|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
16-598 |
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: 825.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 16 ITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETF 95
Cdd:pfam04388 131 ITLLPMIPQLVKQYLPDIFEIFGRLASWNLKNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 96 EEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVShqisarfphrSADVTTSP 175
Cdd:pfam04388 211 EETIKPMLEHVRIHPELVTGTKDHELDPTRWKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 176 YADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPqaTLWSPSMVCGMTTPPTSPGNVP-------PDL 248
Cdd:pfam04388 281 YTDQQSSYGSSTSTPSSTPRLQLSSSSGTSPPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPttpselsPSS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 249 SHPYSKVFGTTAG-GKGTPLG--TPATSPPPAPLCHSDDYVHISLP--QATVTPPRKEERMDSARPCLHRQHHL-LNDRG 322
Cdd:pfam04388 359 SHLSSRGSSPPEAaGEATPETtpAKDSPYLKQPPPLSDSHVHRALPasSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 323 SEEPPGSKGSVTLSDLPGFLGDLA-SEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYR--DSLPGSQRK-- 397
Cdd:pfam04388 439 LLEPPGDKSSVTLSELPDFIKDLAlSSEDSVEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrn 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 398 ------THSAASSSQGASVNPE-----PLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCK 466
Cdd:pfam04388 519 riasycSSTSQSDSHGPATTPEskpsaLAEDGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 467 IPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKL 546
Cdd:pfam04388 599 IPSRQKVSTQSGQPLPYEHLFDLALPKTASLFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRL 678
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1375023171 547 PLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRL 598
Cdd:pfam04388 679 PLPSKSADWTHFGGSAPSDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
587-839 |
3.35e-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: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 587 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDRE 666
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 667 EFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSES-----VQQQMEFLNRQLLVLGEVNELY 741
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAelaeaEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 742 LEQLQNKHSDTTKEVEmmKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQ 821
Cdd:COG1196 400 AQLEELEEAEEALLER--LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250
....*....|....*...
gi 1375023171 822 AAESRYEAQKRITQVFEL 839
Cdd:COG1196 478 ALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
618-850 |
4.61e-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: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 618 QLKLQEKDIQMWkVSLqkeqARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKAN 697
Cdd:TIGR02168 217 ELKAELRELELA-LLV----LRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 698 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEvnelYLEQLQNKHSDTTKEVEMMKAAYrKELEKNrshVLQQ 777
Cdd:TIGR02168 288 KEL---YALANEISRLEQQKQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL-EELKEE---LESL 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375023171 778 TQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ---ARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 850
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
594-832 |
1.39e-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: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 594 RNRRLLRKVIKaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQL-QHDR--EEFYN 670
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 671 QSQELQTKLEDCRN-----MIAELRIELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 727
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 728 NRQLLVLGEVNELYLEQLQNKHSDTT---------KEVEMMKAAYRKELEKNRSHVLQQTQRLdtSQKRILELE--SHLA 796
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINdleskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERL--KETIIKNNSeiKDLT 446
|
250 260 270
....*....|....*....|....*....|....*.
gi 1375023171 797 KKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKR 832
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
617-835 |
4.28e-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: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 617 DQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKA 696
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 697 NNKVCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQNKHSDTTKEVemmKAAyRKELEKNRSHVLQ 776
Cdd:COG3883 92 ARALYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEEL---KAD-KAELEAKKAELEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375023171 777 QTQRLDTSQKrilELESHLAKKDHLLLEQKKYLEDVKLQaRGQLQAAESRYEAQKRITQ 835
Cdd:COG3883 155 KLAELEALKA---ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAE 209
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-850 |
5.97e-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: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 584 ERFKRQQHALRNrrlLRKVIKAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQH 663
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 664 dreEFYNQSQELQT----------KLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLNR 729
Cdd:TIGR02168 289 ---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 730 QLLVLGEVNELYLEQLQNKHSDtTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD-HLLLEQKKY 808
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSK-VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEE 444
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1375023171 809 LEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 850
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
635-848 |
6.55e-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: 57.63 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 635 KEQARYNQLQEqRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKL 714
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 715 SNSESvqqqmeflNRQllvlgevnelyLEQLQnkhsdttKEVEMMKAAyRKELEKnrsHVLQQTQRLDTSQKRILELESH 794
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1375023171 795 LAKKDHLLLEQKKYLEdvklQARGQLQAAESRYEAQ-KRITQVFELEILDLYGRL 848
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAErEELAAKIPPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-840 |
7.70e-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: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 584 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLqEKDIQMWKVSLQKEQARYNQLQEQRdtmvTKLHSQIRQLQH 663
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARL-EAEVEQLEERIAQLSKELTELEAEI----EELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 664 DREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEVNE 739
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 740 LY------LEQLQNKHSDTTKEVEMMKAAYRKELEKNRShvlqqtqRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVK 813
Cdd:TIGR02168 856 SLaaeieeLEELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260
....*....|....*....|....*...
