL-EAKEEIHKLRNEFEKELRERRnelqklekRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 723 TSLEEELADLRAEKESLEKNLS--ERKKKSAQERcraEEEIDEIrksYQEELDKLRQLlkkARVSTDQAAAEQLSLVQAE 800
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKelEQKQQELEKK---EEELEEL---IEEQLQELERI---SGLTAEEAKEILLEKVEEE 166
|
....
gi 961710477 801 LQTQ 804
Cdd:PRK12704 167 ARHE 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
606-802 |
1.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 606 VEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvtEELTAATAQVSRLQLKVTAHQKKE--AELQMQLTESLKETDLL 683
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQ--ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 684 KGQLIKLQAELSELQETSEQAQSKFK--SEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERkkKSAQERCRAEEEI 761
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEelLEALDEEELEEELEELEEELEELEEELEELREELAEL--EAELEQLEEDGEL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 961710477 762 DEIRKSYQEELDKLRQLLKKARVstDQAAAEQLSLVQAELQ 802
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAA--LKLALELLEEAREEYR 510
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
515-793 |
1.52e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 515 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMI---------MGNIQRIIQENERLKQEILEKS 585
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILllnqarlqaLEDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 586 SRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKK 665
Cdd:PLN02939 177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 666 EAELQMQLTE-SLKETDL--LKGQLIKLQAELSELQ--------ETSEQAQ-----SKFKSEK-----QSRRQLELKVTS 724
Cdd:PLN02939 256 EERVFKLEKErSLLDASLreLESKFIVAQEDVSKLSplqydcwwEKVENLQdlldrATNQVEKaalvlDQNQDLRDKVDK 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 725 LEEELADLRAEKESLEK-NLSERKKKSAQERC-RAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQ 793
Cdd:PLN02939 336 LEASLKEANVSKFSSYKvELLQQKLKLLEERLqASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
572-754 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKI---SELIERNQRYVEQSNLMMEKRNNSLqtaTENTQARVLHAEQEKAKVTEELTAA 648
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARREAREQLRQA 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 649 TAQVS----RLQLKVTAHQKKEAELQmQLTESLKEtdllkgqlIKLQAElselQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:COG3096 1011 QAQYSqynqVLASLKSSRDAKQQTLQ-ELEQELEE--------LGVQAD----AEAEERARIRRDELHEELSQNRSRRSQ 1077
|
170 180 190
....*....|....*....|....*....|
gi 961710477 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 |
2.04e-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: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 588 IEEQNDKISELIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARVLHAEQEKAKVTEELTAATAQVSRLQLK-VTA 661
Cdd:pfam15066 365 INKLKENVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVNYVHLQERyITE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 662 HQKKEAE----LQMQLTESLKEtdllkGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELkvtSLEEELAdlRAEKE 737
Cdd:pfam15066 439 MQQKNKSvsqcLEMDKTLSKKE-----EEVERLQQLKGELEKATTSALDLLKREKETREQEFL---SLQEEFQ--KHEKE 508
|
170
....*....|....*...
gi 961710477 738 SLEknlsERKK-KSAQER 754
Cdd:pfam15066 509 NLE----ERQKlKSRLEK 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
587-785 |
2.42e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 587 RIEEQNDKISEL------IERNQRYVEQsnlmMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELTAATAQVSRLql 657
Cdd:PRK04863 895 RVEEIREQLDEAeeakrfVQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRR-- 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 658 kvtAHQKKEAELQMqLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKF----------KSEKQSRRQLelkVTSLEE 727
Cdd:PRK04863 969 ---AHFSYEDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqvlaslKSSYDAKRQM---LQELKQ 1041
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 728 ELADL------------RAEKESLEKNLSE-RKKKSAQERCRA--EEEIDEIRK---SYQEELDKLRQLLKKARVS 785
Cdd:PRK04863 1042 ELQDLgvpadsgaeeraRARRDELHARLSAnRSRRNQLEKQLTfcEAEMDNLTKklrKLERDYHEMREQVVNAKAG 1117
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
577-735 |
2.66e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 577 LKQEILEKSSRIEEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRL 655
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKsEKQSR-----RQLELKVTSLEEELA 730
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAKiadlgRRLNVALAQRVQELN 193
|
....*
gi 961710477 731 DLRAE 735
Cdd:PRK09039 194 RYRSE 198
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
518-787 |
2.69e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 518 EIRMAVSKVADKMDHLMTKV----EELQKHSAgnslllpsmsvtmETSMIMGNIQRIIQENERLKQEILEKSSRIEEQN- 592
Cdd:COG1340 33 ELNEELKELAEKRDELNAQVkelrEEAQELRE-------------KRDELNEKVKELKEERDELNEKLNELREELDELRk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 593 ------------DKISELIERNQRYVEQSNLMMEKRNNSLQTATEntQARVLHAEQEKAKVTEELTAATAQVSRLQLKVT 660
Cdd:COG1340 100 elaelnkaggsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKE--LEKELEKAKKALEKNEKLKELRAELKELRKEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 661 AHQKKEAELQMQLTEslketdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLe 740
Cdd:COG1340 178 EIHKKIKELAEEAQE-------LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 961710477 741 knlseRKKKSAQERCRAEEEIDEIRKsyqEELDKLRqllKKARVSTD 787
Cdd:COG1340 250 -----RKKQRALKREKEKEELEEKAE---EIFEKLK---KGEKLTTE 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
686-869 |
2.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 686 QLIKLQAELSELQETseqaqskfkseKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercRAEEEIDEIR 765
Cdd:COG1579 8 ALLDLQELDSELDRL-----------EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK----RLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 766 ksyqEELDKLRQLLKKARvstdqaAAEQLSLVQAELqtqweakcehllASAKDEhllqyqevcaqRDASQQELLRLQEKC 845
Cdd:COG1579 73 ----ARIKKYEEQLGNVR------NNKEYEALQKEI------------ESLKRR-----------ISDLEDEILELMERI 119
|
170 180
....*....|....*....|....
gi 961710477 846 LALQAQVTALTEQNEQHTKDLENK 869
Cdd:COG1579 120 EELEEELAELEAELAELEAELEEK 143
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
550-868 |
3.25e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 550 LLPSMSVTMETSMImgniqRIIQENERLKQEILEKSSRIEEQ--NDKISELIERNQryvEQSNLMMEKRNNSLQTA-TEN 626
Cdd:TIGR00618 172 LFPLDQYTQLALME-----FAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQ---VLEKELKHLREALQQTQqSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 627 TQARVLHAEQEKAKVTEELTAATAQVSRL--QLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQET---- 700
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELraQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKmrsr 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 701 -----SEQAQSKFKSEKQSRRQLELKVTSLEEELADlRAEKESLEKnlserkkksaQERCRAEEEIDEIRKsYQEELDKL 775
Cdd:TIGR00618 324 akllmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD-AHEVATSIR----------EISCQQHTLTQHIHT-LQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 776 RQLLKKARVSTDQAAAEQlslVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTAL 855
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQ---ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
330
....*....|...
gi 961710477 856 TEQNEQhTKDLEN 868
Cdd:TIGR00618 469 KEREQQ-LQTKEQ 480
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
671-780 |
3.36e-05 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 47.03 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 671 MQLTESLKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKS 750
Cdd:COG4026 131 NELREELLE---LKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKR 207
|
90 100 110
....*....|....*....|....*....|
gi 961710477 751 AQERCRAEEEIDEIrksYQEELDKLRQLLK 780
Cdd:COG4026 208 LLEVFSLEELWKEL---FPEELPEEDFIYF 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-777 |
3.57e-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: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNL-MMEKRNNSLQTATENTQAR----------VLHAE 635
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYsWDEIDVASAEREIAELEAElerldassddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 636 QEKAKVTEELTAATAQVSRLqlkvtahQKKEAELQMQLTESLKETDLLKGQLikLQAELSELQETSEQAQSKFKSEKQSR 715
Cdd:COG4913 692 EQLEELEAELEELEEELDEL-------KGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 716 RQLELKvTSLEEELADLRAEKESLEKNLsERKKKSAQERCRAE-----EEIDEIRkSYQEELDKLRQ 777
Cdd:COG4913 763 VERELR-ENLEERIDALRARLNRAEEEL-ERAMRAFNREWPAEtadldADLESLP-EYLALLDRLEE 826
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
634-870 |
4.13e-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: 48.04 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVS------RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSK 707
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIidleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 708 fksekQSRRQLELKVTSLEEELADLRAEKESLEknlsERKKKSAQERcraEEEIDEIRKSYQEELDKLRQLLKKARvstD 787
Cdd:pfam02463 250 -----QEEIESSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEE---LKLLAKEEEELKSELLKLERRKVDDE---E 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 788 QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRL--------QEKCLALQAQVTALTEQN 859
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLeqleeellAKKKLESERLSSAAKLKE 394
|
250
....*....|.
gi 961710477 860 EQHTKDLENKS 870
Cdd:pfam02463 395 EELELKSEEEK 405
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
575-858 |
4.27e-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: 48.02 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSL-------QTATENTQARVLHAEQ-----EKAK-- 640
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEA-AEEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARal 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 641 ----------VTEELTAATAQV-----------SRLQLKVTAHQKKEAELQM------------------QLTESLKETD 681
Cdd:COG3096 429 cglpdltpenAEDYLAAFRAKEqqateevleleQKLSVADAARRQFEKAYELvckiageversqawqtarELLRRYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 682 LLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTS---LEEELADLRAEKESLEKNLSErkkkSAQERCRAE 758
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAaeeLEELLAELEAQLEELEEQAAE----AVEQRSELR 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 759 EEIDEIRKsyqeeldKLRQLLKKARV-STDQAAAEQLS-----------LVQAELQTQWEAkcEHLLASAKDehllqyqE 826
Cdd:COG3096 585 QQLEQLRA-------RIKELAARAPAwLAAQDALERLReqsgealadsqEVTAAMQQLLER--EREATVERD-------E 648
|
330 340 350
....*....|....*....|....*....|..
