|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-172 |
1.22e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.31 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 10 TQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARV 89
Cdd:COG0666 100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 90 NVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQALSRRRRGGQRLVQHPDLA 169
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
|
...
gi 526118251 170 SQA 172
Cdd:COG0666 260 AAA 262
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-152 |
4.30e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.83 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 9 STQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGAR 88
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526118251 89 VNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQAL 152
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
13-148 |
2.57e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.82 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVT 92
Cdd:COG0666 70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 93 DKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 148
Cdd:COG0666 150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
13-136 |
5.00e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 94.64 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVT 92
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 526118251 93 DKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYA 136
Cdd:COG0666 117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
34-126 |
9.38e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 34 LHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRgARVNVTDkNDKSALILACEKGSAEVAE 113
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 526118251 114 LLLSHGADAGAVD 126
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
10-133 |
3.67e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 88.86 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 10 TQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARV 89
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 526118251 90 NVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDAL 133
Cdd:COG0666 246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
9-93 |
2.43e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.85 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 9 STQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDvlDNDGRTPLMIASLGGHAAICSQLLQRGAR 88
Cdd:pfam12796 9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKLLLEKGAD 86
|
....*
gi 526118251 89 VNVTD 93
Cdd:pfam12796 87 INVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-125 |
3.78e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.41 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVT 92
Cdd:PHA02875 118 MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYF 197
|
90 100 110
....*....|....*....|....*....|....
gi 526118251 93 DKN-DKSALILACEKGSAEVAELLLSHGADAGAV 125
Cdd:PHA02875 198 GKNgCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
67-136 |
1.51e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.51e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 67 LMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHgADAGAVDStGHDALHYA 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
541-876 |
6.31e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 541 LGELGRERQRLQRE------LQSLSQRLQREfvpkpQAQVQLQQLRQsvglLTNELAMEKEATEKLRKLLASQssglrgl 614
Cdd:COG1196 195 LGELERQLEPLERQaekaerYRELKEELKEL-----EAELLLLKLRE----LEAELEELEAELEELEAELEEL------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 615 wdclpadlvgeRSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALEQ 694
Cdd:COG1196 259 -----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----------RRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 695 DLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAaslrQHEKTRGSLVAQAQAWGQELKALLEKYNTAC 774
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 775 REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEV 854
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340
....*....|....*....|..
gi 526118251 855 LAIRGENARLALQLQDSQKNHE 876
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-870 |
6.79e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 211 KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGSSLRpggdgmeqgcPKDLLAE 290
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----------KLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 291 STQELKKQQQAAATVnpVLAPKKAEDSAPGKIQYEVHGRSQPEEQgppqspaSETIRKA---TGQQLTTNGAQTfgpdha 367
Cdd:TIGR02168 338 ELAELEEKLEELKEE--LESLEAELEELEAELEELESRLEELEEQ-------LETLRSKvaqLELQIASLNNEI------ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 368 dQLPAGQKESSQVlGVEPGGTVAEPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKM 447
Cdd:TIGR02168 403 -ERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 448 EARLERVLARLEWAKAGLQ--------VKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGE------K 513
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEnlnaakK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 514 ALGGLAKGQLEK-EMSVLRLSNSNLLEelgelGRERQRLQRELQSLSQRLQREFVPkPQAQVQLQQLRQSVgLLTNELAm 592
Cdd:TIGR02168 561 AIAFLKQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 593 ekEATEKLRKLlasqssGLRGLWDCLPADLVGERSAQSKAAES-----------LEELRACISTLVDRHREAQQVLARLQ 661
Cdd:TIGR02168 633 --NALELAKKL------RPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreIEELEEKIEELEEKIAELEKALAELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 662 EENQQLRGSLSPCREPGTSLkapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAAs 741
Cdd:TIGR02168 705 KELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE- 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 742 lrqHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAEL 821
Cdd:TIGR02168 780 ---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 526118251 822 LKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD 870
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
13-148 |
3.20e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.55 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFL-DVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNV 91
Cdd:PHA02875 51 IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 526118251 92 TDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 148
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
538-873 |
3.53e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 538 LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA------QVQLQQLRQSvglltnELAMEKEATEKLRKLLASQSSGL 611
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGY------ELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 612 RGLWdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVlaRLQEENQQLRGSLSPCREpgtSLKAPASpQVAA 691
Cdd:TIGR02169 250 EEEL----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLER---SIAEKER-ELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 692 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYN 771
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 772 TACREVGRLREavaeERRRSGDLAAQAaeqerqasemRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLS 851
Cdd:TIGR02169 396 KLKREINELKR----ELDRLQEELQRL----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
330 340
....*....|....*....|..