gi 1375023171 814 LqargQLQAAESRY-EAQKRITQVFELE 840
Cdd:TIGR02168 929 L----RLEGLEVRIdNLQERLSEEYSLT 952
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
633-840 |
9.55e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 633 LQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQ 712
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 713 KLSNSESVQQQMEflnrqllvlgevNElyLEQLQNKHSDTTKEVEMMKAAyRKELEKNRSHVLQQTQRLDTS----QKRI 788
Cdd:COG4372 88 QLQAAQAELAQAQ------------EE--LESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1375023171 789 LELESHLAKKDHLLLEQKKYLEDVKLQ-ARGQLQAAESryEAQKRITQVFELE 840
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAeAEQALDELLK--EANRNAEKEEELA 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
583-813 |
2.89e-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: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 583 YERFKRQQHAlrNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHS------ 656
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeele 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 657 ----QIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQlL 732
Cdd:TIGR02168 355 sleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKK-L 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 733 VLGEVNELY--LEQLQNKHSDTTKEVEMMKAAY---RKELEKNRSHVLQQTQRLDTSQKRILELEShlakkdhLLLEQKK 807
Cdd:TIGR02168 431 EEAELKELQaeLEELEEELEELQEELERLEEALeelREELEEAEQALDAAERELAQLQARLDSLER-------LQENLEG 503
|
....*.
gi 1375023171 808 YLEDVK 813
Cdd:TIGR02168 504 FSEGVK 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
642-839 |
1.38e-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: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 642 QLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVSQKLSNSE 718
Cdd:TIGR02168 681 ELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 719 SVQQQMEFLNRQL------LVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELE 792
Cdd:TIGR02168 758 ELEAEIEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1375023171 793 SHLAKkdhlLLEQKKYLEDVKLQARGQL-QAAESRYEAQKRITQVFEL 839
Cdd:TIGR02168 838 RRLED----LEEQIEELSEDIESLAAEIeELEELIEELESELEALLNE 881
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
604-852 |
4.21e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 604 KAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDRE---EFYNQSQELQTKLE 680
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 681 DCRNMIAELRIELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKhS 750
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK-R 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 751 DTTKEVE-------MMKAAYRKE-----LEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------LLEQKKYLEDV 812
Cdd:PRK02224 634 ERKRELEaefdearIEEAREDKEraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerreaLENRVEALEAL 713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1375023171 813 KLQARgQLQAAESRYEAQKRITQVFELEIL-----------DLYGRLEKDG 852
Cdd:PRK02224 714 YDEAE-ELESMYGDLRAELRQRNVETLERMlnetfdlvyqnDAYSHIELDG 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
642-850 |
5.26e-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: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 642 QLQEQRDtmvtKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSE-SV 720
Cdd:COG4942 24 EAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 721 QQQMEFLNRQLLVL---GEVNELYLEQLQNKHSDTTKEVEMMKAaYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAK 797
Cdd:COG4942 100 EAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1375023171 798 KDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 850
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
604-849 |
5.57e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 604 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCR 683
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 684 NMIAELRIELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQNKHSDT 752
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 753 TKEVEMMKAAyrKELEKNRSHVLQQ----TQRLDTSQKRILELESHLAKKDhlllEQKKYLEDVKLQARGQLQAAESRYE 828
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEERredlEELIAERRETIEEKRERAEELR----ERAAELEAEAEEKREAAAEAEEEAE 568
|
250 260
....*....|....*....|.