gi 961710477 827 VCAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:COG3096 649 LAARKQALESQIERLSQPGGAEDPRLLALAER 680
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
663-784 |
4.41e-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: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 663 QKKEAELQMQLTESLKETDLL-KGQLIKLQAELSELQETSEQAQSKFKSEKQsrrqLELKVTSLEEELADLRAEKESLEK 741
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 742 NLSERKKKSAQERCRAEEEIDE--------------IRKSYQEELDKLRQL---LKKaRV 784
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
634-801 |
6.58e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLK--ETDLLK---GQLIKLQAELSELQETSEQAQskf 708
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEkgREDLARealERKAELEAQAEALEAQLAQLE--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 709 ksekQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKkksAQERCR----------AEEEIDEIRKSYQEELDK---L 775
Cdd:COG1842 112 ----EQVEKLKEALRQLESKLEELKAKKDTLKARAKAAK---AQEKVNealsgidsddATSALERMEEKIEEMEARaeaA 184
|
170 180
....*....|....*....|....*.
gi 961710477 776 RQLLKKARVSTDQAAAEQLSLVQAEL 801
Cdd:COG1842 185 AELAAGDSLDDELAELEADSEVEDEL 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
571-776 |
7.45e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 571 IQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATA 650
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAE------LSELQETSEQAQSKFKSEKQSRRQLELKVTS 724
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERieslerIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 961710477 725 LEEELADLRAEKESLEKNLSERKKKSAQE-RCRAEEEIDEIrksyQEELDKLR 776
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEAREdKERAEEYLEQV----EEKLDELR 673
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
517-777 |
7.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 517 TEIRMAVSKVADKMDHLMTKVEEL-QKHSAGNSLllpsmsVTMETsmimgNIQRIIQENERLKQEILEKSSRIEEQNDKI 595
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVeERLERAEDL------VEAED-----RIERLEERREDLEELIAERRETIEEKRERA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 596 SELIERNQRYVEQsnlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELTA-------------ATAQVSRLQLKvt 660
Cdd:PRK02224 540 EELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKERIESlerirtllaaiadAEDEIERLREK-- 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 661 ahQKKEAELQMQLTESLKETDLLKGQLiklQAELSElqETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLE 740
Cdd:PRK02224 615 --REALAELNDERRERLAEKRERKREL---EAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 961710477 741 KNLSER-----KKKSAQERCRAEE----EIDEIRKSYQEELDKLRQ 777
Cdd:PRK02224 688 NELEELeelreRREALENRVEALEalydEAEELESMYGDLRAELRQ 733
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
625-911 |
8.35e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 625 ENTQARvlhaEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQL---TESLKETDLLKGQLIKLQAELSE----L 697
Cdd:pfam01576 5 EEMQAK----EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQELEEilheL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 698 QETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRA--EKESLEKNLSERKKKSAQERCRAEEEideirksYQEELDKL 775
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAarQKLQLEKVTTEAKIKKLEEDILLLED-------QNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 776 RQLLKK--ARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQyQEVCAQRDASQQELLRLQEKCLALQAQVT 853
Cdd:pfam01576 154 RKLLEEriSEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 854 ALTEQNEQHTKDLEN-KSHMSGVAAAATDPSEKVKKIMNQVFQsLRGEFELEESYNGRA 911
Cdd:pfam01576 233 ELRAQLAKKEEELQAaLARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNKA 290
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
643-782 |
1.01e-04 |
|
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: 44.67 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 643 EELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQsrrQLELKV 722
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKD---QALADL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 723 TSLEEELADL--RAE--KESLE--KNLSERKKKSAQERC----------------------RAEEEIDEIRKSYQEELDK 774
Cdd:pfam05010 85 NSVEKSFSDLfkRYEkqKEVISgyKKNEESLKKCAQDYLarikkeeqryqalkahaeekldQANEEIAQVRSKAKAETAA 164
|
....*...
gi 961710477 775 LRQLLKKA 782
Cdd:pfam05010 165 LQASLRKE 172
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
607-861 |
1.33e-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: 46.10 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 607 EQSNLMMEKRNNSLQTATentqarVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTEslketdllkgq 686
Cdd:pfam15709 287 EESQVSIDGRSSPTQTFV------VTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLE----------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 687 likLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEE--LADLRAEKESLEKNLSERKK----KSAQERCRAEEE 760
Cdd:pfam15709 350 ---VERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQrlqlQAAQERARQQQE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 761 idEIRKSYQEeldkLRQllKKARVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKDEHL--LQYQEVCAQRDASQQEL 838
Cdd:pfam15709 427 --EFRRKLQE----LQR--KKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEERLeyQRQKQEAEEKARLEAEE 496
|
250 260
....*....|....*....|...
gi 961710477 839 LRLQEKCLALQAQVTALTEQNEQ 861
Cdd:pfam15709 497 RRQKEEEAARLALEEAMKQAQEQ 519
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
514-740 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 514 QHNTEIRMAVSKVADkmdhlmTKVEELQKHSAGNSLLLPSMSVTMETSMIMGNIQ-------RIIQENERLKQEILEKSS 586
Cdd:pfam15921 615 KKDAKIRELEARVSD------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKtsrnelnSLSEDYEVLKRNFRNKSE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 587 RIEEQNDKISELIERNQRYVEQSNlmmekrnNSLQTaTENTQArvlHAEQEKAKVTEELTAATAQVSRLQLKVTAhqkke 666
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTR-------NTLKS-MEGSDG---HAMKVAMGMQKQITAKRGQIDALQSKIQF----- 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 667 aeLQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELadlraEKESLE 740
Cdd:pfam15921 753 --LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL-----DKASLQ 819
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
689-783 |
1.41e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 689 KLQAELSELQETSEQAQSKFKSEKQSR-RQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRK- 766
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREi 467
|
90
....*....|....*...
gi 961710477 767 -SYQEELDKLRQLLKKAR 783
Cdd:COG2433 468 sRLDREIERLERELEEER 485
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
559-777 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 559 ETSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISEL-IERNQRYVEQS---NLMMEKRNNSLQTATENTQARVLHA 634
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEqAEWKELEKEEEreeDERILEYLKEKAEREEEREAEREEI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 635 EQEKAKVTEELTAATAQVS---------RLQLKVTAHQKKEAELQMQLTESLKEtdllkgQLIKLQAELSELQETSEQAQ 705
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQdekaerdelRAKLYQEEQERKERQKEREEAEKKAR------QRQELQQAREEQIELKERRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 706 SKFKSEKQSRRQLELKVTSLEEELADLRAEK---------ESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLR 776
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmkrlehrRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIE 332
|
.
gi 961710477 777 Q 777
Cdd:pfam13868 333 E 333
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
623-783 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 623 ATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSE 702
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 703 QAQSKfksEKQSRRQLELKVTSLEEELADLRAEKESLEK-NLserkkksaqercRAEEEIDEIRKSYqEELDKLRQLLKK 781
Cdd:COG1196 746 ELLEE---EALEELPEPPDLEELERELERLEREIEALGPvNL------------LAIEEYEELEERY-DFLSEQREDLEE 809
|
..
gi 961710477 782 AR 783
Cdd:COG1196 810 AR 811
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
567-874 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELt 646
Cdd:pfam15921 269 IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 aataqvsrlqlkvtahQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQL-------E 719
Cdd:pfam15921 348 ----------------EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 720 LKVTSLEEELADLRAEKESLEKNLS----------ERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKK--ARVSTD 787
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKamksecqgqmERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 788 QAAAEQLSLVQAELQTQWEA--KCEHLLASAKDEHLLQYQEVcaQRDASQQELLR-LQEKCLALQAQVTALTEQNEQHTK 864
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAieATNAEITKLRSRVDLKLQEL--QHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQ 569
|
330
....*....|
gi 961710477 865 DLENKSHMSG 874
Cdd:pfam15921 570 QIENMTQLVG 579
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
567-754 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQT--ATENTQARVLHAeqekakv 641
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRsgGSVSYLDVLLGS------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 642 tEELTAATAQVSRLQlKVTAHQKKEAELQMQLTESLKET-DLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLEL 720
Cdd:COG3883 112 -ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190
....*....|....*....|....*....|....