gi 526118251 852 EEVLAIRGENARLALQLQDSQK 873
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
13-144 |
6.99e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 64.20 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVT 92
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 526118251 93 DKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 144
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-137 |
7.32e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.46 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 30 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAA-----ICSQLLQRGARVNVTDKNDKSALILA- 103
Cdd:PHA03100 35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAi 114
|
90 100 110
....*....|....*....|....*....|....*
gi 526118251 104 -CEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 137
Cdd:PHA03100 115 sKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
38-118 |
1.59e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 64.92 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 38 ASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLS 117
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 526118251 118 H 118
Cdd:PTZ00322 170 H 170
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
13-134 |
5.22e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.73 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLLLCDHEAFLDVLDNDGRTPLmiaslggHAAICSQ-------- 81
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPL-------HLYLYNAttldvikl 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 82 LLQRGARVNVTDKNDKSALiLACEKG---SAEVAELLLSHGADAGAVDSTGHDALH 134
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-891 |
7.43e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 688 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRgslvaqaqawgQELKALL 767
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-----------QDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 768 EKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKL 847
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 526118251 848 EQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAAR 891
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-802 |
8.88e-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: 62.77 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 601
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 602 KLLASQSSG---LRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPG 678
Cdd:TIGR02168 775 EELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 679 TSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 758
Cdd:TIGR02168 855 ESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 526118251 759 WgQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQE 802
Cdd:TIGR02168 931 L-EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-864 |
1.37e-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: 62.38 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 516 GGLAKGQLEKEMSVLRLSNS--NLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAME 593
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 594 KEATEKLRKLLASQSSglrglwdclpadlvgersAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSP 673
Cdd:TIGR02168 739 EAEVEQLEERIAQLSK------------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 674 CREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRgslv 753
Cdd:TIGR02168 801 LREALDELRA----ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 754 aqaqawgQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGAC 833
Cdd:TIGR02168 873 -------SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330 340 350
....*....|....*....|....*....|....*....
gi 526118251 834 RDK--------EAKIKELLKKLEQLSEEVLAIRGENARL 864
Cdd:TIGR02168 946 SEEysltleeaEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
632-878 |
2.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 632 AAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKA---PASPQVAALEQDLGKLEEELRAVQA 708
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 709 TMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEER 788
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 789 RRsgdLAAQAAEQERQASEM--------RGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGE 860
Cdd:TIGR02168 393 LQ---IASLNNEIERLEARLerledrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250
....*....|....*...
gi 526118251 861 NARLALQLQDSQKNHEEI 878
Cdd:TIGR02168 470 LEEAEQALDAAERELAQL 487
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
13-144 |
2.71e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.45 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAAS--SGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHA--AICSQLLQRGAR 88
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526118251 89 VNV----------------TDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 144
Cdd:PHA03100 169 INAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
524-849 |
2.86e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 524 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAqvQLQQLRQSVGLLTNELAMEKEATEK 599
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAFAPDPEA--ELAALRQRRSELERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 600 LRKLLASQSSGLRGLWDCLP-ADLVGERSaqskAAESLEELRAcistLVDRHREAQQVLARLQEENQQLRGSLSPCREPg 678
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKLLPqANLLADET----LADRLEELRE----ELDAAQEAQAFIQQHGKALAQLEPLVAVLQSD- 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 679 tslkaPAspQVAALEQDLGKLEEELRAVQAT---------------------MSGKSQEIG-KLKQLLYQAteEVAELRA 736
Cdd:COG3096 933 -----PE--QFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyedavgLLGENSDLNeKLRARLEQA--EEARREA 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 737 REAasLRQHEktrgslvAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQER-----QASEMRGR 811
Cdd:COG3096 1004 REQ--LRQAQ-------AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRdelheELSQNRSR 1074
|
330 340 350
....*....|....*....|....*....|....*...
gi 526118251 812 SEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 849
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
522-810 |
3.84e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 601
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 602 KLLASQSSGLRglwdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcrepgtsl 681
Cdd:COG1196 344 EELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 682 kapaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 761
Cdd:COG1196 408 ------AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 526118251 762 ELKALLEKyntacrevgRLREAVAEERRRSGDLAAQAAEQERQASEMRG 810
Cdd:COG1196 482 LLEELAEA---------AARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
519-864 |
6.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 519 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 598
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 599 KLR-----KLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACIstLVDRHREAQQVLARLQEENQQLRGSLSP 673
Cdd:COG1196 502 DYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 674 CREPGTSLKAPASPQ------VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAA---SLRQ 744
Cdd:COG1196 580 DKIRARAALAAALARgaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 745 HEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKE 824
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 526118251 825 KMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARL 864
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
523-865 |
8.70e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 523 LEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRk 602
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 603 llaSQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslk 682
Cdd:PRK02224 356 ---ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 683 apaspQVAALEQDLGKLEEELRAVQA---------------------TMSGKSQEIGKLKQLLYQATEEVAELRAR--EA 739
Cdd:PRK02224 427 -----REAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERleRA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 740 ASLRQHEKTRGSLVAQAQAWGQELKallEKYNTACREvgrlREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQ-FEKT 818
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEV 574
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 526118251 819 AELLKEKMEhlIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLA 865
Cdd:PRK02224 575 AELNSKLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
8-137 |
1.21e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.44 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 8 SSTQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAIcsQLLQRGA 87
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNA 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 526118251 88 RVNVTDKNDKSALILA----CEKgsaEVAELLLSHGADAGAVDSTGHDALHYAL 137
Cdd:PHA02874 246 SINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTAF 296
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
7-137 |
2.15e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.67 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 7 CSSTQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRG 86
Cdd:PHA02874 101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 526118251 87 ARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 137
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
13-128 |
4.03e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 56.60 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCAS------------------SVLLLCDHEAFLDVLDNDGRTPLMIASLGG 74
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 526118251 75 HAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDST 128
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
524-849 |
4.06e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 524 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAQvqLQQLRQSVGLLTNELAMEKEATEK 599
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigsHLAVAFEADPEAE--LRQLNRRRVELERALADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 600 LRKLLASQSSGLRGLWDCLP-ADLVGERSAQSKAAESLEELracistlvDRHREAQQVLARLQEENQQLRGSLSPCREPg 678
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPrLNLLADETLADRVEEIREQL--------DEAEEAKRFVQQHGNALAQLEPIVSVLQSD- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 679 tslkaPAspQVAALEQDLGKLEEELRAVQ---------------------ATMSGKSQEIG-KLKQLLYQATEEVAELR- 735
Cdd:PRK04863 934 -----PE--QFEQLKQDYQQAQQTQRDAKqqafaltevvqrrahfsyedaAEMLAKNSDLNeKLRQRLEQAEQERTRARe 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 736 -AREAAS-LRQHEKTRGSLVAQAQAWGQELKALLEKYNtacrEVGRLREAVAEERrrsgdLAAQAAEQERQASEMRGRSE 813
Cdd:PRK04863 1007 qLRQAQAqLAQYNQVLASLKSSYDAKRQMLQELKQELQ----DLGVPADSGAEER-----ARARRDELHARLSANRSRRN 1077
|
330 340 350
....*....|....*....|....*....|....*.