gi 1375023171 829 AQKRITQVFELEILDLYGRLE 849
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIE 589
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
592-851 |
5.79e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 592 ALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEFYNQ 671
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 672 SQELQTKLEDCRNMIAEL---RIELKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqn 747
Cdd:COG4372 103 LESLQEEAEELQEELEELqkeRQDLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 748 khsDTTKEVEMMKAAYRKELEKNRSHvlqQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRY 827
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEEL---AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260
....*....|....*....|....
gi 1375023171 828 EAQKRITQVFELEILDLYGRLEKD 851
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEE 277
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
608-848 |
6.32e-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: 53.57 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 608 LEEHNAAMKDQLKLQEKDIQMWKvslQKEQARYNQLQEQRDTmvtklHSQIR-QLQHDREEFYNQSQELQTKL----EDC 682
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEK-----EMNLRdELESVREEFIQKGDEVKCKLdkseENA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 683 RNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLlvlgEVNELYLEQLQNKHSDTTKE 755
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQL----NAYEIKVNKLELELASAKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 756 VEMMKAAYRKELEKNR---SHVLQQTQRLDTSQKRILELESHLAKK-DH------LLLEQKKYLEDVKLQAR-GQLQAAE 824
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHkiaemvALMEKHKHQYDKIIEERdSELGLYK 731
|
250 260
....*....|....*....|....
gi 1375023171 825 SRYEAQKRITQVFELEILDLYGRL 848
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
587-841 |
8.53e-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: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 587 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQeqrdtmvtklhsQIRQLQHDRE 666
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 667 EFYNQSQELQTKLEDCRNMIAELRiELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 729
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 730 QLLVLGEVNELyLEQLQNKHSDTTKEVEmmKAAYRKElEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYL 809
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE--VATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270
....*....|....*....|....*....|....*.
gi 1375023171 810 EDVKLQA----RGQLQAAESRYEAQKRITQVFELEI 841
Cdd:TIGR00618 412 IDTRTSAfrdlQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
559-840 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 559 GGS--PPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKvikaAALEEHNAAMKD---QLKLQEKDIQMwkvsL 633
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDasrKIGEIEKEIEQ----L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 634 QKEQARYNQLQEQrdtmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELllsqvsqk 713
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI-------- 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 714 lsnsESVQQQMEFLNRQLlvlgEVNELYLEQLQNKHSDTTKEVEMM------KAAYRKELEKNRSHVlqqTQRLDTSQKR 787
Cdd:TIGR02169 794 ----PEIQAELSKLEEEV----SRIEARLREIEQKLNRLTLEKEYLekeiqeLQEQRIDLKEQIKSI---EKEIENLNGK 862
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1375023171 788 ILELESHLAKKDHLLLEQKKYLEDVK---LQARGQLQAAESRYEAQKriTQVFELE 840
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKkerDELEAQLRELERKIEELE--AQIEKKR 916
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
595-746 |
1.21e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 595 NRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYNQLQEQRDTMVTKL---HSQIRQLQHDREEFY 669
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375023171 670 NQ-SQELQTKLEDCRNMIAELRIELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 746
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
564-769 |
3.75e-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: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 564 SDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIKAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 639
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 640 YNQLQEQRDTMVTklhsQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIEL----KKANNKVCHT-ELLLSQVSQKL 714
Cdd:TIGR02168 889 LALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1375023171 715 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN---KHSDTTKEVEMMKAAyRKELEK 769
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEElkeRYDFLTAQKEDLTEA-KETLEE 1021
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
588-851 |
5.21e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 588 RQQHALRNRRLLRKVIKAA-----ALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ---RDTMVTKLHSQIR 659
Cdd:COG4372 39 ELDKLQEELEQLREELEQAreeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 660 QLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLV 733
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 734 LGEVNElyLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKY--LED 811
Cdd:COG4372 199 EEELAE--AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdtEEE 276
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1375023171 812 VKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 851
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
620-850 |
5.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 620 KLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklhSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRIELKKANNK 699
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELE--------EELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 700 vchtellLSQVSQKLSNSESVqQQMEFLNRQLLVLGEVnelyLEQLQNKHsDTTKEVEMMKAAYRKELEKNRSHVLQQTQ 779
Cdd:COG4717 118 -------LEKLEKLLQLLPLY-QELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375023171 780 RLDTSQKRilELESHLAKKDHLLLEQKKYLEDVKlQARGQLQAAESRYEAQKRitqvfELEILDLYGRLEK 850
Cdd:COG4717 185 QLSLATEE--ELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLEN-----ELEAAALEERLKE 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-781 |
8.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 583 YERFKRQQHALRNRRllrkvikaAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARyNQLQEqrdtmvtkLHSQIRQLQ 662
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAE--------LPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 663 HDREEFynqsQELQTKLEDCRNMIAELRIELKKANNKVchTELLLSQVSQKLSNSESVQQQMEFLNRQllvlgevnelyL 742
Cdd:COG4717 153 ERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEE-----------L 215
|
170 180 190
....*....|....*....|....*....|....*....