gi 961710477 721 KVTSLEEELADLRAEKESLEKNLSERKKKSAQER 754
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
672-880 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 672 QLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKK--- 748
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 749 ---------------KSAQERCRAEEEIDEIRKSYQEELDKLRQLlkKARVSTDQAAAEQLSLVQAELQTQWEAKcEHLL 813
Cdd:COG3883 97 rsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKAD--KAELEAKKAELEAKLAELEALKAELEAA-KAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 814 ASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMSGVAAAAT 880
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| 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 961710477 194 VEVGDSLEVAYTSWLLQnhvlGQVLDSTANKDKLLrLKLGSGKVIKAWEDGMLGMKKGGKRLLVIPPA 261
Cdd:COG1047 1 IEKGDVVTLHYTLKLED----GEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPE 63
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
628-776 |
1.60e-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: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 628 QARVLHAEQEKakvteeLTAATAQVSRLQLKVTAHQKKEAELQMQLTESlketdllkgQLIKLQAELSELQETSEQAQSK 707
Cdd:pfam08614 15 RTALLEAENAK------LQSEPESVLPSTSSSKLSKASPQSASIQSLEQ---------LLAQLREELAELYRSRGELAQR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 708 FKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERkkksaqercraEEEIDEIRKSY---QEELDKLR 776
Cdd:pfam08614 80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR-----------EEELREKRKLNqdlQDELVALQ 140
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
664-802 |
1.60e-04 |
|
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: 43.05 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 664 KKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQ----------SKFKSEKQSRRQlelKVTSLEEELADLR 733
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAIleaenskaevETLKAEIEEMAQ---NLRDLELDLVTLR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 734 AEKESLEKNLSERKkksaqercraeEEIDEIRKSyQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQ 802
Cdd:pfam10473 80 SEKENLTKELQKKQ-----------ERVSELESL-NSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
586-804 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 586 SRIEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQ--LKVTAHQ 663
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 664 KKEAELQMQLTESLKE----TDLLKGQLI---------KLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA 730
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfSDFLDRLSAlskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 731 DLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQ 804
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
572-803 |
1.73e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENT--QARV------LHAEQEKA 639
Cdd:PTZ00440 560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNdlQEKVkyilnkFYKGDLQE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 640 KVTEELTAATAQVSRLQlkvTAHQKKEaeLQMQLTESLKETDLLK-------GQLIK-LQAELSELQETSEQAQSKF--- 708
Cdd:PTZ00440 640 LLDELSHFLDDHKYLYH---EAKSKED--LQTLLNTSKNEYEKLEfmksdniDNIIKnLKKELQNLLSLKENIIKKQlnn 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 709 --KSEKQSRRQLELKVTSLEEELADLRAEKESLE---KNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKAR 783
Cdd:PTZ00440 715 ieQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKEN 794
|
250 260
....*....|....*....|..
gi 961710477 784 VSTDQAAA--EQLSLVQAELQT 803
Cdd:PTZ00440 795 KISNDINIlkENKKNNQDLLNS 816
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
669-861 |
1.95e-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: 43.99 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 669 LQMQLTESLKETDLLKGQLIKlqaELSELQETSEQAQSKFKSEKQS-RRQLELKvtslEEELADLRAEKESLEkNLSERK 747
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQ---ECEEIERRRQELASRYTQQTAElQTQLLQK----EKEQASLKKELQALR-PFAKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 748 KKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQT-QWEAKCEHLLASAKDEHLLQYQE 826
Cdd:pfam14988 81 ESQEREIQDLEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQELRILELGERATrELKRKAQALKLAAKQALSEFCRS 160
|
170 180 190
....*....|....*....|....*....|....*
gi 961710477 827 VCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ 861
Cdd:pfam14988 161 IKRENRQLQKELLQLIQETQALEAIKSKLENRKQR 195
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-851 |
2.03e-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: 44.91 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 571 IQENERLKQEILEKSSRIEEQNDKisELIERNQRYVEQSNLMMEKRNNSLQTA----TENTQARVL---HAEQEKAKVTE 643
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEE--ERERALEEEEEKEEERKEERKRYRQELeeqiEEREQKRQEeyeEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 644 ELTAATAQVSRLQLKvtaHQKKEAELQMQLTESLKETDLLKGQLIKLQAE--------LSELQETSEQAQSKFKSEKQSR 715
Cdd:pfam13868 106 IVERIQEEDQAEAEE---KLEKQRQLREEIDEFNEEQAEWKELEKEEEREederileyLKEKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 716 RQLELKVTSLEEELADLRAEKESL------EKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDkLRQLLKKARVSTDQA 789
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDELraklyqEEQERKERQKEREEAEKKARQRQELQQAREEQIE-LKERRLAEEAEREEE 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 790 AAEQLSLVQAELQTQW---EAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQ 851
Cdd:pfam13868 262 EFERMLRKQAEDEEIEqeeAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
568-806 |
2.38e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLkqeiLEKSSRIEEQNDK---ISELIER-NQRYVEQSNLM--MEKRNNSLQTAT---ENTQARVLHAEQ-- 636
Cdd:PRK10929 109 QEILQVSSQL----LEKSRQAQQEQDRareISDSLSQlPQQQTEARRQLneIERRLQTLGTPNtplAQAQLTALQAESaa 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 637 EKAKVTE----ELTAATAQ-VSRLQLKVtaHQKKEAELQMQLT---------------ESLKETDLLK---GQL------ 687
Cdd:PRK10929 185 LKALVDElelaQLSANNRQeLARLRSEL--AKKRSQQLDAYLQalrnqlnsqrqreaeRALESTELLAeqsGDLpksiva 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 688 -IKLQAELSelQETSEQAQSKFKSEKQSRR------QLELKVTSLEEE---LADLRAEKESLEKNLS---ERKKKSAQER 754
Cdd:PRK10929 263 qFKINRELS--QALNQQAQRMDLIASQQRQaasqtlQVRQALNTLREQsqwLGVSNALGEALRAQVArlpEMPKPQQLDT 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 961710477 755 CRAEEEIDEIRksYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWE 806
Cdd:PRK10929 341 EMAQLRVQRLR--YEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
726-812 |
2.38e-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: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELADLRAEKEslEKNLSERKKKSAQERCRAEEEiDEIRKsyqEELDKLRQLLKKARvstdqAAAEQLSLVqAELQTQW 805
Cdd:pfam15927 5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72
|
....*....
gi 961710477 806 E--AKCEHL 812
Cdd:pfam15927 73 EryMRCDGL 81
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
568-840 |
2.50e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.36 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLKQEILEKSSRieeqndkiseliernqryveqsnlmmekrnNSLQTATENTqARVLHAEQEKAKVTEELTA 647
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGV------------------------------EGLDSSTALT-LELEELRQERDLLREEIQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 648 ATAQVSRLQlkvtahqkkeaeLQMQLTESlketdllkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEE 727
Cdd:pfam09787 66 LRGQIQQLR------------TELQELEA------------QQQEEAESSREQLQELEEQLATERSARREAEAELERLQE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 728 EladLRAEKESLeknlsERKKKSAQERCRAEEeideirksyqEELDKLR-QLLKKARVSTDQAAAE----QL--SLVQAe 800
Cdd:pfam09787 122 E---LRYLEEEL-----RRSKATLQSRIKDRE----------AEIEKLRnQLTSKSQSSSSQSELEnrlhQLteTLIQK- 182
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 961710477 801 lQTQWEAkcehlLASAKDEHLLQYQEVCAQRDASQQELLR 840
Cdd:pfam09787 183 -QTMLEA-----LSTEKNSLVLQLERMEQQIKELQGEGSN 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
656-825 |
2.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 656 QLKVTAHQKKEAELQMQLTESLKETD-LLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLra 734
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 735 EKESLEKNLSERKKKSAqercRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAK--CEHL 812
Cdd:COG4717 426 DEEELEEELEELEEELE----ELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALklALEL 501
|
170
....*....|...
gi 961710477 813 LASAKDEHLLQYQ 825
Cdd:COG4717 502 LEEAREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
567-772 |
2.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKS-SRIEEQNDKISELIERNQRYVEQSNLMMEKRNNslqtatentqarvlhaEQEKAKVTEEL 645
Cdd:PRK03918 565 LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELERE----------------EKELKKLEEEL 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 646 TAATAQVSRLQLKVTAHQKKEAELQMQLTEslKETDLLKGQLIKLQAELSELQEtseqaqsKFKSEKQSRRQLELKVTSL 725
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRA-------ELEELEKRREEIKKTLEKL 699
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 726 EEELADLRAEKESLEK---------NLSER-KKKSAQERCRAEEEIDEIRKSYQEEL 772
Cdd:PRK03918 700 KEELEEREKAKKELEKlekalerveELREKvKKYKALLKERALSKVGEIASEIFEEL 756
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
580-754 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 580 EILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELtaATAQVSrlq 656
Cdd:pfam05911 664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlesTKSQLQESEQLIAELRSEL--ASLKES--- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 657 lkvtahqKKEAELQMQ-LTESLKETDLlkgQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELAdlRAE 735
Cdd:pfam05911 739 -------NSLAETQLKcMAESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNE 806
|
170 180
....*....|....*....|
gi 961710477 736 KESLEKNL-SERKKKSAQER 754
Cdd:pfam05911 807 KKESSNCDaDQEDKKLQQEK 826
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
713-823 |
3.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDK-LRQLLKKARVSTDQAAA 791
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYASVKA 606
|
90 100 110
....*....|....*....|....*....|..
gi 961710477 792 EQLSLVQAELQTQWEAKCEHLLASAKDEHLLQ 823
Cdd:PRK00409 607 HELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
553-936 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 553 SMSvTMETSMIMGNIQRIIQEnerLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnLMMEKRNNSLQTATENtqarvl 632
Cdd:pfam15921 209 SMS-TMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQNKIEL--LLQQHQDRIEQLISEH------ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 633 haEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKEtdlLKGQLIKLQAELSELQETSEQ--------- 703
Cdd:pfam15921 277 --EVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD---LESTVSQLRSELREAKRMYEDkieelekql 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 704 --AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLS---ERKKKSAQERCRAEEEIDEIRKSYQE---ELDKL 775
Cdd:pfam15921 352 vlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 776 RQLLKKARVSTDQAAAEQLSLVQAelqtqweakcehllasaKDEHLLQYQEVCAQRDASQQELLRLQEKclaLQAQVTAL 855
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQG-----------------KNESLEKVSSLTAQLESTKEMLRKVVEE---LTAKKMTL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 856 tEQNEQHTKDLENKSHMSGVAAAATDpsEKVKKIMNQV------FQSLRGEFE-----------LEESYNGR-AVLGTIM 917
Cdd:pfam15921 492 -ESSERTVSDLTASLQEKERAIEATN--AEITKLRSRVdlklqeLQHLKNEGDhlrnvqteceaLKLQMAEKdKVIEILR 568
|
410
....*....|....*....