gi 526118251 814 QFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 849
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
13-137 |
6.10e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.61 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQ-LLQRGARVNV 91
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNS 437
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 526118251 92 TDKNDKSALILACEKG-SAEVAELLLSHGADAGAVDSTGHDALHYAL 137
Cdd:PHA02876 438 KNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-825 |
6.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 449 ARLERVLARLEWAKAGLQVkpEVPSQESREGALKAAPGSIKQDEEKekrvpgaqgepLGALGGEKALGGLAKGQLEKEMS 528
Cdd:COG1196 239 AELEELEAELEELEAELEE--LEAELAELEAELEELRLELEELELE-----------LEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 529 VLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREfvpKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQS 608
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 609 SGLRglwdclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQ 688
Cdd:COG1196 383 ELAE--------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 689 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLe 768
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL- 522
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 526118251 769 kyntaCREVGRLREAVAEERRrsgdlAAQAAEQERQASEMRGRSEQFEKTAELLKEK 825
Cdd:COG1196 523 -----AGAVAVLIGVEAAYEA-----ALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
459-846 |
1.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 459 EWAKAGLQVKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGEKALGGLAKGQLEKEmsvlrlSNSNLL 538
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA------KKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 539 EELGELGRERQRLQRELQSLSQRLQrEFVPKPQAQVQLQQLRQsvglltnelAMEKEATEKLRKLL-ASQSSGLRGLWDC 617
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK---------AEEAKKADEAKKAEeAKKADEAKKAEEK 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 618 LPADLVGERSAQSKAAE--SLEELRACISTLVDRHREAQqVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQD 695
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 696 LGKLEEELRAVQATMSGKSQEIGKLKQLlyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR 775
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 776 EVGRLREAVAEERRRSGDLAA--------------QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK 841
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKaeeenkikaeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
....*
gi 526118251 842 ELLKK 846
Cdd:PTZ00121 1783 EELDE 1787
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
16-137 |
1.50e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.26 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 16 LLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKN 95
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 526118251 96 DksALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 137
Cdd:PLN03192 624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
688-895 |
1.79e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 688 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREA---ASLRQHEKTRGSLVAQAQAWGQELK 764
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 765 ALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELL 844
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 526118251 845 KKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYME 895
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
522-893 |
2.41e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEmsvLRLSNSnlleELGELGRERQRLQRELQSLSQrlqrefvpkpqaqvQLQQLRQSVGLLTNELAMEKEATEKlr 601
Cdd:pfam15921 346 ELEKQ---LVLANS----ELTEARTERDQFSQESGNLDD--------------QLQKLLADLHKREKELSLEKEQNKR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 602 kllasqssglrgLWDclpadlvgersAQSKAAESLEELRaciSTLVDRHREAQQVLARLQ----EENQQLRGSLSPCREP 677
Cdd:pfam15921 403 ------------LWD-----------RDTGNSITIDHLR---RELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 678 GTSLKAPAS--PQVAALEQDLGKLEEELRAVQATMSGKSQEIGKL------KQLLYQATE-EVAELRAREAASLR--QHE 746
Cdd:pfam15921 457 NESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQelQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 747 KTRGSLVAQAQAWGQELKALLEKYNTAC----REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFektaELL 822
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF----KIL 612
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526118251 823 KEKmehligacrdKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEI---ISTYRNHLLNAARGY 893
Cdd:pfam15921 613 KDK----------KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
13-148 |
5.85e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.10 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLH-WAASSGCASSVL-LLCDHEAFLDVLDNDGRTPL--MIASLGGHAAICSQLLQRGAR 88
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAvLLKSRNANVELLrLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCD 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526118251 89 VNVTDKNDKSALILACEKGS--AEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 148
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
8-103 |
6.22e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.10 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 8 SSTQCVKVLLQHGANEDAVDAENRSPLHWAAS-SGCASSVLL-LCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQR 85
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279
|
90
....*....|....*...
gi 526118251 86 GARVNVTDKNDKSALILA 103
Cdd:PHA03095 280 GADINAVSSDGNTPLSLM 297
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
82-136 |
6.87e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 6.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 82 LLQRG-ARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYA 136
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
10-142 |
7.38e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 10 TQCVKVLLQHGANEDAVDAEN-RSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGAR 88
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 89 VNVTDKNDKSALILACEK-GSAEVAELLLSHGADAGAVDST-GHDALHYALHTQDK 142
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERK 282
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
30-83 |
7.87e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 7.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 526118251 30 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLL 83
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
13-140 |
7.92e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.72 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASS------VLLLCDHEAfldvLDNDGRTPLMIASLGG--HAAICSQLLQ 84
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRArivrelIRAGCDPAA----TDMLGNTPLHSMATGSscKRSLVLPLLI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526118251 85 RGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTG------------HDALHYALHTQ 140
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGntplslmvrnnnGRAVRAALAKN 313
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-878 |
1.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 698 KLEEELRAVQATmsgKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREV 777
Cdd:PTZ00121 1213 KAEEARKAEDAK---KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 778 GRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAI 857
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
170 180
....*....|....*....|.
