|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-667 |
0e+00 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 909.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 7 VGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHD----------------- 69
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDkhlfdklneclkkaatr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 70 ----------------------------------KMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 115
Cdd:pfam04388 81 lqaltllghvvrrqptwlhkianhpllksllkclKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 116 KKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 195
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 196 WKRLETHDVVIECAKISLDPTEASYEDGYSVShqisarfphrSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQL 275
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 276 PQTLSSPSTRLITEPPqaTLWSPSMVCGMTTPPTSPGNVP-------PDLSHPYSKVFGTTG--GKGTPLG--TPATSPP 344
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPttpselsPSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 345 PAPLCHSDDYVHISLP--QATVTPPRKEERMDSARPCLHRQHHL-LNDRGSEEPPGSKGSVTLSDLPGFLGDLA-SEEDS 420
Cdd:pfam04388 389 KQPPPLSDSHVHRALPasSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 421 IEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYR--DSLPGSQRK--------THSAASSSQGASVNPE-----PLH 485
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 486 SSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAH 565
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 566 HFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLL 645
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 2240436665 646 LHNQLLYERFKRQQHALRNRRL 667
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-908 |
3.60e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 656 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDRE 735
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 736 EFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSES-----VQQQMEFLNRQLLVLGEVNELY 810
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAelaeaEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 811 LEQLQNKHSDTTKEVEmmKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQ 890
Cdd:COG1196 400 AQLEELEEAEEALLER--LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250
....*....|....*...
gi 2240436665 891 AAESRYEAQKRITQVFEL 908
Cdd:COG1196 478 ALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
687-919 |
4.93e-10 |
|
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: 63.92 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 687 QLKLQEKDIQMWkVSLqkeqARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKAN 766
Cdd:TIGR02168 217 ELKAELRELELA-LLV----LRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 767 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEvnelYLEQLQNKHSDTTKEVEMMKAAYrKELEKNrshVLQQ 846
Cdd:TIGR02168 288 KEL---YALANEISRLEQQKQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL-EELKEE---LESL 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436665 847 TQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ---ARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 919
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-901 |
1.33e-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: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 663 RNRRLLRKVIKaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQL-QHDR--EEFYN 739
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 740 QSQELQTKLEDCRN-----MIAELRIELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 796
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 797 NRQLLVLGEVNELYLEQLQNKHSDTT---------KEVEMMKAAYRKELEKNRSHVLQQTQRLdtSQKRILELE--SHLA 865
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINdleskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERL--KETIIKNNSeiKDLT 446
|
250 260 270
....*....|....*....|....*....|....*.
gi 2240436665 866 KKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKR 901
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
686-904 |
4.64e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 686 DQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKA 765
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 766 NNKVCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQNKHSDTTKEVemmKAAyRKELEKNRSHVLQ 845
Cdd:COG3883 92 ARALYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEEL---KAD-KAELEAKKAELEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436665 846 QTQRLDTSQKrilELESHLAKKDHLLLEQKKYLEDVKLQaRGQLQAAESRYEAQKRITQ 904
Cdd:COG3883 155 KLAELEALKA---ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAE 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-917 |
5.59e-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: 58.01 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 704 KEQARYNQLQEqRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKL 783
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 784 SNSESvqqqmeflNRQllvlgevnelyLEQLQnkhsdttKEVEMMKAAyRKELEKnrsHVLQQTQRLDTSQKRILELESH 863
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2240436665 864 LAKKDHLLLEQKKYLEdvklQARGQLQAAESRYEAQ-KRITQVFELEILDLYGRL 917
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAErEELAAKIPPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-919 |
6.54e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 653 ERFKRQQHALRNrrlLRKVIKAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQH 732
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 733 dreEFYNQSQELQT----------KLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLNR 798
Cdd:TIGR02168 289 ---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 799 QLLVLGEVNELYLEQLQNKHSDtTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD-HLLLEQKKY 877
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSK-VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEE 444
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2240436665 878 LEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 919
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-909 |
8.09e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 653 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLqEKDIQMWKVSLQKEQARYNQLQEQRdtmvTKLHSQIRQLQH 732
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARL-EAEVEQLEERIAQLSKELTELEAEI----EELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 733 DREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEVNE 808
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 809 LY------LEQLQNKHSDTTKEVEMMKAAYRKELEKNRShvlqqtqRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVK 882
Cdd:TIGR02168 856 SLaaeieeLEELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260
....*....|....*....|....*...