gi 961710477 918 NTIKMVTlQLLNQHEQDKG 936
Cdd:pfam15921 569 QQIENMT-QLVGQHGRTAG 586
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-787 |
3.68e-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: 44.50 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 517 TEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMIM--GNIQRIiQENERLKQEILEKSSRIEEQNDK 594
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQraAHEARI-RELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 595 ISELIER--NQRYVEQSnlmmEKRNnsLQTATENTQA--RVLHAEQEKAKVTEELTAATAQ-----VSRLQLKVTAHQKK 665
Cdd:pfam07888 155 MKERAKKagAQRKEEEA----ERKQ--LQAKLQQTEEelRSLSKEFQELRNSLAQRDTQVLqlqdtITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 666 EAE----------LQMQLTESLKETDLLKGQL----------------IKLQA-----ELSELQETSEQAQSKFKSEKQS 714
Cdd:pfam07888 229 EAEnealleelrsLQERLNASERKVEGLGEELssmaaqrdrtqaelhqARLQAaqltlQLADASLALREGRARWAQERET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 715 RRQ-----------LELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSY--------------Q 769
Cdd:pfam07888 309 LQQsaeadkdriekLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaqkekeqlqaekQ 388
|
330
....*....|....*...
gi 961710477 770 EELDKLRQLLKKARVSTD 787
Cdd:pfam07888 389 ELLEYIRQLEQRLETVAD 406
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
514-710 |
4.02e-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: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 514 QHNTEIRMAVSKVADKMDHLMTKVEE---LQKHSAgnslllpsmsvTMETSmimgniqriIQENERLKQEILEK----SS 586
Cdd:pfam15665 22 AHEEEIQQILAETREKILQYKSKIGEeldLKRRIQ-----------TLEES---------LEQHERMKRQALTEfeqyKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 587 RIEEQNDKISEliERNQRYVEQSNLMMEKRNNSLQTATENTQARVlHAEQEKAKVTEELTAATAQ-VSRLQLKVTAHQKK 665
Cdd:pfam15665 82 RVEERELKAEA--EHRQRVVELSREVEEAKRAFEEKLESFEQLQA-QFEQEKRKALEELRAKHRQeIQELLTTQRAQSAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 961710477 666 EAELQMQLTESLK-ETDLLKGQLIKLQAELSELQETSEQAQSKFKS 710
Cdd:pfam15665 159 SLAEQEKLEELHKaELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
514-868 |
4.20e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 514 QHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMEtsMIMGNIQRIIQE-------NERLKQEILEKSS 586
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP--GRQSIIDLKEKEipelrnkLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 587 RIEEQNDKISEL----------------IERNQRYVEQSNLMMEKRNNSLQTAteNTQARVLHAEQEKAKVTEELTAATA 650
Cdd:TIGR00606 766 DIEEQETLLGTImpeeesakvcltdvtiMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 651 QVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQlelkVTSLEEELA 730
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 731 DLRAEKESLEKNLSERKKKSAQERCRAEEEIDEI---RKSYQEELD--KLRQLL-KKARVSTDQAAAEQLSLVQAELQTQ 804
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQdgKDDYLKqKETELNTVNAQLEECEKHQEKINED 999
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 805 WEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTaLTEQNEQHTKDLEN 868
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ-VLQMKQEHQKLEEN 1062
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
569-862 |
4.58e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 569 RIIQ-ENERLKQEILEKSSRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQarvlhaEQEKAKvtEELTA 647
Cdd:pfam05557 10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLE------KREAEA--EEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 648 ATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDL-LKGQLIKLQ--------------AELSELQETSEQAQSKFKSEK 712
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVIScLKNELSELRrqiqraelelqstnSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 713 QSRRQLELKVTSL---EEELADLRAEKESLEKNLSERKK-KSAQERC--------RAEEEIDEIRKS------YQEELDK 774
Cdd:pfam05557 153 QLRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNsKSELARIpelekeleRLREHNKHLNENienkllLKEEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 775 LRQLLKKARVSTDQAAAEQLSL--VQAELQtQWE----AKCEHL----LASAKDEHLLQYQEVCAQR------DASQQEL 838
Cdd:pfam05557 233 LKRKLEREEKYREEAATLELEKekLEQELQ-SWVklaqDTGLNLrspeDLSRRIEQLQQREIVLKEEnssltsSARQLEK 311
|
330 340
....*....|....*....|....*.
gi 961710477 839 LR--LQEKCLALQAQVTALTEQNEQH 862
Cdd:pfam05557 312 ARreLEQELAQYLKKIEDLNKKLKRH 337
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
568-860 |
4.70e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVE--------QSNLM----MEK-------RNNSLQTATENTQ 628
Cdd:pfam05557 145 KAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseivknsKSELAripeLEKelerlreHNKHLNENIENKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 629 ARVLHAEQEKAKVtEELTAATAQVSRLQLKVTahqKKEAELQ------MQLTESLKETDLLKGQLIKLQaelselQETSE 702
Cdd:pfam05557 225 LLKEEVEDLKRKL-EREEKYREEAATLELEKE---KLEQELQswvklaQDTGLNLRSPEDLSRRIEQLQ------QREIV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 703 QAQSKFKSEKQSRrQLELKVTSLEEELADLRAEKESLEKNLSERK--KKSAQERCR-AEEEID---EIRKSYQEEL---D 773
Cdd:pfam05557 295 LKEENSSLTSSAR-QLEKARRELEQELAQYLKKIEDLNKKLKRHKalVRRLQRRVLlLTKERDgyrAILESYDKELtmsN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 774 KLRQLLKKARVSTD--QAAAEQLSLVQAEL-QTQWEAKCEHLLASAKDEHL--LQYQEVCAQRDASQQELLRLQEKCLAL 848
Cdd:pfam05557 374 YSPQLLERIEEAEDmtQKMQAHNEEMEAQLsVAEEELGGYKQQAQTLERELqaLRQQESLADPSYSKEEVDSLRRKLETL 453
|
330
....*....|..
gi 961710477 849 QAQVTALTEQNE 860
Cdd:pfam05557 454 ELERQRLREQKN 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
726-867 |
5.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 726 EEELADLRAEKESLEKNLSErkkksAQERCraeEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAeqlslvQAELQtQW 805
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-----AEERL---EALEAELDALQERREALQRLAEYSWDEIDVASA------EREIA-EL 673
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 806 EAKCEHLLASAKDehLLQYQEvcaQRDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLE 867
Cdd:COG4913 674 EAELERLDASSDD--LAALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
514-745 |
5.41e-04 |
|
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: 43.17 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 514 QHNTEIRMAVSKVAdkMDHLMTKVEELQKHSAGNSlllpsmsvtmetsmimGNIQRIIQENERLKQEILEKSSRIEEQND 593
Cdd:pfam06008 35 ENAHKIQIEILEKE--LSSLAQETEELQKKATQTL----------------AKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 594 KISELIERNQRY-VEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAkvTEELTAATAQVSRLQLKVTAHQKKeael 669
Cdd:pfam06008 97 NIKEINEKVATLgENDFALPSSDLSRMLAEAQrmlGEIRSRDFGTQLQNA--EAELKAAQDLLSRIQTWFQSPQEE---- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 670 qmqlTESLKETdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSE 745
Cdd:pfam06008 171 ----NKALANA--LRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
567-840 |
5.59e-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: 43.75 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRyvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELT 646
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ--AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 647 AATAQVSRLQLKVtahQKKEAELQMQLTESLKETDLLKGQL---IKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVT 723
Cdd:pfam13868 156 RILEYLKEKAERE---EEREAEREEIEEEKEREIARLRAQQekaQDEKAERDELRAKLYQEEQERKERQKEREEAEKKAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 724 SLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARvstdqaaaeqlslvqAELQT 803
Cdd:pfam13868 233 QRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR---------------RELEK 297
|
250 260 270
....*....|....*....|....*....|....*..