gi 1375023171 743 EQLQNKHSDTTKEVEMMKAAYRKELEKNRshvLQQTQRL 781
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER---LKEARLL 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
597-850 |
1.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 597 RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLH------SQIRQLqhdREEFYN 670
Cdd:PRK03918 149 KVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReineisSELPEL---REELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 671 QSQELQtKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQLQNK 748
Cdd:PRK03918 226 LEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 749 HSDTTKEVEMMKAAYR---KELEKNRSHVLQQTQRLDTSQKRILELESHLA--KKDHLLLEQKKYLEDVKLQARGQL--- 820
Cdd:PRK03918 305 YLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLtgl 384
|
250 260 270
....*....|....*....|....*....|....*
gi 1375023171 821 ---QAAESRYEAQKRITQVFE--LEILDLYGRLEK 850
Cdd:PRK03918 385 tpeKLEKELEELEKAKEEIEEeiSKITARIGELKK 419
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
595-830 |
1.67e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 595 NRRLLRKVIKAAALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYNQLQEQRDTMVT------KLHSQIRQLQHDREE 667
Cdd:pfam00038 10 NDRLASYIDKVRFLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 668 FYNQSQELQTKLEDCRNMIAELRIELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQ 746
Cdd:pfam00038 87 FRQKYEDELNLRTSAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 747 NKHSDTTKEVEM--------------MKAAY-------RKELEKN---RSHVLQQ-----TQRLDTSQKRILE------- 790
Cdd:pfam00038 149 AQVSDTQVNVEMdaarkldltsalaeIRAQYeeiaaknREEAEEWyqsKLEELQQaaarnGDALRSAKEEITElrrtiqs 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1375023171 791 LESHLAKkdhlLLEQKKYLEDvklqargQLQAAESRYEAQ 830
Cdd:pfam00038 229 LEIELQS----LKKQKASLER-------QLAETEERYELQ 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
596-835 |
2.92e-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: 48.19 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 596 RRLLRKVIKAAALEEHNAAMKD----QLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtMVTKLHSQIRQLQHDREEFYNQ 671
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKE-MLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 672 SQELQTKLEDCRNMIAELRIELKKANNKVchtELLLSQVsQKLSNSE----SVQQQMEFLNRQLLVLGEVNELYLEQLQN 747
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL-QHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 748 ------KHSDTTKEVEMMKAAYRKELEKNRSHvLQQTQRL-DTSQKRILELESHLAKkdhllLEqkkyLEDVKLqargqL 820
Cdd:pfam15921 574 mtqlvgQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILkDKKDAKIRELEARVSD-----LE----LEKVKL-----V 638
|
250
....*....|....*
gi 1375023171 821 QAAESRYEAQKRITQ 835
Cdd:pfam15921 639 NAGSERLRAVKDIKQ 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
656-851 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 656 SQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchtellLSQVSQKLSNSEsvqQQMEFLNRQLlvlg 735
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALE---QELAALEAEL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 736 EVNELYLEQLQNKHSDTTKEV-EMMKAAYRKELEKNRSHVLQQTQRLDTSqkRILELESHLAKKDHLLLEQ----KKYLE 810
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1375023171 811 DVK---LQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 851
Cdd:COG4942 164 ALRaelEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
613-832 |
5.65e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.00 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 613 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRIE 692
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 693 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQNkhsdTTKEVemmkAAYRKELEK 769
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375023171 770 NRSH---VL----QQTQRLDTS----QKRILELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESryEAQKR 832
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 ... |
604-747 |
6.57e-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: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 604 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQ-IRQLQHDREEFynqsQELQTKledc 682