gi 2240436665 883 LqargQLQAAESRY-EAQKRITQVFELE 909
Cdd:TIGR02168 929 L----RLEGLEVRIdNLQERLSEEYSLT 952
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
702-909 |
9.71e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 702 LQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQ 781
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 782 KLSNSESVQQQMEflnrqllvlgevNElyLEQLQNKHSDTTKEVEMMKAAyRKELEKNRSHVLQQTQRLDTS----QKRI 857
Cdd:COG4372 88 QLQAAQAELAQAQ------------EE--LESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2240436665 858 LELESHLAKKDHLLLEQKKYLEDVKLQ-ARGQLQAAESryEAQKRITQVFELE 909
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAeAEQALDELLK--EANRNAEKEEELA 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-882 |
3.03e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 652 YERFKRQQHAlrNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHS------ 725
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeele 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 726 ----QIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQlL 801
Cdd:TIGR02168 355 sleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKK-L 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 802 VLGEVNELY--LEQLQNKHSDTTKEVEMMKAAY---RKELEKNRSHVLQQTQRLDTSQKRILELEShlakkdhLLLEQKK 876
Cdd:TIGR02168 431 EEAELKELQaeLEELEEELEELQEELERLEEALeelREELEEAEQALDAAERELAQLQARLDSLER-------LQENLEG 503
|
....*.
gi 2240436665 877 YLEDVK 882
Cdd:TIGR02168 504 FSEGVK 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-908 |
1.47e-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: 55.83 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 711 QLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVSQKLSNSE 787
Cdd:TIGR02168 681 ELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 788 SVQQQMEFLNRQL------LVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELE 861
Cdd:TIGR02168 758 ELEAEIEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2240436665 862 SHLAKkdhlLLEQKKYLEDVKLQARGQL-QAAESRYEAQKRITQVFEL 908
Cdd:TIGR02168 838 RRLED----LEEQIEELSEDIESLAAEIeELEELIEELESELEALLNE 881
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-921 |
4.26e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 673 KAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDRE---EFYNQSQELQTKLE 749
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 750 DCRNMIAELRIELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKhS 819
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-R 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 820 DTTKEVE-------MMKAAYRKE-----LEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------LLEQKKYLEDV 881
Cdd:PRK02224 634 ERKRELEaefdearIEEAREDKEraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerreaLENRVEALEAL 713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2240436665 882 KLQARgQLQAAESRYEAQKRITQVFELEIL-----------DLYGRLEKDG 921
Cdd:PRK02224 714 YDEAE-ELESMYGDLRAELRQRNVETLERMlnetfdlvyqnDAYSHIELDG 763
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-917 |
4.74e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 677 LEEHNAAMKDQLKLQEKDIQMWKvslQKEQARYNQLQEQRDTmvtklHSQIR-QLQHDREEFYNQSQELQTKL----EDC 751
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEK-----EMNLRdELESVREEFIQKGDEVKCKLdkseENA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 752 RNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLlvlgEVNELYLEQLQNKHSDTTKE 824
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQL----NAYEIKVNKLELELASAKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 825 VEMMKAAYRKELEKNR---SHVLQQTQRLDTSQKRILELESHLAKK-DH------LLLEQKKYLEDVKLQAR-GQLQAAE 893
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHkiaemvALMEKHKHQYDKIIEERdSELGLYK 731
|
250 260
....*....|....*....|....
gi 2240436665 894 SRYEAQKRITQVFELEILDLYGRL 917
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
711-919 |
5.69e-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: 53.23 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 711 QLQEQRDtmvtKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSE-SV 789
Cdd:COG4942 24 EAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 790 QQQMEFLNRQLLVL---GEVNELYLEQLQNKHSDTTKEVEMMKAaYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAK 866
Cdd:COG4942 100 EAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2240436665 867 KDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 919
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-918 |
5.79e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 673 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCR 752
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 753 NMIAELRIELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQNKHSDT 821
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 822 TKEVEMMKAAyrKELEKNRSHVLQQ----TQRLDTSQKRILELESHLAKKDhlllEQKKYLEDVKLQARGQLQAAESRYE 897
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEERredlEELIAERRETIEEKRERAEELR----ERAAELEAEAEEKREAAAEAEEEAE 568
|
250 260
....*....|....*....|.