gi 961710477 804 QWEAKCEHLLASAKDEhlLQYQEVCAQRDASQQELLR 840
Cdd:pfam13868 298 QIEEREEQRAAEREEE--LEEGERLREEEAERRERIE 332
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
635-778 |
5.82e-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: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 635 EQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTE--SLKETDLLKgqlikLQAELSELQETSEQAQSKFKSEK 712
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEleDCDPTELDR-----AKEKLKKLLQEIMIKVKKLEELE 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961710477 713 QSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqercraeeeiDEIRKsYQEELDKLRQL 778
Cdd:smart00787 232 EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTF----------KEIEK-LKEQLKLLQSL 286
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
632-902 |
5.98e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 632 LHAEQEKAKVTEELTAATAQVSRLqlkVTAHQKKEAELQMQL-TESLKETDllkgqliKLQAELSELQETSEQ------- 703
Cdd:NF041483 83 IQADQLRADAERELRDARAQTQRI---LQEHAEHQARLQAELhTEAVQRRQ-------QLDQELAERRQTVEShvnenva 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 704 --AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAqERCRAEEEIDEIRKSYQEEldklrQLLKK 781
Cdd:NF041483 153 waEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEA-ESARAEAEAILRRARKDAE-----RLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 782 ARVSTDQAA--AEQLSLVQAELQTQWEAKCEHLLASAkdEHLLQYQEVcAQRDASQQELLRLQEKCLALQAQVTALTEQN 859
Cdd:NF041483 227 ASTQAQEATdhAEQLRSSTAAESDQARRQAAELSRAA--EQRMQEAEE-ALREARAEAEKVVAEAKEAAAKQLASAESAN 303
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 961710477 860 EQHTKdlENKSHMSGVAAAATDPSEKVKKIMNQVFQSLRGEFE 902
Cdd:NF041483 304 EQRTR--TAKEEIARLVGEATKEAEALKAEAEQALADARAEAE 344
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
598-752 |
6.89e-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: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 598 LIERNQRYVEQSNlMMEKRNNSLQTATENTQAR--VLHAEQEKAKVTEEltaataqvsrlQLKVTAHQKKEAELQ--MQL 673
Cdd:cd12923 10 LKEINKEYLDKSR-EYDELYEKYNKLSQEIQLKrqALEAFEEAVKMFEE-----------QLRTQEKFQKEAQPHekQRL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961710477 674 TESLKetdllkgqliKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQ 752
Cdd:cd12923 78 MENNE----------LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQKDQYLRWLKRKGVSQEE 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-774 |
7.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELTAATAQ 651
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE--LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 652 vsrlQLKVTAHQKKEAE-LQMQLTESLKETDLLKgqliklqaelselqetSEQAQSKFKSEKQSRRQLELKVTSLEeela 730
Cdd:PTZ00121 1693 ----ALKKEAEEAKKAEeLKKKEAEEKKKAEELK----------------KAEEENKIKAEEAKKEAEEDKKKAEE---- 1748
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 961710477 731 dLRAEKesleknlsERKKKSAQERCRAEEEIDEIRKSY----QEELDK 774
Cdd:PTZ00121 1749 -AKKDE--------EEKKKIAHLKKEEEKKAEEIRKEKeaviEEELDE 1787
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
687-812 |
8.46e-04 |
|
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: 41.14 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 687 LIKLQAELSELQETSEQAQSKFKsekqsrrQLELKVTSLEEELADL-------RAEKESLEKNLSERKKK---SAQERCR 756
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKVK-------ELEQENLEKEQEIKSLthknqqlEEEVEKLEEQLKEAKEKaeeSEKLKTN 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710477 757 A----------EEEIDEIRKSYQEELDKLRQllkkarvsTDQAAAEQLSLVQAELQT--QWEAKCEHL 812
Cdd:pfam12718 75 NenltrkiqllEEELEESDKRLKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
572-756 |
8.62e-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: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 572 QENERLKQEILEKSSRIEEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEELTAAT 649
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQEEFRRK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 650 AQVSRLQLKVTAHQKKEAELQMQlteslKEtdlLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEEL 729
Cdd:pfam15709 432 LQELQRKKQQEEAERAEAEKQRQ-----KE---LEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
170 180
....*....|....*....|....*..
gi 961710477 730 ADLRAEKESleknlserkKKSAQERCR 756
Cdd:pfam15709 504 AARLALEEA---------MKQAQEQAR 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-888 |
9.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 573 ENERLKQEILEKSS---RIEE-QNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHaEQEKAKVTEELTAA 648
Cdd:PTZ00121 1112 EEARKAEEAKKKAEdarKAEEaRKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK-KAEAARKAEEVRKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 649 TaQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQsKFKSEKQSRRQLELKVTSLEEE 728
Cdd:PTZ00121 1191 E-ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 729 LADLRAE--------------KESLEKNLSERKKKSAQERCRAEE--EIDEIRKSYQEELDKLRQLLKKARVSTDQAAAE 792
Cdd:PTZ00121 1269 QAAIKAEearkadelkkaeekKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 793 qlslvqaelQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQElLRLQEKCLALQAQVTAltEQNEQHTKDLENKSHM 872
Cdd:PTZ00121 1349 ---------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKA--EEDKKKADELKKAAAA 1416
|
330
....*....|....*.
gi 961710477 873 SGVAAAATDPSEKVKK 888
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKK 1432
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
631-858 |
9.13e-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: 43.35 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 631 VLHAEQEKAKVTEELTAATAQVSRLQLK--VTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQEtSEQAQSKF 708
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWErqRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE-EKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 709 KSEKQSR-RQLELKVTSLEEELADLRAEKESLEknlsERKKKSAQERCRAEEEideiRKSYQ-------EELDKLRQLLK 780
Cdd:pfam07888 124 RAAHEARiRELEEDIKTLTQRVLERETELERMK----ERAKKAGAQRKEEEAE----RKQLQaklqqteEELRSLSKEFQ 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961710477 781 KARVSTDQAAAEQLSLVQAELQTQweakceHLLASAkdehllqyQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLT------QKLTTA--------HRKEAENEALLEELRSLQERLNASERKVEGLGEE 259
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
689-777 |
1.06e-03 |
|
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: 40.68 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 689 KLQAELSELQETSEQAQSKFKSEKQSRRQ----LELKVTSLEEELADLRAEKESLEK-----------NLSERKKKSAQE 753
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKE 126
|
90 100
....*....|....*....|....
gi 961710477 754 RCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam09744 127 YSKLHERETEVLRKLKEVVDRQRD 150
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
669-858 |
1.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 669 LQMQLTESLKETDLLKGQLIKLQAELSElqetSEQAQSKFKSEKQS------RRQLELKVTSLEEELADLRAEKESLEKN 742
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLvdlseeAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 743 LSERKKKSAQERCRAEEEI-DEIRKSYQEELDKLRQLLKKARVS-TD-----QAAAEQLSLVQAELQtqweakcehllas 815
Cdd:COG3206 242 LAALRAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARyTPnhpdvIALRAQIAALRAQLQ------------- 308
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 961710477 816 akdehllqyQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:COG3206 309 ---------QEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
663-854 |
1.28e-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: 42.75 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 663 QKKEAELQMQLTESLKETDLLKGQL-------IKLQAELSELQETSEQAQSKFKSEKQSRRQLEL---KVTSLEEELADL 732
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQNrlanqriLELQQQVEELQKALQEQGSKAEDSSLLKQKLEEhleKLHEAQSELQKK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 733 RAEKESLEKNLS---ERKKKSAQERCRA-EEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAK 808
Cdd:pfam05622 383 KEQIEELEPKQDsnlAQKIDELQEALRKkDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEK-DKK 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 809 CEHLLASAKDEHLLQYQE------------VCAQRDASQQELLRLQ---EKCLALQAQVTA 854
Cdd:pfam05622 462 IEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
307-499 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 307 SAAPSPIPGADSLSADPVVSPPTSVPFKSGEPALRIKSnslneqlTVNTNPDTVKAKLISRMAKMgQPMLPILPPQLDSN 386
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPSQVSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 387 DSEIEEVntVRGAGQPVATP-SMQPSLQPaHPVLPQMTSQAPQPSVSglQAPsaalmqvasLDSHSAVSGNAQSFQpyag 465
Cdd:pfam03154 264 QPLPQPS--LHGQMPPMPHSlQTGPSHMQ-HPVPPQPFPLTPQSSQS--QVP---------PGPSPAAPGQSQQRI---- 325
|
170 180 190
....*....|....*....|....*....|....*.
gi 961710477 466 mqayAYPHASAVTSQLQPAR--PLYPTPLSQsPHFQ 499
Cdd:pfam03154 326 ----HTPPSQSQLQSQQPPReqPLPPAPLSM-PHIK 356
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
585-819 |
1.51e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 585 SSRIEEQNDKISELIERNQRYVEQSNLMMEkrnnSLQTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAhqk 664
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLE----DLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINI--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 665 keaeLQMQLTESlketdllkGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELK-VTSLEEELADLRAEKESLEKNL 743
Cdd:PLN02939 175 ----LEMRLSET--------DARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcVHSLSKELDVLKEENMLLKDDI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 744 SERKkksaqercraeEEIDEIRKSYQE--ELDKLRQLLK------KARVSTDQAAAEQLSLVQAELqtqWEAKCE---HL 812
Cdd:PLN02939 243 QFLK-----------AELIEVAETEERvfKLEKERSLLDaslrelESKFIVAQEDVSKLSPLQYDC---WWEKVEnlqDL 308
|
....*..