gi 526118251 858 RGENARLALQLQDSQKNHEEI 878
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEK 1390
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-865 |
1.08e-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: 52.75 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEMSVLRLSNsnLLEELGELGRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGlltnelAMEKEATEKLR 601
Cdd:TIGR02168 224 ELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVS------ELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 602 KLLASQSsglrglwdcLPADLVGERSAQSKAAESLEELRACISTLVDRHR----EAQQVLARLQEENQQLRgslspcrep 677
Cdd:TIGR02168 289 ELYALAN---------EISRLEQQKQILRERLANLERQLEELEAQLEELEskldELAEELAELEEKLEELK--------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 678 gtslkapasPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQ 757
Cdd:TIGR02168 351 ---------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 758 AWGQELKALLEKYNTAcrEVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacRDKE 837
Cdd:TIGR02168 418 RLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARL 491
|
330 340
....*....|....*....|....*...
gi 526118251 838 AKIKELLKKLEQLSEEVLAIRGENARLA 865
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
589-886 |
1.15e-06 |
|
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: 52.66 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 589 ELAMEKEATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDR---HREAQQVLARLQE-EN 664
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEElRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 665 QQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQ---------------ATE 729
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssieeqrrllqtlhSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 730 EVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVA-------EERRRSGDLAAQAAEQE 802
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAtidtrtsAFRDLQGQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 803 RQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKiKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 882
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
....
gi 526118251 883 RNHL 886
Cdd:TIGR00618 514 NPAR 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
631-821 |
1.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 631 KAAESLEELRACISTLvdRHREAQQVLARLQEENQQLRGSLSpcrepgtSLKApaspQVAALEQDLGKLEEELRAVQATM 710
Cdd:COG4913 266 AARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA-------RLEA----ELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 711 SG-KSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERR 789
Cdd:COG4913 333 RGnGGDRLEQLEREIERLERELEERERR-----------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|..
gi 526118251 790 RSGDLAAQAAEQERQAsemrgRSEQFEKTAEL 821
Cdd:COG4913 402 ALEEALAEAEAALRDL-----RRELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-892 |
2.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 648 DRHREAQQVLARLQEENQQLRGSLspcrepgtslkapaspqvAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQA 727
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL------------------AALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 728 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-----ELKALL--EKYNTACREVGRLREAVAEERRRSGDLAAQAAE 800
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 801 QERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIIS 880
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|..
gi 526118251 881 TYRNHLLNAARG 892
Cdd:COG4942 242 RTPAAGFAALKG 253
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
10-127 |
2.52e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 51.03 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 10 TQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASlgGHA---AICSQLLQRG 86
Cdd:PHA02878 181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHG 258
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 526118251 87 ARVNVTDK-NDKSALILACEkgSAEVAELLLSHGADAGAVDS 127
Cdd:PHA02878 259 VDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNS 298
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
521-817 |
4.62e-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: 50.84 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 521 GQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEK-----E 595
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 596 ATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCR 675
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 676 EPGTSLKAPASpQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRA--REAASLRQHEKTRGSLV 753
Cdd:TIGR02169 879 DLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQ 957
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526118251 754 AQAQAWGQELKALLEKYNTACREvgrlreaVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEK 817
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQE-------YEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-138 |
5.57e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 8 SSTQCVKVLLQHGANEDAVDAENRSPLHWAASSGC-ASSVLLLCDHEAFLDVLDNDGRTPLMIAS-LGGHAAICSQLLQR 85
Cdd:PHA02876 285 SLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLEL 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 526118251 86 GARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALH 138
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC 417
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
14-154 |
8.18e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 49.68 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 14 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNvtd 93
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526118251 94 KNDKSaLILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAlhTQDKALWRHLQQALSR 154
Cdd:PHA02876 239 KNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA--SQAPSLSRLVPKLLER 296
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
686-883 |
1.50e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 686 SPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKA 765
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----AQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 766 LLEKYNTACREVGRLREAVAEERRRSGDLAA-----QAAEQERQASEMRGRSEQ--FEKTAELLK--EKMEHLIgacrDK 836
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKlrkeiERLEWRQQTEVLSPEEEKelVEKIKELEKelEKAKKAL----EK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 526118251 837 EAKIKELLKKLEQLSEEVLAIRGENARLAlqlQDSQKNHEEIISTYR 883
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELA---EEAQELHEEMIELYK 202
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
13-141 |
1.52e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 48.51 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAI--CSQLLQRGARVN 90
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 526118251 91 VTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQD 141
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
537-737 |
1.62e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 537 LLEELGELGRERQRLQRELQSLSQRLQRefVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLwd 616
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 617 clpadlvgERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQDL 696
Cdd:COG4913 329 --------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 526118251 697 GKLEEELRAVQAtmsgksqEIGKLKQLLYQATEEVAELRAR 737
Cdd:COG4913 401 EALEEALAEAEA-------ALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
13-85 |
2.38e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 2.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICsQLLQR 85
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV-QLLSR 169
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
62-94 |
2.81e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.89 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|....