gi 2240436665 898 AQKRITQVFELEILDLYGRLE 918
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIE 589
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
661-920 |
5.99e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 661 ALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEFYNQ 740
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 741 SQELQTKLEDCRNMIAEL---RIELKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqn 816
Cdd:COG4372 103 LESLQEEAEELQEELEELqkeRQDLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 817 khsDTTKEVEMMKAAYRKELEKNRSHvlqQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRY 896
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEEL---AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260
....*....|....*....|....
gi 2240436665 897 EAQKRITQVFELEILDLYGRLEKD 920
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEE 277
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
656-910 |
7.60e-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: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 656 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQeqrdtmvtklhsQIRQLQHDRE 735
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 736 EFYNQSQELQTKLEDCRNMIAELRiELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 798
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 799 QLLVLGEVNELyLEQLQNKHSDTTKEVEmmKAAYRKElEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYL 878
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE--VATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270
....*....|....*....|....*....|....*.
gi 2240436665 879 EDVKLQA----RGQLQAAESRYEAQKRITQVFELEI 910
Cdd:TIGR00618 412 IDTRTSAfrdlQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
628-909 |
1.00e-06 |
|
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: 53.15 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 628 GGS--PPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKvikaAALEEHNAAMKD---QLKLQEKDIQMwkvsL 702
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDasrKIGEIEKEIEQ----L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 703 QKEQARYNQLQEQrdtmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELllsqvsqk 782
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI-------- 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 783 lsnsESVQQQMEFLNRQLlvlgEVNELYLEQLQNKHSDTTKEVEMM------KAAYRKELEKNRSHVlqqTQRLDTSQKR 856
Cdd:TIGR02169 794 ----PEIQAELSKLEEEV----SRIEARLREIEQKLNRLTLEKEYLekeiqeLQEQRIDLKEQIKSI---EKEIENLNGK 862
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436665 857 ILELESHLAKKDHLLLEQKKYLEDVK---LQARGQLQAAESRYEAQKriTQVFELE 909
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKkerDELEAQLRELERKIEELE--AQIEKKR 916
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
664-815 |
1.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 664 NRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYNQLQEQRDTMVTKL---HSQIRQLQHDREEFY 738
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436665 739 NQ-SQELQTKLEDCRNMIAELRIELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 815
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
633-838 |
3.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 633 SDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIKAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 708
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 709 YNQLQEQRDTMVTklhsQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIEL----KKANNKVCHT-ELLLSQVSQKL 783
Cdd:TIGR02168 889 LALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436665 784 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN---KHSDTTKEVEMMKAAyRKELEK 838
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEElkeRYDFLTAQKEDLTEA-KETLEE 1021
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-920 |
5.57e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 657 RQQHALRNRRLLRKVIKAA-----ALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ---RDTMVTKLHSQIR 728
Cdd:COG4372 39 ELDKLQEELEQLREELEQAreeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 729 QLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLV 802
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 803 LGEVNElyLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKY--LED 880
Cdd:COG4372 199 EEELAE--AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdtEEE 276
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2240436665 881 VKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 920
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
689-904 |
6.43e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 689 KLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklhSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRIELKKANNK 768
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELE--------EELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 769 VCHTELLLS-----QVSQKLSNS-ESVQQQMEFLNRQLLVLGEVnELYLEQLQNKHSDTTKEVEmmkAAYRKELEKNRSH 842
Cdd:COG4717 118 LEKLEKLLQllplyQELEALEAElAELPERLEELEERLEELREL-EEELEELEAELAELQEELE---ELLEQLSLATEEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2240436665 843 VLQQTQRLDTSQKRILELESHLAKKDhlllEQKKYLEdvklQARGQLQAAESRYEAQKRITQ 904
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQ----EELEELE----EELEQLENELEAAALEERLKE 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
666-919 |
8.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 666 RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLH------SQIRQLqhdREEFYN 739
Cdd:PRK03918 149 KVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReineisSELPEL---REELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 740 QSQELQtKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQLQNK 817
Cdd:PRK03918 226 LEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 818 HSDTTKEVEMMKAAYR---KELEKNRSHVLQQTQRLDTSQKRILELESHLA--KKDHLLLEQKKYLEDVKLQARGQL--- 889
Cdd:PRK03918 305 YLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLtgl 384
|
250 260 270
....*....|....*....|....*....|....*
gi 2240436665 890 ---QAAESRYEAQKRITQVFE--LEILDLYGRLEK 919
Cdd:PRK03918 385 tpeKLEKELEELEKAKEEIEEeiSKITARIGELKK 419
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
652-850 |
8.96e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 652 YERFKRQQHALRNRRllrkvikaAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARyNQLQEqrdtmvtkLHSQIRQLQ 731
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAE--------LPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 732 HDREEFynqsQELQTKLEDCRNMIAELRIELKKANNKVchTELLLSQVSQKLSNSESVQQQMEFLNRQllvlgevnelyL 811
Cdd:COG4717 153 ERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEE-----------L 215
|
170 180 190
....*....|....*....|....*....|....*....