gi 961710477 813 LASAKDE 819
Cdd:PLN02939 309 LDRATNQ 315
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
566-771 |
1.75e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERL------KQEILEKSSRIEEQNDKISELIERNQRYV-------EQSNLMMEKRNNSLQTATENTQARVL 632
Cdd:PTZ00440 2378 KLLKNIKRNNTLcnnnniKDFISNIGKSVETIKQRFSSNLPEKEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDI 2457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 633 HAEQEKAKVTEELTAataqVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEK 712
Cdd:PTZ00440 2458 DNEKNKENNNMNAEK----IDDLIENVTSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNS 2533
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 713 QS-RRQLELKVTSLEE-------ELADLRAEKESLEKNL---SERKKKSAQERCRAEEEIDEIRKSYQEE 771
Cdd:PTZ00440 2534 TYiINELESHVSKLNEllsyidnEIKELENEKLKLLEKAkieESRKERERIESETQEDNTDEEQINRQQQ 2603
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
517-863 |
1.77e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 517 TEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSLLLPSMSVTMETSMimgniQRIIQENERL--KQEILEKSSRIEEQND 593
Cdd:PRK10246 179 TEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTDEEKQLltAQQQQQQSLNWLTRLD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 594 KISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLH------AEQEKA---------KVTEELTAATAQVSRL-QL 657
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRphweriQEQSAAlahtrqqieEVNTRLQSTMALRARIrHH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 658 KVTAHQKKEAELQmQLTESLKETDLL--------------------KGQLIKLQAELSELQE------------TSEQAQ 705
Cdd:PRK10246 334 AAKQSAELQAQQQ-SLNTWLAEHDRFrqwnnelagwraqfsqqtsdREQLRQWQQQLTHAEQklnalpaitltlTADEVA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 706 SKFKSEKQSRrQLELKVTSLEEELADLRAEKESLEKNLSerkkKSAQERCRAEEEIDEIRKSYQEeldKLRQLLKKARVS 785
Cdd:PRK10246 413 AALAQHAEQR-PLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNEMRQRYKE---KTQQLADVKTIC 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 786 TDQAAAEQLSLVQAELQTqweAKCEHLLASAKDEHLLQYQEVC-----AQRDASQQELLRLQEKCLALQAQVTALTEQNE 860
Cdd:PRK10246 485 EQEARIKDLEAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEVKKLGEEGAALRGQLDALTKQLQ 561
|
...
gi 961710477 861 QHT 863
Cdd:PRK10246 562 RDE 564
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
615-764 |
2.11e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.89 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 615 KRNNSLQTATEntqarvlHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETdLLKGQLIKLQAEL 694
Cdd:COG2882 2 KRSFRLQTLLD-------LAEKEEDEAARELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQG-LSAAQLRNYQQFI 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 695 SELQETSEQAQSKfksEKQSRRQLELKvtslEEELADLRAEKESLEKnLSERKKKSAQERCRAEE--EIDEI 764
Cdd:COG2882 74 ARLDEAIEQQQQQ---VAQAEQQVEQA----RQAWLEARQERKALEK-LKERRREEERQEENRREqkELDEL 137
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
654-783 |
2.24e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 40.28 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 654 RLQLKVTAHQKKEAELQM----QLTESLKETDLLKgqlikLQAELSELQETSEQaqskfKSEKQSRrqLELKVTSLEEEL 729
Cdd:pfam13870 12 RLELITLKHTLAKIQEKLeqkeELGEGLTMIDFLQ-----LQIENQALNEKIEE-----RNKELKR--LKLKVTNTVHAL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 961710477 730 ADLRaEKESLEKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKAR 783
Cdd:pfam13870 80 THLK-EKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLR 132
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
582-865 |
2.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 582 LEKSSR-----IEEQNDKISELiERNQRYVEQSNLMMEKRNNSLQTATE-NTQARVLHAEQEKAKVTEELTAATAQV--S 653
Cdd:pfam01576 683 LERSKRaleqqVEEMKTQLEEL-EDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELedE 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 654 RLQ--LKVTAHQKKEAELQ---MQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEE 728
Cdd:pfam01576 762 RKQraQAVAAKKKLELDLKeleAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 729 LADLRAEKESleknlSERKKKSAQ-ERCRAEEEIDEIRKSYQEELDKLRQLlkKARVStdqaaaeQLSLVQAELQTQWEA 807
Cdd:pfam01576 842 LLQLQEDLAA-----SERARRQAQqERDELADEIASGASGKSALQDEKRRL--EARIA-------QLEEELEEEQSNTEL 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 808 KCEHLLASAKDEHLLQyQEVCAQRDASQ-------------QEL-LRLQE-----------KCLALQAQVTALTEQNEQH 862
Cdd:pfam01576 908 LNDRLRKSTLQVEQLT-TELAAERSTSQksesarqqlerqnKELkAKLQEmegtvkskfksSIAALEAKIAQLEEQLEQE 986
|
...
gi 961710477 863 TKD 865
Cdd:pfam01576 987 SRE 989
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
652-873 |
2.46e-03 |
|
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: 40.66 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 652 VSRLQLKVTAHQKKEAELQMQLTESLKETDLLKgQLIKLQaelselqetsEQAQSKFKSekqSRRQLELKVTSLEEELAD 731
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKLEELRKENRLLK-RLQKRQ----------EKALGKYEG---TESELPQLIARHNEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 732 LRAE---KESLEKNLSERKKKSAQERCRAeeeideirksyQEELDKLRQLLKkarvstDQAAAEQLSLVQ--AELQTQWE 806
Cdd:pfam15619 72 LRERlrrLQEKERDLERKLKEKEAELLRL-----------RDQLKRLEKLSE------DKNLAEREELQKklEQLEAKLE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 807 AKCEHLLASAKDEHLLQyqevcaqrDASQQELLRLQEKCLALQAQVTALTEQNEQHTKDLENKSHMS 873
Cdd:pfam15619 135 DKDEKIQDLERKLELEN--------KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
951-1129 |
2.74e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 951 PRQPSVSGSAGPPPVPlSGEMQGSPSLSPEQAVQEAVPPPPRVlsTPQEEVQGREGEPSEAEALSeieEGSLSPELTCGP 1030
Cdd:PHA03247 2878 PARPPVRRLARPAVSR-STESFALPPDQPERPPQPQAPPPPQP--QPQPPPPPQPQPPPPPPPRP---QPPLAPTTDPAG 2951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 1031 SQRALGPPTSVPPMPPGPVLVDSECEETLASAlenPCVEEPESTARlSLTSHLLKGDPLASGSESPGEEPQPP--ELKK- 1107
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA---PSREAPASSTP-PLTGHSLSRVSSWASSLALHEETDPPpvSLKQt 3027
|
170 180
....*....|....*....|....*...
gi 961710477 1108 ------DEDVTSSAIPYREPGGTEAGSP 1129
Cdd:PHA03247 3028 lwppddTEDSDADSLFDSDSERSDLEAL 3055
|
|
| Sds3 |
pfam08598 |
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing ... |
682-833 |
3.27e-03 |
|
Sds3-like; Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The co-repressor complex contains a core of at least seven proteins. This family represents the conserved region found in Sds3, Dep1 and BRMS1-homolog p40 proteins.
Pssm-ID: 430099 Cd Length: 218 Bit Score: 40.42 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 682 LLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELadlraEKESLEKNLSERKKKSAQERcraEEEI 761
Cdd:pfam08598 19 LYRNKLTALQTELQLLHQGSHPELLQYYRDLEEERDAELKRLRLREEY-----QLKRIDIETKADRTAAHQEF---KKLV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961710477 762 DEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKdEHLLQYQEVCAQRDA 833
Cdd:pfam08598 91 KLLKEKLYDETTQKIYRLNEERRLLDLANTNSYLVDYKKTRSHTLAGLLNPNFTSR-NNPVDPGELVTDRRS 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
624-844 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 624 TENTQARVLHAEQEKAKvteELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ 703
Cdd:COG1196 553 VEDDEVAAAAIEYLKAA---KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 704 AQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERcRAEEEIDEIRKSYQEELDKLRQLLKKAR 783
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-LEELAERLAEEELELEEALLAEEEEERE 708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 784 VSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQ------RDASQQELLRLQEK 844
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
715-871 |
3.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 715 RRQLELKVTSLEEELADLRAEKESLEKnlserkkksAQERCRAEEEIDEIRKSYQE---ELDKLRQLLKKARVSTDQAAA 791
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 792 EQLSLVQAELQTQWEAkcehllasakdehlLQyqevcAQRDASQQELLRLQEKCLALQAQ--------VTALTEQNEQHT 863
Cdd:COG4913 291 ELLEAELEELRAELAR--------------LE-----AELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLE 351
|
....*...
gi 961710477 864 KDLENKSH 871
Cdd:COG4913 352 RELEERER 359
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
655-839 |
3.33e-03 |
|
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: 41.66 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 655 LQLKVTAHQKKEAELqmqLTESLKEtdllkgqLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRA 734
Cdd:pfam07111 53 LELEGSQALSQQAEL---ISRQLQE-------LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 735 E---KESLEKNLSERKKKsaqercraeeEIDEIRKSYQEELDKLRQLLKKArVSTDQAAAEQLSLVQAELQTQWEAKCEH 811
Cdd:pfam07111 123 AlagAEMVRKNLEEGSQR----------ELEEIQRLHQEQLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAGEAKQ 191
|
170 180
....*....|....*....|....*...
gi 961710477 812 LLASAKDEHLLQYQEVCAQRDASQQELL 839
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQVTL 219
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-782 |
3.45e-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: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 621 QTATENTQARVLHAEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQET 700
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 701 SEQAQSKFKSEkQSRRQLELKVTSLEEELADL-----RAEKESLEknLSERKKKSAQERCRAEEEIDEIRKSyQEELDKL 775
Cdd:COG1196 749 EEEALEELPEP-PDLEELERELERLEREIEALgpvnlLAIEEYEE--LEERYDFLSEQREDLEEARETLEEA-IEEIDRE 824
|
....*...