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVL-HAEdIKALQALREEL----NELKAE---- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375023171 683 rnmIAELRIELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQN 747
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 ... |
616-835 |
1.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 616 KDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKK 695
Cdd:TIGR04523 116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 696 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQNKHSDTTKEVEMMKAAY---RKELEK 769
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKDEQnkiKKQLSE 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375023171 770 NRSHVLQQTQRLDTSQKRILELESHLA-----KKDHLLLEQKKYLEDVKLQARG-QLQAAESryeaQKRITQ 835
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEiQNQISQN----NKIISQ 339
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
634-872 |
1.37e-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: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 634 QKEQA-RYNQLQEQRDTM-VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKAnnkvchtELLLSQVS 711
Cdd:COG1196 208 QAEKAeRYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-------RLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 712 QKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDttkevemmKAAYRKELEKNRSHVLQQTQRLDTSQKRILEL 791
Cdd:COG1196 281 LEL---EEAQAEEYELLAELARLEQDIARLEERRRELEER--------LEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 792 ESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEER 871
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 1375023171 872 L 872
Cdd:COG1196 430 L 430
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
609-813 |
1.61e-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: 45.73 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 609 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYNQLQ------EQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDC 682
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 683 RNMIAELRIELKK-ANNKVCHTELLLSQVSQKL-------SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTK 754
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375023171 755 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVK 813
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
589-694 |
1.70e-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: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 589 QQHALRNRRLlrkVIKAAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYNQLQEQRDTMvtKLHSQ-----IRQLQH 663
Cdd:pfam13851 50 SEIQQENKRL---TEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 1375023171 664 DREEFYNQS----QELQTKLEdCRNMIAELRIELK 694
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-746 |
1.88e-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: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 584 ERFKRQQHALRNR-RLLRKVIKAAALEEhnAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ 662
Cdd:TIGR02168 361 EELEAELEELESRlEELEEQLETLRSKV--AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 663 HDREEFYNQSQE-LQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRqllvlgEVNELY 741
Cdd:TIGR02168 439 QAELEELEEELEeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE------GVKALL 512
|
....*
gi 1375023171 742 LEQLQ 746
Cdd:TIGR02168 513 KNQSG 517
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
597-841 |
2.24e-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: 44.52 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 597 RLLRKVIKAAA--------LEEHNAaMKDQLKLQEKDI-QMWKVSLQKEQARYN----QLQEQRDTMVTKLHSQIRQLQH 663
Cdd:pfam13868 9 RELNSKLLAAKcnkerdaqIAEKKR-IKAEEKEEERRLdEMMEEERERALEEEEekeeERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 664 DREEFYNQS-QELQTKLEDCRNMIAE-LRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLY 741
Cdd:pfam13868 88 KRQEEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 742 LEQLQNkhsdttKEVEMMKAAYRKELEKNRshvlqQTQRLDTSQKRILElesHLAKKDHLLLeqKKYLEDVKLQARGQ-L 820
Cdd:pfam13868 161 LKEKAE------REEEREAEREEIEEEKER-----EIARLRAQQEKAQD---EKAERDELRA--KLYQEEQERKERQKeR 224
|
250 260
....*....|....*....|.