gi 2240436665 812 EQLQNKHSDTTKEVEMMKAAYRKELEKNRshvLQQTQRL 850
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER---LKEARLL 251
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
664-899 |
1.82e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 664 NRRLLRKVIKAAALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYNQLQEQRDTMVT------KLHSQIRQLQHDREE 736
Cdd:pfam00038 10 NDRLASYIDKVRFLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 737 FYNQSQELQTKLEDCRNMIAELRIELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQ 815
Cdd:pfam00038 87 FRQKYEDELNLRTSAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 816 NKHSDTTKEVEM--------------MKAAY-------RKELEKN---RSHVLQQ-----TQRLDTSQKRILE------- 859
Cdd:pfam00038 149 AQVSDTQVNVEMdaarkldltsalaeIRAQYeeiaaknREEAEEWyqsKLEELQQaaarnGDALRSAKEEITElrrtiqs 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2240436665 860 LESHLAKkdhlLLEQKKYLEDvklqargQLQAAESRYEAQ 899
Cdd:pfam00038 229 LEIELQS----LKKQKASLER-------QLAETEERYELQ 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
665-904 |
2.71e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 665 RRLLRKVIKAAALEEHNAAMKD----QLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtMVTKLHSQIRQLQHDREEFYNQ 740
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKE-MLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 741 SQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVsQKLSNSE----SVQQQMEFLNRQLLVLGEVNELYLEQLQN 816
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL-QHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 817 ------KHSDTTKEVEMMKAAYRKELEKNRSHvLQQTQRL-DTSQKRILELESHLAKkdhllLEqkkyLEDVKLqargqL 889
Cdd:pfam15921 574 mtqlvgQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILkDKKDAKIRELEARVSD-----LE----LEKVKL-----V 638
|
250
....*....|....*
gi 2240436665 890 QAAESRYEAQKRITQ 904
Cdd:pfam15921 639 NAGSERLRAVKDIKQ 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
725-920 |
3.44e-05 |
|
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: 47.45 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 725 SQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchtellLSQVSQKLSNSEsvqQQMEFLNRQLlvlg 804
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALE---QELAALEAEL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 805 EVNELYLEQLQNKHSDTTKEV-EMMKAAYRKELEKNRSHVLQQTQRLDTSqkRILELESHLAKKDHLLLEQ----KKYLE 879
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2240436665 880 DVK---LQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 920
Cdd:COG4942 164 ALRaelEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
682-901 |
4.42e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.38 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 682 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRIE 761
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 762 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQNkhsdTTKEVemmkAAYRKELEK 838
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2240436665 839 NRSH---VL----QQTQRLDTS----QKRILELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESryEAQKR 901
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEQArnerKKTLTGLESSLQKDQQQLSE----LRANESRLRDSIARAER--EAKAR 259
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
673-816 |
6.15e-05 |
|
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: 43.78 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 673 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQ-IRQLQHDREEFynqsQELQTKledc 751
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVL-HAEdIKALQALREEL----NELKAE---- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436665 752 rnmIAELRIELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQN 816
Cdd:pfam07926 73 ---IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-904 |
9.70e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 685 KDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKK 764
Cdd:TIGR04523 116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 765 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQNKHSDTTKEVEMMKAAY---RKELEK 838
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKDEQnkiKKQLSE 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2240436665 839 NRSHVLQQTQRLDTSQKRILELESHLA-----KKDHLLLEQKKYLEDVKLQARG-QLQAAESryeaQKRITQ 904
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEiQNQISQN----NKIISQ 339
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
678-882 |
1.40e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 678 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYNQLQ------EQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDC 751
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 752 RNMIAELRIELKK-ANNKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTK 823
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436665 824 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVK 882
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-941 |
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 2240436665 703 QKEQA-RYNQLQEQRDTM-VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKAnnkvchtELLLSQVS 780
Cdd:COG1196 208 QAEKAeRYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-------RLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 781 QKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDttkevemmKAAYRKELEKNRSHVLQQTQRLDTSQKRILEL 860
Cdd:COG1196 281 LEL---EEAQAEEYELLAELARLEQDIARLEERRRELEER--------LEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 861 ESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEER 940
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 2240436665 941 L 941
Cdd:COG1196 430 L 430
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
666-910 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 666 RLLRKVIKAAA--------LEEHNAaMKDQLKLQEKDI-QMWKVSLQKEQARYN----QLQEQRDTMVTKLHSQIRQLQH 732
Cdd:pfam13868 9 RELNSKLLAAKcnkerdaqIAEKKR-IKAEEKEEERRLdEMMEEERERALEEEEekeeERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 733 DREEFYNQS-QELQTKLEDCRNMIAE-LRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLY 810
Cdd:pfam13868 88 KRQEEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 811 LEQLQNkhsdttKEVEMMKAAYRKELEKNRshvlqQTQRLDTSQKRILElesHLAKKDHLLLeqKKYLEDVKLQARGQ-L 889
Cdd:pfam13868 161 LKEKAE------REEEREAEREEIEEEKER-----EIARLRAQQEKAQD---EKAERDELRA--KLYQEEQERKERQKeR 224
|
250 260
....*....|....*....|.