gi 961710477 776 -RQLLKKA 782
Cdd:COG1196 825 tRERFLET 832
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
566-861 |
3.53e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 566 NIQRIIQENERLKQEILEKSsrIEEQNDKISEL---------IER-NQRYVEQSNLMMEKRNNSLQTATE-NTQARVLHA 634
Cdd:PRK04778 26 RNYKRIDELEERKQELENLP--VNDELEKVKKLnltgqseekFEEwRQKWDEIVTNSLPDIEEQLFEAEElNDKFRFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 635 EQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAElQMQLTESLKET------DLL------------------------- 683
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEK-NREEVEQLKDLyrelrkSLLanrfsfgpaldelekqlenleeefs 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 684 --------------KGQLIKLQAELSELQETSEQ-------AQSKFKSE----KQSRRQLE-----LKVTSLEEELADLR 733
Cdd:PRK04778 183 qfveltesgdyveaREILDQLEEELAALEQIMEEipellkeLQTELPDQlqelKAGYRELVeegyhLDHLDIEKEIQDLK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 734 AEKESLEKNLSERKKKSAQERCRA-EEEIDEI----------RKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQ---- 798
Cdd:PRK04778 263 EQIDENLALLEELDLDEAEEKNEEiQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsytl 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 799 ----AELQTQWEAKCEHLLAsakdehllQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQNEQ 861
Cdd:PRK04778 343 neseLESVRQLEKQLESLEK--------QYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEK 401
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
706-792 |
3.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 706 SKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDEIRKsYQEELDKLRQLLKKARVS 785
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
|
....*..
gi 961710477 786 TDQAAAE 792
Cdd:COG1340 80 RDELNEK 86
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
697-809 |
3.96e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 697 LQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAE----KESLEKNLSERKKKSAQERCR-AEEEIDEIRKSYQEE 771
Cdd:pfam05672 16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEerarREEEARRLEEERRREEEERQRkAEEEAEEREQREQEE 95
|
90 100 110
....*....|....*....|....*....|....*...
gi 961710477 772 LDKLRQLLKKARVSTdQAAAEQLSLVQAELQTQWEAKC 809
Cdd:pfam05672 96 QERLQKQKEEAEAKA-REEAERQRQEREKIMQQEEQER 132
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
727-858 |
4.05e-03 |
|
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: 38.77 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 727 EELADLRAEKESLEKNLS--ERKKKSAQERCRAEEEI-DEIRKSYQEELdklrqLLKKARVSTDQAAAEQLSLVQAELQt 803
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAAdaEAQLQKLQEDLEKQAEIaREAQQNYEREL-----VLHAEDIKALQALREELNELKAEIA- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 804 QWEAKCEhllaSAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTALTEQ 858
Cdd:pfam07926 75 ELKAEAE----SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
597-777 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 597 ELIE-RNQRYVEQSNLM-----MEKRNNSLQTATENTQARVLHAEqEKAKVTEeltaataqvsrlqlKVTAHQKKEAElq 670
Cdd:pfam15905 160 ELMKlRNKLEAKMKEVMakqegMEGKLQVTQKNLEHSKGKVAQLE-EKLVSTE--------------KEKIEEKSETE-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 671 mQLTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSrrqLELKVTSLEEELADLRAEKESLEknlSERKKKS 750
Cdd:pfam15905 223 -KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLE---SEKEELL 295
|
170 180 190
....*....|....*....|....*....|...
gi 961710477 751 AQERCRAE------EEIDEIRKSYQEELDKLRQ 777
Cdd:pfam15905 296 REYEEKEQtlnaelEELKEKLTLEEQEHQKLQQ 328
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
672-803 |
4.25e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 672 QLTESLKETDLLKGQLIKLQAELSELQetseQAQSKFKSEKQSRRQLELkVTSLEEELADLRAEKESLEKNLSERkkkSA 751
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFR----NRNGILDPEATAEALLQL-IATLEGQLAELEAELAALRSYLSPN---SP 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 961710477 752 QERcRAEEEIDeirkSYQEELDKLRQLLkkarvsTDQAAAEQLSLVQAELQT 803
Cdd:COG3524 250 QVR-QLRRRIA----ALEKQIAAERARL------TGASGGDSLASLLAEYER 290
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
663-867 |
4.61e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 663 QKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQaqsKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEK- 741
Cdd:pfam03528 7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE---DLKRQNAVLQEAQVELDALQNQLALARAEMENIKAv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 742 -NLSERKKksaqercraEEEIDEIRKSYQEELDKLRQLLKKarvsTDQAAAEQLSLVQAELQTQWE----------AKCE 810
Cdd:pfam03528 84 aTVSENTK---------QEAIDEVKSQWQEEVASLQAIMKE----TVREYEVQFHRRLEQERAQWNqyresaereiADLR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 811 HLLASAKDEHLLQYQEVCAQRDASqqellRLQEKCLALQAQVTALTE---QNEQHTKDLE 867
Cdd:pfam03528 151 RRLSEGQEEENLEDEMKKAQEDAE-----KLRSVVMPMEKEIAALKAkltEAEDKIKELE 205
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
693-868 |
4.73e-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: 40.67 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 693 ELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEE---IDEIRKSYQ 769
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEreqMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 770 EElDKLRQLLKKARVstdQAAAEQLSLVQAELQTQWEAKCEHLLasAKDEHLLQYQEVCAQRDAS-QQELLRLQEKCLAL 848
Cdd:pfam13868 112 EE-DQAEAEEKLEKQ---RQLREEIDEFNEEQAEWKELEKEEER--EEDERILEYLKEKAEREEErEAEREEIEEEKERE 185
|
170 180
....*....|....*....|
gi 961710477 849 QAQVTALTEQNEQHTKDLEN 868
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDE 205
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
640-804 |
4.85e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.17 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 640 KVTEELTAATAQVSRLQLKVTAHQKkeaELQMQLTeslKETDLLKGQLiklQAELSELQETSEQAQSKFKSEKQSR-RQL 718
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQ---ELVDRLE---KETEALRERL---QKDLEEVRAKLEPYLEELQAKLGQNvEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 719 ELKVTSLEEELAD-LRAEKESLEKNLSErkkKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLV 797
Cdd:pfam01442 72 RQRLEPYTEELRKrLNADAEELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEV 148
|
....*..
gi 961710477 798 QAELQTQ 804
Cdd:pfam01442 149 QAQLSQR 155
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
558-733 |
5.03e-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: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 558 METSMIMGNIQRIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQtatENTQArvlhaEQE 637
Cdd:pfam15294 98 FEEREFTSSNKKPNFELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQATQALD---EKSKL-----EKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 638 KAKVTEELTAATAQVSRLQlKVTAHQKKEAELQMQLTESLKETDL----LKGQLIKLQAELSELQETSEQAQS----KFk 709
Cdd:pfam15294 170 LKDLQKEQGAKKDVKSNLK-EISDLEEKMAALKSDLEKTLNASTAlqksLEEDLASTKHELLKVQEQLEMAEKelekKF- 247
|
170 180
....*....|....*....|....
gi 961710477 710 SEKQSRRQLELKVTSLEEELADLR 733
Cdd:pfam15294 248 QQTAAYRNMKEMLTKKNEQIKELR 271
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
567-842 |
5.25e-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: 40.96 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 567 IQRIIQENERLKQEILEKSSRIEEQNDKISEL---IERNQRYVEQSNLMME---KRNNSLQTATENTQARVLHAEQ---E 637
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDVKERKINVLqkkIENLQEQLRDKDKQLAglkERVKSLQTDSSNTDTALTTLEEalsE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 638 KAKVTEeltaataqvsRLQLKvtaHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSElQETS-----EQAQSKFKS-- 710
Cdd:pfam10174 448 KERIIE----------RLKEQ---REREDRERLEELESLKKENKDLKEKVSALQPELTE-KESSlidlkEHASSLASSgl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 711 EKQSR-RQLELKVTSLEEELADLRAE-KESLEKNLSERKKKSAQERCRA-EEEI----DEIRKSyQEELDKLRQLLKKA- 782
Cdd:pfam10174 514 KKDSKlKSLEIAVEQKKEECSKLENQlKKAHNAEEAVRTNPEINDRIRLlEQEVarykEESGKA-QAEVERLLGILREVe 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961710477 783 --RVSTDQ--AAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEVCAQRDASQQELLRLQ 842
Cdd:pfam10174 593 neKNDKDKkiAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
568-937 |
5.32e-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: 40.98 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 568 QRIIQENERLKQEILEKSSRIEEQNDKIS------ELIERNQRYVEQSNLmmEKRNNSLQTAtENTQARVLHAEQEKAKV 641
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNGELSAADAAVAkdrselEALEDQHGAFLDADI--ETAAADQEQL-PSWQSELENLEERLKAL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 642 TEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIK--LQAELSELQETSEQAQSKFKSEKQ--SRRQ 717
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEddLQALESELREQLEAGKLEFNEEEYrlKSRL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 718 LELK-----VTSLEEELADLRAEKESLEKnLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKA--RVSTDQAA 790
Cdd:pfam12128 447 GELKlrlnqATATPELLLQLENFDERIER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeeRQSALDEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 791 AEQLS----LVQAELQTQ---WEAKCEHLLASakdEHLLQYQEVCAQRDASQQELLRLQEKCLALQAqvtalTEQNEQHT 863
Cdd:pfam12128 526 ELQLFpqagTLLHFLRKEapdWEQSIGKVISP---ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKR-----IDVPEWAA 597
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 864 KDLENKSHMSGVAAAATDPSEKVKKIMNQVFQsLRGEFE---LEESYNGRAVLGTIMNTIKMVTLQllnQHEQDKGQ 937
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQ-ANGELEkasREETFARTALKNARLDLRRLFDEK---QSEKDKKN 670
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
695-906 |
5.58e-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: 41.11 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 695 SELQETSEQAQSKFKSEKQSRRQLELKvtsLEEELADLRAEKESlEKNLSERKKKSAQERCRAEEEI-DEIRKSYQEELD 773
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIID---LEELKLQELKLKEQ-AKKALEYYQLKEKLELEEEYLLyLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 774 KLRQLLKKARVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLLQYQEvcaQRDASQQELLRLQEKCLALQAQVT 853
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK---EEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 961710477 854 ALTEQNEQHTKDLENKSHMSGVAAAATDPSEKVKKIMNQVFQSLRGEFELEES 906
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
720-854 |
5.72e-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: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 720 LKVTSLEEELADLRAEKESLEKnlserkkksaqERCRAEEEIDEirkSYQEELDKLRQLLKKARvstdqaaaEQLslvqA 799
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 800 ELQTQWEAKCEHL--LASAKDEHLLQYQEVCAQRDASQQELLRLQEKCLALQAQVTA 854
Cdd:COG0542 458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
678-811 |
6.06e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 39.77 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 678 KETDLLKGQLIKLQAELSELQETSEQAqskFKSEKQSRRQLELKVTSLEEEladlraeKESLEKNLSErKKKSAQERCRA 757
Cdd:cd07647 67 KETENVANAHIQLAQSLREEAEKLEEF---REKQKEERKKTEDIMKRSQKN-------KKELYKKTMK-AKKSYEQKCRE 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961710477 758 EEEIDEIRKS-----YQEELDKLRQLLKKARVSTDQA-AAEQLSLVQAE-LQTQWEAKCEH 811
Cdd:cd07647 136 KDKAEQAYEKsssgaQPKEAEKLKKKAAQCKTSAEEAdSAYKSSIGCLEdARVEWESEHAT 196
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
575-795 |
6.39e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 575 ERLKQEI-LEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVlhaEQEKAKVTEELTAATAQVS 653
Cdd:PRK05771 34 EDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV---EEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 654 RLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQA------ELSELQETSEQAQSKFKSEKQSRR-----QLELKV 722
Cdd:PRK05771 111 ELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELS 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 723 TSLEEELADLRAEKESL--EKNLSERKKKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKAR--VSTDQAAAEQLS 795
Cdd:PRK05771 191 DEVEEELKKLGFERLELeeEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYeyLEIELERAEALS 267
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
649-777 |
6.90e-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: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 649 TAQVSRLQLKVTAHQKKEAELQMQLtESLK--ETDLlkgqliklqAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLE 726
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKI-DALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKE 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 961710477 727 EELADLRAEKESLEKNLSerkkkSAQERC-RAEEEIDEIRKSYQEELDKLRQ 777
Cdd:pfam18595 71 IELRELERREERLQRQLE-----NAQEKLeRLREQAEEKREAAQARLEELRE 117
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
673-749 |
7.18e-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: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 673 LTESLKETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELA------DLRAEKESLEKNLSER 746
Cdd:pfam05837 1 LLPLINRRDELSSAILKLSSELRELQEELTEVEKENLRLKRKNRELAAELLELAKEKEsrredpKLRAQLEKLEAELKKS 80
|
...