gi 526118251 62 DGRTPLMIASL-GGHAAICSQLLQRGARVNVTDK 94
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
625-877 |
3.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 625 ERSAQSKAAESLEELRAcistlVDRHREAQQVLARLQEE--NQQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEE 702
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKK-----AEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 703 LRAVQATmsgKSQEIGKLKQLLYQATE----EVAELRAREA------ASLRQHEKTRGSLVA--QAQAWGQELKALLEKY 770
Cdd:PTZ00121 1290 KKADEAK---KAEEKKKADEAKKKAEEakkaDEAKKKAEEAkkkadaAKKKAEEAKKAAEAAkaEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 771 NTAcrevgrlrEAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEhligacrdKEAKIKELLKKLEQL 850
Cdd:PTZ00121 1367 EAA--------EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA--------AKKKADEAKKKAEEK 1430
|
250 260
....*....|....*....|....*...
gi 526118251 851 SE-EVLAIRGENARLAlqlQDSQKNHEE 877
Cdd:PTZ00121 1431 KKaDEAKKKAEEAKKA---DEAKKKAEE 1455
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
519-882 |
3.62e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 519 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEA-- 596
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 597 -TEKLRKLLASQSSGLRG-LWDCLPADLVgERSAQSKAAESLEELRACISTLVDRHReaQQVLARLQEENQQLRgSLSPC 674
Cdd:pfam01576 289 kAEKQRRDLGEELEALKTeLEDTLDTTAA-QQELRSKREQEVTELKKALEEETRSHE--AQLQEMRQKHTQALE-ELTEQ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 675 REPGTSLKAPASPQVAALEQDLGKLEEELRAVQatmSGKSQEIGKLKQLLYQateeVAELRAReaasLRQHEKTRGSLVA 754
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQ----LQELQAR----LSESERQRAELAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 755 QAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR 834
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 526118251 835 DKE-------AKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 882
Cdd:pfam01576 514 NVErqlstlqAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
47-103 |
4.04e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 526118251 47 LLLCDHEAfLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILA 103
Cdd:pfam13857 1 LLEHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-863 |
4.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 698 KLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREV 777
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 778 GRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEaKIKELLKKLEQL--SEEVL 855
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK-KEAEEKKKAEELkkAEEEN 1728
|
....*...
gi 526118251 856 AIRGENAR 863
Cdd:PTZ00121 1729 KIKAEEAK 1736
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
16-70 |
4.73e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 16 LLQHG-ANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIA 70
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
63-116 |
7.00e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 7.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 526118251 63 GRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLL 116
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
539-791 |
1.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 539 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELamekeateklrkllasqssglrglwdcl 618
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 619 padlvgersaqSKAAESLEELRACISTLVDRHREAQQVLARLQEE-NQQLRGSLSPCREPGTS-LKAPASPQ-------- 688
Cdd:COG4942 72 -----------RALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLAlLLSPEDFLdavrrlqy 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 689 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLE 768
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260
....*....|....*....|...
gi 526118251 769 KYNTACREVGRLREAVAEERRRS 791
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
694-876 |
1.42e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 694 QDLGKLEEELRAVQATMSGKSQEIGKLKQLlyqaTEEVAELRAREAAslRQHEKTRGSLVAQAQAWGQELKALLEKYNTA 773
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 774 CREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEE 853
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|...
gi 526118251 854 VLAIRGENARLALQLQDSQKNHE 876
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
539-893 |
1.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 539 EELGELGRERQRLQRELQSLSQRLQREFVPKP--QAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLWD 616
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 617 CLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAAL---- 692
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllal 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 693 -----------------------------------EQDLGKLEEELRAVQATMSGKSQEIGKLKQL-------------- 723
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeelle 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 724 LYQATEEVAELR-----AREAASLRQHEKTRGSLVAQAQAWG-QELKALLEKYNTACREVGRLREavAEERRRSGDLAAQ 797
Cdd:COG4717 342 LLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEE--LEEQLEELLGELE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 798 AAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK---------ELLKKLEQLSEEVLAIRGENARLALQL 868
Cdd:COG4717 420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqleedgelaELLQELEELKAELRELAEEWAALKLAL 499
|
410 420
....*....|....*....|....*
gi 526118251 869 QDSQKNHEEIISTYRNHLLNAARGY 893
Cdd:COG4717 500 ELLEEAREEYREERLPPVLERASEY 524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
625-878 |
1.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 625 ERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASpQVAALEQDLGKLEEELR 704
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 705 AVQATMSGKSQEIGKLKQLLyqateEVAELRAREAASLRQHEKTRgslvaqaqawgQELKALLEKYNTACREV----GRL 780
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEI-----EELEEKVKELKELKEKAEEY-----------IKLSEFYEEYLDELREIekrlSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 781 REAVAEERRRSGDLA---AQAAEQERQASEMRGRSEQFEKTAELL---KEKMEHLIG-----ACRDKE---AKIKELLKK 846
Cdd:PRK03918 320 EEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERlkkrlTGLTPEkleKELEELEKA 399
|
250 260 270
....*....|....*....|....*....|..