gi 1375023171 821 QAAESRYEAQKRITQVFELEI 841
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQI 245
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
600-850 |
2.44e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 600 RKVIKAaaLEEHNAAMKDQLKlqekDI-QMWKvSLQKEqarynqLQEQrdtmVTKLHSQIRQLQhdrEEFYN-------- 670
Cdd:PRK04778 197 REILDQ--LEEELAALEQIME----EIpELLK-ELQTE------LPDQ----LQELKAGYRELV---EEGYHldhldiek 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 671 QSQELQTKLEDCRNMIAELriELKKANNKvchtellLSQVSQKLsnsESVQQQME-------FLNRQLLVLGEvnelYLE 743
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEK-------NEEIQERI---DQLYDILErevkarkYVEKNSDTLPD----FLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 744 QLQNKHSDTTKEVEMMKAAYR---KELEKNRSH----------VLQQTQRLDTSQKRILELESHLAK-KDHLL---LEQK 806
Cdd:PRK04778 321 HAKEQNKELKEEIDRVKQSYTlneSELESVRQLekqleslekqYDEITERIAEQEIAYSELQEELEEiLKQLEeieKEQE 400
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1375023171 807 KYLEDVKlqargQLQAAESryEAQKRItQVFELEILDLYGRLEK 850
Cdd:PRK04778 401 KLSEMLQ-----GLRKDEL--EAREKL-ERYRNKLHEIKRYLEK 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
583-836 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 583 YERFKRQQHALRNRRLLRKVI------KAAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDT------- 649
Cdd:COG4913 584 KGNGTRHEKDDRRRIRSRYVLgfdnraKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 650 -----MVTKLHSQIRQLQHDREEF----------YNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKL 714
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 715 SNSESVQQQMEFLN----RQLLVLGEVNELYLEQLQNKHSDTTKEvemmKAAYRKELEKNRSHVLQQ----TQRLDTSQK 786
Cdd:COG4913 737 EAAEDLARLELRALleerFAAALGDAVERELRENLEERIDALRAR----LNRAEEELERAMRAFNREwpaeTADLDADLE 812
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1375023171 787 RILELESHLAK--KDHL--LLEQ-KKYLEDVKLQARGQLQAA--ESRYEAQKRITQV 836
Cdd:COG4913 813 SLPEYLALLDRleEDGLpeYEERfKELLNENSIEFVADLLSKlrRAIREIKERIDPL 869
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
615-811 |
2.74e-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: 43.22 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 615 MKDQLKLQEKDIQMWKVSLQKeqarYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNmIAELRI--- 691
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQE----CEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP-FAKLKEsqe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 692 ------ELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNrqLLVLGEVNELYLEQLQNKHSDTTKEV-----EMMK 760
Cdd:pfam14988 85 reiqdlEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQELR--ILELGERATRELKRKAQALKLAAKQAlsefcRSIK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1375023171 761 AAYRkELEKNRSHVLQQTQRLDtsqkrilELESHLAKKDHLLLEQKKYLED 811
Cdd:pfam14988 163 RENR-QLQKELLQLIQETQALE-------AIKSKLENRKQRLKEEQWYLEA 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
585-844 |
3.29e-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: 45.04 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 585 RFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHD 664
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 665 REE----------FYNQSQELQTKLEDcRNMIAELRIEL--KKANNKVCHTELL------------------LSQVSQKL 714
Cdd:TIGR00606 908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 715 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QNKHSDTTKEVEMMKAAYRKELekNRSHVLQQTQrldTSQKriL 789
Cdd:TIGR00606 987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQ---EHQK--L 1059
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375023171 790 ELESHLAKKDH-LLLEQKKYLEDVKLQARGQL-----QAAESRYEAQKRITQVFELEILDL 844
Cdd:TIGR00606 1060 EENIDLIKRNHvLALGRQKGYEKEIKHFKKELrepqfRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
585-835 |
8.09e-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: 43.57 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 585 RFKRQQHALRNRRLLRKVIKAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQ---EQRDtmvtklhsqiRQL 661
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 662 QHDREEfynqSQELQTKLEDCRNMIAELRielkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 741
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 742 LEQLQNKHSDTTKEVEMMKaayrKELEKNRSHVLQQTQRLDTSQKRILELEshlakkdhllLEQKKYLEDVKLQA---RG 818
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKAteeRS 566
|
250
....*....|....*..