gi 961710477 747 KKK 749
Cdd:pfam05837 81 RRR 83
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
634-775 |
7.38e-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: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQK-KEA---------ELQMQLTESLKETDLLKGQLIKLQAELSELQETSEQ 703
Cdd:pfam13851 52 IQQENKRLTEPLQKAQEEVEELRKQLENYEKdKQSlknlkarlkVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEA 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961710477 704 AQS--KFKSEKQSrRQLELKVTSLEEELadlraekESLEKNLSERKKKS---AQERCRAEEEIDEIRKSYQEELDKL 775
Cdd:pfam13851 132 AIQdvQQKTGLKN-LLLEKKLQALGETL-------EKKEAQLNEVLAAAnldPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
694-781 |
7.60e-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: 39.03 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 694 LSELQETSEQAQSKfksekqsRRQLELKVTSLEEELADLRAEKESLEKNLSERKKKSAQERCRAEEEIDE---IRKSYQE 770
Cdd:pfam06785 85 FKILEETLEELQSE-------EERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEkqlLINEYQQ 157
|
90
....*....|.
gi 961710477 771 ELDKLRQLLKK 781
Cdd:pfam06785 158 TIEEQRSVLEK 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
511-857 |
8.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKhsagNSLLLPSMSVTMETSMIMGNiqriiQENERLKQEILEKSSRIEE 590
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSR----NMEMLNGQSVCPVCGTTLGE-----EKSNHIINHYNEKKSRLEE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 591 QNDKIseliERNQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTE-ELTAATAQVSRLQLKVTAHQKKEAEL 669
Cdd:PRK01156 484 KIREI----EIEVKDIDEKIVDLKKRKEYL----ESEEINKSINEYNKIESARaDLEDIKIKINELKDKHDKYEEIKNRY 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 670 QMQLTESL--KETDLLKGQLIKLQAELSELQETSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESlEKNLSERK 747
Cdd:PRK01156 556 KSLKLEDLdsKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN-EANNLNNK 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 748 KKSAQERCRAEEEIDEIRKSYQEELDKLRQLLKKARVSTDQAAAEQLSLVQAELQTQwEAKCEHLLASAKDEHLLQYQEV 827
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-DAKANRARLESTIEILRTRINE 713
|
330 340 350
....*....|....*....|....*....|
gi 961710477 828 CAQRDASQQELLRLQEKCLALQAQVTALTE 857
Cdd:PRK01156 714 LSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
663-854 |
8.78e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 663 QKKEAELQMQLTESLKETDLLKGQL-----IKLQA----ELSE----------LQETSEQAQSKFKSE--------KQSR 715
Cdd:COG0497 171 KKELEELRADEAERARELDLLRFQLeeleaAALQPgeeeELEEerrrlsnaekLREALQEALEALSGGeggaldllGQAL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 716 RQLElKVTSLEEELADLRAEKESLEKNLSErkkkSAQE--RCRAEEEIDEIRKSYQEE-LDKLRQLLKKARVSTDQAAAe 792
Cdd:COG0497 251 RALE-RLAEYDPSLAELAERLESALIELEE----AASElrRYLDSLEFDPERLEEVEErLALLRRLARKYGVTVEELLA- 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 793 qlslvqaeLQTQWEAKCEHLLASakDEHLLQYQevcAQRDASQQELLRL--------QEKCLALQAQVTA 854
Cdd:COG0497 325 --------YAEELRAELAELENS--DERLEELE---AELAEAEAELLEAaeklsaarKKAAKKLEKAVTA 381
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
561-782 |
8.88e-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: 40.38 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 561 SMIMGNIqrIIQENERLKQEILEKSSRIEEQNDKISELIERNQRYVEQSNLMMEKR--------NNSLQtATENTQARVL 632
Cdd:NF033838 28 SLFLGGV--VHAEEVRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRkhtqnvalNKKLS-DIKTEYLYEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 633 HAEQEKA------KVTEELTAATAQ----VSRLQLKVTAHQKKEAELQMQlTESLKETDLLKGQLI---KLQAELSELQE 699
Cdd:NF033838 105 NVLKEKSeaeltsKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEAEKK-AKDQKEEDRRNYPTNtykTLELEIAESDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 700 TSEQAQSKFKSEKQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKK--KSAQERCRAEEEIDEIRKSYQEELDKLRQ 777
Cdd:NF033838 184 EVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
....*
gi 961710477 778 LLKKA 782
Cdd:NF033838 264 RAKRG 268
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
563-747 |
9.34e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 563 IMGNIQRIIQENERLKQEIL--------EKSSRIEEQNDKISELIERN---QRYVEQSN-------LMMEKRNNSLQTAT 624
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEeldldeaeEKNEEIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 625 ENTQA--RVLHAEQEKAK-VTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLKETDLLKGQLIKLQAELSELQETS 701
Cdd:PRK04778 334 DRVKQsyTLNESELESVRqLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDE 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 961710477 702 EQAQSK---FKSEKQS-RRQLE-LKVTSLEEELADL----RAEKESLEKNLSERK 747
Cdd:PRK04778 414 LEAREKlerYRNKLHEiKRYLEkSNLPGLPEDYLEMffevSDEIEALAEELEEKP 468
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
634-843 |
9.42e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.89 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 634 AEQEKAKVTEELTAATAQVSRLQLKVTAHQKKEAELQMQLTESLK--ETDLLKGQLIKLQaelsELQETSEQAQSKFKSE 711
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTkgNEELAREALAEKK----SLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 712 KQSRRQLELKVTSLEEELADLRAEKESLEKNLSERKkksAQErcraeeeideirksyqeeldKLRQLLKKARVSTDQAAA 791
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAK---AQE--------------------AVQTSLGSLSTSSATDSF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 961710477 792 EQLSLVQAELQTQWEAKCEhlLASAKDEhLLQYQEVCAQRDASQQELLRLQE 843
Cdd:pfam04012 167 ERIEEKIEEREARADAAAE--LASAVDL-DAKLEQAGIQMEVSEDVLARLKA 215
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
684-861 |
9.46e-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: 40.21 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 684 KGQLIKLQAELSELqetsEQAQSKFKSEKQSRRQLELKVTSLEEE----LADLRAEKESLEKNLSERKKKSAQERCRAEE 759
Cdd:pfam12128 240 RPEFTKLQQEFNTL----ESAELRLSHLHFGYKSDETLIASRQEErqetSAELNQLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961710477 760 EIdeirKSYQEELDKLRQLLK---KARVSTDQAAAEQLSLVQAELQTQ-------------WEAKCEHLLASAKDEHLLQ 823
Cdd:pfam12128 316 AV----AKDRSELEALEDQHGaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRD 391
|
170 180 190
....*....|....*....|....*....|....*....
gi 961710477 824 YQEVCAQRDASQQELLRLQEKCLA-LQAQVTALTEQNEQ 861
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEA 430
|
|
|