gi 526118251 847 LEQLSEEVLAIRGENARLALQLQDSQKNHEEI 878
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
634-859 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 634 ESLEELRACISTLvDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQVAALEQDLgkLEEELRAVQATMSGK 713
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELE-----------YLRAALRLWFAQRRLEL--LEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 714 SQEIGKLKQLLYQATEEVAELRAreaaslrqhektrgslvAQAQAWGQELKALLekyntacREVGRLREAVAEERRRSGD 793
Cdd:COG4913 308 EAELERLEARLDALREELDELEA-----------------QIRGNGGDRLEQLE-------REIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 794 LAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDK----EAKIKELLKKLEQLSEEVLAIRG 859
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLER 433
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
539-886 |
1.94e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 539 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEK------------------L 600
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcsL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 601 RKLLASQSSGLRGLWDCLPADLVGERSAQSKAAE----------SLEELRACIS---TLVDRHREAQQVLARLQEENQQL 667
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAedeKLLDEKKQFEKIAEELKGKEQEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 668 RGSLSpcrepgtslkapaspqvaALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEK 747
Cdd:pfam05483 442 IFLLQ------------------AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 748 trgsLVAQAQAWGQELKALLEKYNTACREVGRLREAV----AEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAE--- 820
Cdd:pfam05483 504 ----LTQEASDMTLELKKHQEDIINCKKQEERMLKQIenleEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARsie 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 821 ---LLKEK-MEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENA--------------RLALQLQDSQKNHEEIISTY 882
Cdd:pfam05483 580 yevLKKEKqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNY 659
|
....
gi 526118251 883 RNHL 886
Cdd:pfam05483 660 QKEI 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-744 |
2.15e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 519 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 598
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 599 KLRKLLASQSSGL--RGLWDCLPADLVGERSAQS-KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcr 675
Cdd:COG4942 101 AQKEELAELLRALyrLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526118251 676 epgtSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQ 744
Cdd:COG4942 178 ----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
631-883 |
3.29e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 631 KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALE-------------QDLG 697
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 698 KLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAR---EAASLRQHEKTRGSL------VAQAQAWgQELKALLE 768
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVckiageVERSQAW-QTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 769 KYntacrevgrlREAVAeerrrsgdLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHlIGACRDKEAKIKELLKKLE 848
Cdd:COG3096 503 RY----------RSQQA--------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQR-IGQQLDAAEELEELLAELE 563
|
250 260 270
....*....|....*....|....*....|....*
gi 526118251 849 QLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 883
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
623-881 |
3.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 623 VGERSAQSKAAESLEELRACISTLVDRhrEAQQVLARLQEENQQLRGSLSPC---REPGTSLKAPASPQVAALE---QDL 696
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEerrEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 697 GKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACRE 776
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----------RDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 777 VGRLREAVAEERrrsgdLAAQAAEQerQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLA 856
Cdd:PRK02224 323 DEELRDRLEECR-----VAAQAHNE--EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260
....*....|....*....|....*
gi 526118251 857 IRGENARLALQLQDSQKNHEEIIST 881
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREE 420
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
701-878 |
5.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 701 EELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRl 780
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 781 reaVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKE-------KMEHLIGACRDKEAKIKELLKKLEQ---L 850
Cdd:PTZ00121 1669 ---KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaeekkKAEELKKAEEENKIKAEEAKKEAEEdkkK 1745
|
170 180
....*....|....*....|....*...
gi 526118251 851 SEEVLAIRGENARLALQLQDSQKNHEEI 878
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
537-898 |
5.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 537 LLEELGEL----GRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGLLtNELAMEKEATEKLRKLLASQSSGLR 612
Cdd:COG4717 51 LEKEADELfkpqGRKPELNLKELKELEEELK-------EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 613 GLWDCLPADLVGERSAQSKAA--ESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVA 690
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 691 ALEQDLGKLEEELRAVQATMSGKSQEIGKL--KQLLYQATEEVAELR--AREAASLRQHEKTRGSLVAQAQAWGQELKAL 766
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALEERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 767 LEKYNTACREVGRLREAVAEERRRSGDLAA----QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR-----DKE 837
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaeelEEE 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526118251 838 AKIKELLKKLEQL-------SEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYMEHEV 898
Cdd:COG4717 363 LQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
572-790 |
6.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 572 AQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwdclpaDLVGERSAQSKAAESLEELRAcISTLVDRHR 651
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEID-VASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 652 EAQQVLARLQEENQQLRGslspcrepgtsLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEV 731
Cdd:COG4913 672 ELEAELERLDASSDDLAA-----------LEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 526118251 732 AELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRR 790
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
631-877 |
6.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 631 KAAESLEELRACIstlvDRHREAQQVLARLQEENQQLRGSLSPC-REpgtslKAPASPQVAALEQDLGKLEEELRAVQAT 709
Cdd:PRK02224 231 QARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETeRE-----REELAEEVRDLRERLEELEEERDDLLAE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 710 MSGKSQEIGKLKQllyqateEVAELRAREaaslrqhEKTRGSLVAQAQAWGQELKallekyntacrEVGRLREAVAEERR 789
Cdd:PRK02224 302 AGLDDADAEAVEA-------RREELEDRD-------EELRDRLEECRVAAQAHNE-----------EAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 790 RSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQ 869
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
....*...
gi 526118251 870 DSQKNHEE 877
Cdd:PRK02224 437 TARERVEE 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
535-854 |
7.44e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 535 SNLLEELGELGRERQRLQRELQSLSQRL--QREFVPKPQAQVQLQQLRQSV-GLLTNELAMEKEATEKLRKLLASQSSGL 611
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 612 RGLWDclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKApaspqvaa 691
Cdd:PRK03918 542 KSLKK----ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 692 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaASLRQHEKTRgslvaqaqawgqelkallEKYN 771
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELR------------------EEYL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 772 TACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTaELLKEKMEHLIGACRDKEAKIKE-LLKKLEQL 850
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLKErALSKVGEI 748
|
....