gi 2240436665 890 QAAESRYEAQKRITQVFELEI 910
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQI 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-815 |
1.96e-04 |
|
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: 45.82 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 653 ERFKRQQHALRNR-RLLRKVIKAAALEEhnAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ 731
Cdd:TIGR02168 361 EELEAELEELESRlEELEEQLETLRSKV--AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 732 HDREEFYNQSQE-LQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRqllvlgEVNELY 810
Cdd:TIGR02168 439 QAELEELEEELEeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE------GVKALL 512
|
....*
gi 2240436665 811 LEQLQ 815
Cdd:TIGR02168 513 KNQSG 517
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
658-763 |
1.98e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 658 QQHALRNRRLlrkVIKAAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYNQLQEQRDTMvtKLHSQ-----IRQLQH 732
Cdd:pfam13851 50 SEIQQENKRL---TEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 2240436665 733 DREEFYNQS----QELQTKLEdCRNMIAELRIELK 763
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
684-880 |
2.05e-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: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 684 MKDQLKLQEKDIQMWKVSLQKeqarYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNmIAELRI--- 760
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQE----CEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP-FAKLKEsqe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 761 ------ELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNrqLLVLGEVNELYLEQLQNKHSDTTKEV-----EMMK 829
Cdd:pfam14988 85 reiqdlEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQELR--ILELGERATRELKRKAQALKLAAKQAlsefcRSIK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2240436665 830 AAYRkELEKNRSHVLQQTQRLDtsqkrilELESHLAKKDHLLLEQKKYLED 880
Cdd:pfam14988 163 RENR-QLQKELLQLIQETQALE-------AIKSKLENRKQRLKEEQWYLEA 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
654-913 |
2.62e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 654 RFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHD 733
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 734 REE----------FYNQSQELQTKLEDcRNMIAELRIEL--KKANNKVCHTELL------------------LSQVSQKL 783
Cdd:TIGR00606 908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 784 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QNKHSDTTKEVEMMKAAYRKELekNRSHVLQQTQrldTSQKriL 858
Cdd:TIGR00606 987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQ---EHQK--L 1059
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436665 859 ELESHLAKKDH-LLLEQKKYLEDVKLQARGQL-----QAAESRYEAQKRITQVFELEILDL 913
Cdd:TIGR00606 1060 EENIDLIKRNHvLALGRQKGYEKEIKHFKKELrepqfRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
652-905 |
2.68e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 652 YERFKRQQHALRNRRLLRKVI------KAAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDT------- 718
Cdd:COG4913 584 KGNGTRHEKDDRRRIRSRYVLgfdnraKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 719 -----MVTKLHSQIRQLQHDREEF----------YNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKL 783
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 784 SNSESVQQQMEFLN----RQLLVLGEVNELYLEQLQNKHSDTTKEvemmKAAYRKELEKNRSHVLQQ----TQRLDTSQK 855
Cdd:COG4913 737 EAAEDLARLELRALleerFAAALGDAVERELRENLEERIDALRAR----LNRAEEELERAMRAFNREwpaeTADLDADLE 812
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2240436665 856 RILELESHLAK--KDHL--LLEQ-KKYLEDVKLQARGQLQAA--ESRYEAQKRITQV 905
Cdd:COG4913 813 SLPEYLALLDRleEDGLpeYEERfKELLNENSIEFVADLLSKlrRAIREIKERIDPL 869
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
669-919 |
3.40e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 669 RKVIKAaaLEEHNAAMKDQLKlqekDI-QMWKvSLQKEqarynqLQEQrdtmVTKLHSQIRQLQhdrEEFYN-------- 739
Cdd:PRK04778 197 REILDQ--LEEELAALEQIME----EIpELLK-ELQTE------LPDQ----LQELKAGYRELV---EEGYHldhldiek 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 740 QSQELQTKLEDCRNMIAELriELKKANNKvchtellLSQVSQKLsnsESVQQQME-------FLNRQLLVLGEvnelYLE 812
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEK-------NEEIQERI---DQLYDILErevkarkYVEKNSDTLPD----FLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 813 QLQNKHSDTTKEVEMMKAAYR---KELEKNRSH----------VLQQTQRLDTSQKRILELESHLAK-KDHLL---LEQK 875