gi 1375023171 819 QLQAAESRYEAQKRITQ 835
Cdd:pfam17380 567 RLEAMEREREMMRQIVE 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
584-849 |
9.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 584 ERFKRQQHALRNR-RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTM---VTKLHSQIR 659
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELeaeLAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 660 QL-QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQ---------------- 722
Cdd:COG4717 181 ELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaalla 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 723 -----------QMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNR-------------------S 772
Cdd:COG4717 261 llglggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelL 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375023171 773 HVLQQTQRLDTSQKRILELESHLaKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQvfelEILDLYGRLE 849
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLE 412
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
605-700 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 605 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNqlQEQRDTMVTKLHSQIRQLQHDREEFynqSQELQTKLedcRN 684
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 1375023171 685 MIAELRIELKKANNKV 700
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
595-815 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 595 NRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQE 674
Cdd:TIGR04523 420 EKELLEKEIER--LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 675 L-----QTKleDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYL 742
Cdd:TIGR04523 498 LkklneEKK--ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQ 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375023171 743 EQ--LQNKHS---DTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 815
Cdd:TIGR04523 576 TQksLKKKQEekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
587-798 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 587 KRQQHALRNRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ---- 662
Cdd:COG4942 41 KELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 663 ----------HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFlnrqll 732
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375023171 733 vlgevnelyLEQLQNKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTSQKRILELESHLAKK 798
Cdd:COG4942 190 ---------LEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
584-844 |
2.69e-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: 41.06 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 584 ERFKRQQHALRNRRLLRKVIKAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYNQLQE------------------ 645
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAewkelekeeereederil 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 646 ----QRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIelkkannkvchtELLLSQVSQKlsnseSVQ 721
Cdd:pfam13868 159 eylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA------------KLYQEEQERK-----ERQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 722 QQMEFLNRQLLVLGEVNELYLEQLQNKhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDtsQKRILELESHLAKKDHL 801
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQIELK--------ERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEH 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1375023171 802 LLEQKKYLEDVKLQARGQ----LQAAESRYEAQKRITQVFELEILDL 844
Cdd:pfam13868 292 RRELEKQIEEREEQRAAEreeeLEEGERLREEEAERRERIEEERQKK 338
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
619-829 |
2.74e-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: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 619 LKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTK--LHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKA 696
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDK 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 697 NNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQNKHSDTTKEvEMMKAayrkeLEKNRS 772
Cdd:pfam10174 599 DKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-ELMGA-----LEKTRQ 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 773 HVLQQTQRLDTSQKRILELESHLAKkdhLLLEQKKYLEDV---KLQArgqLQAAESRYEA 829
Cdd:pfam10174 670 ELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
593-836 |
2.88e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 593 LRNRRLLRKVIKAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVSLQ---KEQAR---------YNQLQEQR- 647
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISYTspdPELAAavanalaeaYLEQNLELr 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 648 -----------DTMVTKLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLL 707
Cdd:COG3206 170 reearkaleflEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 708 ---SQVSQKLSNSESVQQqmefLNRQLLVL-GEVNELyLEQLQNKHSDtTKEVEMMKAAYRKELEKNRSHVLQQTQ-RLD 782
Cdd:COG3206 250 gsgPDALPELLQSPVIQQ----LRAQLAELeAELAEL-SARYTPNHPD-VIALRAQIAALRAQLQQEAQRILASLEaELE 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375023171 783 TSQKRILELESHLAKKDHLLLE----QKKYLEdvkLQArgQLQAAESRYEA-QKRITQV 836
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAElpelEAELRR---LER--EVEVARELYESlLQRLEEA 377
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
605-731 |
3.97e-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: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 605 AAALEEHNAAmKDQLKLQEKDIQmwkvSLQKE----QARYNQLQEQ--------------------------------RD 648
Cdd:COG3883 47 EELNEEYNEL-QAELEALQAEID----KLQAEiaeaEAEIEERREElgeraralyrsggsvsyldvllgsesfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 649 TMVTKLHSQ----IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLsnsESVQQQM 724
Cdd:COG3883 122 SALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQL 198
|
....*..
gi 1375023171 725 EFLNRQL 731
Cdd:COG3883 199 AELEAEL 205
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
647-785 |
4.02e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 647 RDTMVTKLHSQ---IRQLQHDREEFYNQSQELQTklEDCRNMIAELRI---ELKKANNKVCHTELLLSQVSQKLSNS--- 717
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDI--ERLYRMIDILNDaqqQIKWTNQPRIYLEVALVKLCEQAAASpey 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375023171 718 ----ESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVemmKAAYRKELEKNrSHVLQQTQRLDTSQ 785
Cdd:PRK05563 368 dtelEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNK---KKKYKVPRGKI-YKVLKEATRQDLEL 435
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
641-727 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 641 NQLQEQRdTMVTKLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRIELK-KANNKVCHTELLLSQVSQKLSn 716
Cdd:cd16855 8 QQLEELR-QRTQETENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 1375023171 717 sesvQQQMEFL 727
Cdd:cd16855 86 ----QLRMELA 92
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
638-837 |
4.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 638 ARYNQLQEQRDTMVTKLHSQ---IRQLQ---HDREEFYN--------------------QSQELQTKLEDCRNMIAELRI 691
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLsfdVQKLQrlhQAFSRFIGshlavafeadpeaelrqlnrRRVELERALADHESQEQQQRS 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 692 ELKKANNKVCHTELLLSQVSqkLSNSESVQQQMEFLNRQLLVLgEVNELYLEQlqnkHSDTTKEVEMMKAAYR---KELE 768
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA-EEAKRFVQQ----HGNALAQLEPIVSVLQsdpEQFE 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 769 KNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------------------LLEQKKYLEDVKLQARGQLQAAESRYeAQ 830
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsyedaaemlaknsdlnekLRQRLEQAEQERTRAREQLRQAQAQL-AQ 1017
|
....*..