gi 526118251 851 SEEV 854
Cdd:PRK03918 749 ASEI 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
522-858 |
7.87e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQ------REFVPKPQAQVQLQQLRQS--VGLLTNELAME 593
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqiNDLESKIQNQEKLNQQKDEqiKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 594 KEaTEKLRKLLASQSSGLRglwdclpaDLVGERSAQSKAAESL----EELRACISTLVDRHREAQQVLARLQEENQQLRG 669
Cdd:TIGR04523 426 KE-IERLKETIIKNNSEIK--------DLTNQDSVKELIIKNLdntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 670 SLSPCREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKqllyqatEEVAELrareaaslrQHEKTR 749
Cdd:TIGR04523 497 ELKKLNEEKKELEE----KVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKD---------DFELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 750 GSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMrgrseqfEKTAELLKEKMEHL 829
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL-------EKELEKAKKENEKL 629
|
330 340
....*....|....*....|....*....
gi 526118251 830 igacrdkEAKIKELLKKLEQLSEEVLAIR 858
Cdd:TIGR04523 630 -------SSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
8-41 |
8.60e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 8.60e-04
10 20 30
....*....|....*....|....*....|....
gi 526118251 8 SSTQCVKVLLQHGANEDAVDAENRSPLHWAASSG 41
Cdd:pfam13637 12 GHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
522-884 |
1.01e-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: 43.09 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 522 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQ----QLRQSVGLLTN--------- 588
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqkELEQNNKKIKElekqlnqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 589 ----ELAMEKEA--TEKLRKLLASQSSGLRGlwdcLPADLVGERSAQSKAAESLEELRACISTL------VDRH-REAQQ 655
Cdd:TIGR04523 295 seisDLNNQKEQdwNKELKSELKNQEKKLEE----IQNQISQNNKIISQLNEQISQLKKELTNSesenseKQRElEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 656 VLARLQEENQQLRGSLspcrepgTSLKApaspQVAALEQDLGK-------LEEELRAVQATMSGKSQEIGKLKQLLYQAT 728
Cdd:TIGR04523 371 EIEKLKKENQSYKQEI-------KNLES----QINDLESKIQNqeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 729 EEVAELRAREAA---SLRQHEKTRGSLvaqaqawGQELKALLEKYNtacrevgrlreavaEERRRSGDLAAQAAEQERQA 805
Cdd:TIGR04523 440 SEIKDLTNQDSVkelIIKNLDNTRESL-------ETQLKVLSRSIN--------------KIKQNLEQKQKELKSKEKEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 806 SEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLAL--QLQDSQKNHEEIISTYR 883
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQTQK 578
|
.
gi 526118251 884 N 884
Cdd:TIGR04523 579 S 579
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
643-782 |
1.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 643 ISTLVDRHREAQQVLARLQEENQQLRGSLSpcREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKS-------Q 715
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialrA 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526118251 716 EIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLRE 782
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
451-884 |
1.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 451 LERVLARLEWAKAGLQVKpeVPSQESREGALKAapgSIKQDEEKEKRVPGAQGEPLG--ALGGEKALGGLAKGQLEKEMS 528
Cdd:PRK03918 243 LEKELESLEGSKRKLEEK--IRELEERIEELKK---EIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 529 VL---------RLSN-SNLLEELGELGRERQRLQRELQSLSQRLqREFVPKPQAQVQLQQLRQSVGLLTNELAMEK---- 594
Cdd:PRK03918 318 RLeeeingieeRIKElEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKEleel 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 595 -----EATEKLRKLLASQSSgLRGLWDCLPADLVGERSAQSKA------------AESLEELRACISTLVDRHREAQQVL 657
Cdd:PRK03918 397 ekakeEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 658 ARLQEENQQLRGSLSPCREPgTSLKAPASpQVAALEQDLGKL--------EEELRAVQATMSGKSQEIGKLKQLLYQATE 729
Cdd:PRK03918 476 RKLRKELRELEKVLKKESEL-IKLKELAE-QLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 730 EVAELRAREAAsLRQHEKTRGSLVAQAQAWGQELKALLEkyntacREVGRLREAVAEErrrsgdLAAQAAEQERQASEmr 809
Cdd:PRK03918 554 LKKKLAELEKK-LDELEEELAELLKELEELGFESVEELE------ERLKELEPFYNEY------LELKDAEKELEREE-- 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 810 grsEQFEKTAELLKEKMEHLigacRDKEAKIKELLKKLEQL------------SEEVLAIRGENARLALQLQDSQKNHEE 877
Cdd:PRK03918 619 ---KELKKLEEELDKAFEEL----AETEKRLEELRKELEELekkyseeeyeelREEYLELSRELAGLRAELEELEKRREE 691
|
....*..