Cdd:PRK04778 321 HAKEQNKELKEEIDRVKQSYTlneSELESVRQLekqleslekqYDEITERIAEQEIAYSELQEELEEiLKQLEeieKEQE 400
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2240436665 876 KYLEDVKlqargQLQAAESryEAQKRItQVFELEILDLYGRLEK 919
Cdd:PRK04778 401 KLSEMLQ-----GLRKDEL--EAREKL-ERYRNKLHEIKRYLEK 436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
654-904 |
5.46e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 654 RFKRQQHALRNRRLLRKVIKAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQ---EQRDtmvtklhsqiRQL 730
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 731 QHDREEfynqSQELQTKLEDCRNMIAELRielkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 810
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 811 LEQLQNKHSDTTKEVEMMKaayrKELEKNRSHVLQQTQRLDTSQKRILELEshlakkdhllLEQKKYLEDVKLQA---RG 887
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKAteeRS 566
|
250
....*....|....*..
gi 2240436665 888 QLQAAESRYEAQKRITQ 904
Cdd:pfam17380 567 RLEAMEREREMMRQIVE 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
653-918 |
1.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 653 ERFKRQQHALRNR-RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTM---VTKLHSQIR 728
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELeaeLAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 729 QL-QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQ---------------- 791
Cdd:COG4717 181 ELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaalla 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 792 -----------QMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNR-------------------S 841
Cdd:COG4717 261 llglggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelL 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2240436665 842 HVLQQTQRLDTSQKRILELESHLaKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQvfelEILDLYGRLE 918
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLE 412
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
674-769 |
1.36e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.26 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 674 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNqlQEQRDTMVTKLHSQIRQLQHDREEFynqSQELQTKLedcRN 753
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 2240436665 754 MIAELRIELKKANNKV 769
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
664-884 |
1.45e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 664 NRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQE 743
Cdd:TIGR04523 420 EKELLEKEIER--LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 744 L-----QTKleDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYL 811
Cdd:TIGR04523 498 LkklneEKK--ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQ 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436665 812 EQ--LQNKHS---DTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 884
Cdd:TIGR04523 576 TQksLKKKQEekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
653-913 |
1.81e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 653 ERFKRQQHALRNRRLLRKVIKAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYNQLQE------------------ 714
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAewkelekeeereederil 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 715 ----QRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIelkkannkvchtELLLSQVSQKlsnseSVQ 790
Cdd:pfam13868 159 eylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA------------KLYQEEQERK-----ERQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 791 QQMEFLNRQLLVLGEVNELYLEQLQNKhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDtsQKRILELESHLAKKDHL 870
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQIELK--------ERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEH 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2240436665 871 LLEQKKYLEDVKLQARGQ----LQAAESRYEAQKRITQVFELEILDL 913
Cdd:pfam13868 292 RRELEKQIEEREEQRAAEreeeLEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
656-867 |
2.65e-03 |
|
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: 41.29 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 656 KRQQHALRNRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ---- 731
Cdd:COG4942 41 KELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 732 ----------HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFlnrqll 801