gi 1375023171 831 KriTQVF 837
Cdd:PRK04863 1018 Y--NQVL 1022
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
587-788 |
5.12e-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: 39.98 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 587 KRQQHALRNRRLlRKVIKAA-----ALEEHNAAMKDQLKLQEKDIqMWKVSLQKEQARYNQLQeqrdtmvtklhSQIRQL 661
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDApaelrELRQELAALQAKAEAAPKEI-LASLSLEELEQRLLQTS-----------AQLQEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 662 QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNEL 740
Cdd:pfam12795 98 QNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1375023171 741 YLEQLQNkhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRI 788
Cdd:pfam12795 169 EQELLSN---------NNRQDLLKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
614-846 |
5.35e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 614 AMKDQLKLQEKDIQMWKVSLQKEQARYNQ----LQEQRDTMVTKLH---SQIRQLQHDREEFYNQSQELQ-------TKL 679
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEelkeLAEKRDELNAQVKelrEEAQELREKRDELNEKVKELKeerdelnEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 680 EDCRNMIAELRIELKKANNKvchtELLLSQVSQKLSNSESVQQ--------QMEFLNR-------------QLLVLGEVN 738
Cdd:COG1340 88 NELREELDELRKELAELNKA----GGSIDKLRKEIERLEWRQQtevlspeeEKELVEKikelekelekakkALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 739 ELY--LEQLQNKHSDTTKEV-----------EMMKAAY------RKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD 799
Cdd:COG1340 164 ELRaeLKELRKEAEEIHKKIkelaeeaqelhEEMIELYkeadelRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1375023171 800 HLLLEQKKYLEDVKLQA-----RGQLQAAESRYEAQKRITqvFElEILDLYG 846
Cdd:COG1340 244 KELKKLRKKQRALKREKekeelEEKAEEIFEKLKKGEKLT--TE-ELKLLQK 292
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
605-850 |
6.97e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 605 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQaryNQLQEQRDTMvtklhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 683
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESEN---AELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 684 NMIAELRIELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQNKHSDTTKevemmkaay 763
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 764 RKELEKNRSHVLQQTQRLDTSQKRileLESHLAKKDHLLLEQKKYLEDVKlqarGQLQAAEsryEAQKRITQVFELEILD 843
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRN---VERQLSTLQAQLSDMKKKLEEDA----GTLEALE---EGKKRLQRELEALTQQ 560
|
250
....*....|...
gi 1375023171 844 L------YGRLEK 850
Cdd:pfam01576 561 LeekaaaYDKLEK 573
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
658-844 |
7.28e-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: 39.24 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 658 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVC-------HTELLLSQVSQKLSNSESVQQQMEFLNRQ 730
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeeleRTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 731 LLVLGEVNELYLEQLQNKHSDTTkevEMMKAAYRKELEKNRSHVLQQT------QRLDTSQKRILELESHL--------- 795
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAK---EIAEEADRKYEEVARKLVVVEGdleraeERAELAESKIVELEEELkvvgnnlks 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1375023171 796 --AKKDHLLLEQKKYLEDVK-LQARgqLQAAESRYEAQKRITQVFELEILDL 844
Cdd:pfam00261 160 leASEEKASEREDKYEEQIRfLTEK--LKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
715-832 |
8.59e-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: 37.66 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375023171 715 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN--KHSDTTKEVEMMKAAYRKELEKNRSHVLQQ----TQRLDTSQKRI 788
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQELAILEAENskAEVETLKAEIEEMAQNLRDLELDLVTLRSEkenlTKELQKKQERV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1375023171 789 LELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESRYEAQKR 832
Cdd:pfam10473 97 SELESLNSSLENLLEE----KEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| |