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436665 802 vlgevnelyLEQLQNKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTSQKRILELESHLAKK 867
Cdd:COG4942 190 ---------LEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
688-898 |
2.69e-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: 41.73 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 688 LKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTK--LHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKA 765
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDK 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 766 NNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQNKHSDTTKEvEMMKAayrkeLEKNRS 841
Cdd:pfam10174 599 DKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-ELMGA-----LEKTRQ 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 842 HVLQQTQRLDTSQKRILELESHLAKkdhLLLEQKKYLEDV---KLQArgqLQAAESRYEA 898
Cdd:pfam10174 670 ELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
683-915 |
3.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 683 AMKDQLKLQEKDIQMWKVSLQKEQARYNQ----LQEQRDTMVTKLH---SQIRQLQHDREEFYNQSQELQ-------TKL 748
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEelkeLAEKRDELNAQVKelrEEAQELREKRDELNEKVKELKeerdelnEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 749 EDCRNMIAELRIELKKANNKvchtELLLSQVSQKLSNSESVQQ--------QMEFLNR-------------QLLVLGEVN 807
Cdd:COG1340 88 NELREELDELRKELAELNKA----GGSIDKLRKEIERLEWRQQtevlspeeEKELVEKikelekelekakkALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 808 ELY--LEQLQNKHSDTTKEV-----------EMMKAAY------RKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD 868
Cdd:COG1340 164 ELRaeLKELRKEAEEIHKKIkelaeeaqelhEEMIELYkeadelRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2240436665 869 HLLLEQKKYLEDVKLQA-----RGQLQAAESRYEAQKRITqvFElEILDLYG 915
Cdd:COG1340 244 KELKKLRKKQRALKREKekeelEEKAEEIFEKLKKGEKLT--TE-ELKLLQK 292
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
674-800 |
4.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 674 AAALEEHNAAmKDQLKLQEKDIQmwkvSLQKE----QARYNQLQEQ--------------------------------RD 717
Cdd:COG3883 47 EELNEEYNEL-QAELEALQAEID----KLQAEiaeaEAEIEERREElgeraralyrsggsvsyldvllgsesfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 718 TMVTKLHSQ----IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLsnsESVQQQM 793
Cdd:COG3883 122 SALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQL 198
|
....*..
gi 2240436665 794 EFLNRQL 800
Cdd:COG3883 199 AELEAEL 205
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
716-854 |
4.33e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 716 RDTMVTKLHSQ---IRQLQHDREEFYNQSQELQTklEDCRNMIAELRI---ELKKANNKVCHTELLLSQVSQKLSNS--- 786
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDI--ERLYRMIDILNDaqqQIKWTNQPRIYLEVALVKLCEQAAASpey 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2240436665 787 ----ESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVemmKAAYRKELEKNrSHVLQQTQRLDTSQ 854
Cdd:PRK05563 368 dtelEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNK---KKKYKVPRGKI-YKVLKEATRQDLEL 435
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
710-796 |
4.96e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 39.55 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 710 NQLQEQRdTMVTKLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRIELK-KANNKVCHTELLLSQVSQKLSn 785
Cdd:cd16855 8 QQLEELR-QRTQETENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 2240436665 786 sesvQQQMEFL 796
Cdd:cd16855 86 ----QLRMELA 92
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
707-906 |
5.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 707 ARYNQLQEQRDTMVTKLHSQ---IRQLQ---HDREEFYN--------------------QSQELQTKLEDCRNMIAELRI 760
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLsfdVQKLQrlhQAFSRFIGshlavafeadpeaelrqlnrRRVELERALADHESQEQQQRS 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 761 ELKKANNKVCHTELLLSQVSqkLSNSESVQQQMEFLNRQLLVLgEVNELYLEQlqnkHSDTTKEVEMMKAAYR---KELE 837
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA-EEAKRFVQQ----HGNALAQLEPIVSVLQsdpEQFE 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 838 KNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------------------LLEQKKYLEDVKLQARGQLQAAESRYeAQ 899
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsyedaaemlaknsdlnekLRQRLEQAEQERTRAREQLRQAQAQL-AQ 1017
|
....*..
gi 2240436665 900 KriTQVF 906
Cdd:PRK04863 1018 Y--NQVL 1022
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-905 |
5.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 662 LRNRRLLRKVIKAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVSLQ---KEQAR---------YNQLQEQR- 716
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISYTspdPELAAavanalaeaYLEQNLELr 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 717 -----------DTMVTKLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLL 776
Cdd:COG3206 170 reearkaleflEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 777 SQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQNKHSDtTKEVEMMKAAYRKELEKNRSHVLQQTQ-RLDTSQK 855
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-VIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2240436665 856 RILELESHLAKKDHLLLE----QKKYLEdvkLQArgQLQAAESRYEA-QKRITQV 905
Cdd:COG3206 328 REASLQAQLAQLEARLAElpelEAELRR---LER--EVEVARELYESlLQRLEEA 377
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
727-913 |
6.19e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.63 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 727 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVC-------HTELLLSQVSQKLSNSESVQQQMEFLNRQ 799
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeeleRTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 800 LLVLGEVNELYLEQLQNKHSDTTkevEMMKAAYRKELEKNRSHVLQQT------QRLDTSQKRILELESHL--------- 864
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAK---EIAEEADRKYEEVARKLVVVEGdleraeERAELAESKIVELEEELkvvgnnlks 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2240436665 865 --AKKDHLLLEQKKYLEDVK-LQARgqLQAAESRYEAQKRITQVFELEILDL 913
Cdd:pfam00261 160 leASEEKASEREDKYEEQIRfLTEK--LKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
674-919 |
6.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 674 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQaryNQLQEQRDTMvtklhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 752
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESEN---AELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 753 NMIAELRIELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQNKHSDTTKevemmkaay 832
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 833 RKELEKNRSHVLQQTQRLDTSQKRileLESHLAKKDHLLLEQKKYLEDVKlqarGQLQAAEsryEAQKRITQVFELEILD 912
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRN---VERQLSTLQAQLSDMKKKLEEDA----GTLEALE---EGKKRLQRELEALTQQ 560
|
250
....*....|...
gi 2240436665 913 L------YGRLEK 919
Cdd:pfam01576 561 LeekaaaYDKLEK 573
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
656-857 |
6.52e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 656 KRQQHALRNRRLlRKVIKAA-----ALEEHNAAMKDQLKLQEKDIqMWKVSLQKEQARYNQLQeqrdtmvtklhSQIRQL 730
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDApaelrELRQELAALQAKAEAAPKEI-LASLSLEELEQRLLQTS-----------AQLQEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 731 QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNEL 809
Cdd:pfam12795 98 QNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2240436665 810 YLEQLQNkhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRI 857
Cdd:pfam12795 169 EQELLSN---------NNRQDLLKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
656-901 |
6.69e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 656 KRQQHALRNRRLLRKVIKAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklHSQIRQLQHDRE 735
Cdd:pfam13868 62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 736 EFYNQSQEL------QTKLEDCRNM--------IAELRIELKKANNKVchTELLLSQVSQKLSNSESVQQQMEFLnRQLL 801
Cdd:pfam13868 134 EFNEEQAEWkelekeEEREEDERILeylkekaeREEEREAEREEIEEE--KEREIARLRAQQEKAQDEKAERDEL-RAKL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 802 VLGEVN----ELYLEQLQNKHsdttKEVEMMKAAYRKELEkNRSHVLQQTQRLD-TSQKRILELESHLAKKDhLLLEQKK 876
Cdd:pfam13868 211 YQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIE-LKERRLAEEAEREeEEFERMLRKQAEDEEIE-QEEAEKR 284
|
250 260
....*....|....*....|....*..
gi 2240436665 877 YLEDVKLQA--RGQLQAAESRYEAQKR 901
Cdd:pfam13868 285 RMKRLEHRRelEKQIEEREEQRAAERE 311
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
784-901 |
8.36e-03 |
|
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: 38.05 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 784 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN--KHSDTTKEVEMMKAAYRKELEKNRSHVLQQ----TQRLDTSQKRI 857
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQELAILEAENskAEVETLKAEIEEMAQNLRDLELDLVTLRSEkenlTKELQKKQERV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2240436665 858 LELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESRYEAQKR 901
Cdd:pfam10473 97 SELESLNSSLENLLEE----KEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
684-910 |
9.21e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 684 MKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQI--RQLQHDREEFYNQSQELQTKLEDCRNMIAELRIE 761
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLEssREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436665 762 LKKANNKVCHTELLLSQVSQKLsnsESVQQQMEflnrqllvlGEVNELYleqlqNKHSDTTKEVEMMKAAYRKELEKNRs 841
Cdd:TIGR00606 271 IKALKSRKKQMEKDNSELELKM---EKVFQGTD---------EQLNDLY-----HNHQRTVREKERELVDCQRELEKLN- 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436665 842 hvlQQTQRLDTSQKRILELESHLAKKDHLLLEQ--KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEI 910
Cdd:TIGR00606 333 ---KERRLLNQEKTELLVEQGRLQLQADRHQEHirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
|
| |