gi 526118251 878 IISTYRN 884
Cdd:PRK03918 692 IKKTLEK 698
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
98-144 |
1.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 526118251 98 SALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 144
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
544-877 |
1.25e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 544 LGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR-----------------KLLAS 606
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikkleediLLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 607 QSSGL---RGLWDCLPADLVGERSAQSKAAESLEELR----ACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGT 679
Cdd:pfam01576 146 QNSKLskeRKLLEERISEFTSNLAEEEEKAKSLSKLKnkheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 680 SLKApaspQVAALEQDLGKLEEELRAVQA----TMSGKSQEIGKLKQLLYQATEEVAELrAREAASLRQHEKTRGSLVAQ 755
Cdd:pfam01576 226 ELQA----QIAELRAQLAKKEEELQAALArleeETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 756 AQAWGQELKALLEKYNTAC-------REVGRLREAVAEERRRsgdlaaqaaeQERQASEMRGR-SEQFEKTAELLKEKME 827
Cdd:pfam01576 301 LEALKTELEDTLDTTAAQQelrskreQEVTELKKALEEETRS----------HEAQLQEMRQKhTQALEELTEQLEQAKR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 526118251 828 HLIGACRDK---EAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEE 877
Cdd:pfam01576 371 NKANLEKAKqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
62-91 |
1.44e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|
gi 526118251 62 DGRTPLMIASLGGHAAICSQLLQRGARVNV 91
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1-134 |
1.88e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.92 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 1 MKRIFSCSSTQcvkvLLQHGA-NEDAvdaenrspLHWAASSGC--ASSVLLLCDHEAFLDVLDND---GRTPLMIASLGG 74
Cdd:cd22192 33 IKKLLKCPSCD----LFQRGAlGETA--------LHVAALYDNleAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526118251 75 HAAICSQLLQRGARVN---VTD----KNDKSAL-----IL---ACEkGSAEVAELLLSHGADAGAVDSTGHDALH 134
Cdd:cd22192 101 NLNLVRELIARGADVVsprATGtffrPGPKNLIyygehPLsfaACV-GNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
13-148 |
1.92e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.87 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 13 VKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVL-----------------------DNDGRTPLMI 69
Cdd:PHA02874 51 VELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmiktildcgidvnikDAELKTFLHY 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526118251 70 ASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 148
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
76-144 |
2.05e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 2.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526118251 76 AAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL-HTQDKAL 144
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVkHYNKPIV 217
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
95-121 |
2.52e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 2.52e-03
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
78-141 |
2.74e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.59 E-value: 2.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526118251 78 ICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQD 141
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
576-858 |
2.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 576 LQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRG--LWDCLPADLVGERSAQ-SKAAESLEELRACISTL---VDR 649
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpVEGSPHVETIEEDRERvEELEAELEDLEEEVEEVeerLER 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 650 HREAQQVLARLQ--EENQQLRGSLSPCREPGTSLKapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKlkqllyqA 727
Cdd:PRK02224 501 AEDLVEAEDRIErlEERREDLEELIAERRETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEE-------A 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 728 TEEVAELRAREAA---SLRQHEKTRGSLVAQAQAwGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAaeQERQ 804
Cdd:PRK02224 571 REEVAELNSKLAElkeRIESLERIRTLLAAIADA-EDEIERLREKREALAELNDERRERLAEKRERKRELEAEF--DEAR 647
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526118251 805 ASEMRGRSEQFEKTAELLKEKMEHL----------IGACRDKEAKIKELLKKLEQLSEEVLAIR 858
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELreerddlqaeIGAVENELEELEELRERREALENRVEALE 711
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
539-876 |
3.84e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 539 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKlrkllASQSSGLRGLWDCL 618
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-----HEVATSIREISCQQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 619 PADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQqLRGSLSPCREPGTSLKAPASPQVAALEQDLGK 698
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 699 LEEELRAVQATMSGKSQEIGKLKQLlYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR--- 775
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqr 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 776 ---EVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacrdkEAKIKELLKKLEQLSE 852
Cdd:TIGR00618 533 geqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-------QNITVRLQDLTEKLSE 605
|
330 340
....*....|....*....|....
gi 526118251 853 EVLAIRGENARLALQLQDSQKNHE 876
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQD 629
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
81-146 |
4.16e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.81 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526118251 81 QLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWR 146
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIER 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
688-883 |
4.61e-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: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 688 QVAALEQDLGKLEEELRA---------VQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 758
Cdd:COG3206 183 QLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 759 wgQELKALLEKYNtacrevgRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEA 838
Cdd:COG3206 263 --PVIQQLRAQLA-------ELEAELAELSARYTPNHPDVIALRAQIAALR---AQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 526118251 839 KIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 883
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
620-791 |
5.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 620 ADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALE-QDLGK 698
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-----------QIRGNGgDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 699 LEEELRAVQATMSGKSQEIGKLKQLLYQAT-------EEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYN 771
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180
....*....|....*....|
gi 526118251 772 TACREVGRLReavaeeRRRS 791
Cdd:COG4913 423 ELEAEIASLE------RRKS 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
621-814 |
5.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 621 DLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLrgslspcrepgtslkapasPQVAALEQDLGKLE 700
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL-------------------GKNLDDEDELEQLQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 701 EELRAVQATMSgksqeigklkqllyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWgQELKALLEkyntacrevgRL 780
Cdd:PRK04863 561 EELEARLESLS--------------ESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA----------RL 615
|
170 180 190
....*....|....*....|....*....|....*..
gi 526118251 781 REAVAEE---RRRSGDLAAQAAEQERQASEMRGRSEQ 814
Cdd:PRK04863 616 REQSGEEfedSQDVTEYMQQLLERERELTVERDELAA 652
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
513-869 |
7.70e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 513 KALGGLAKGQLEKEMSVLRLSNSNL--------------------LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA 572
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLekvssltaqlestkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 573 QVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwDCLPADLvgERSAQSKAAESLEELRACISTLVDRH-R 651
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT----------ECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHgR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 652 EAQQVL---ARLQEENQQLRGSLSPCRepgtSLKAPASPQVAALEQDLGKLE-EELRAVQATmSGKSQEIGKLKQLLYQA 727
Cdd:pfam15921 584 TAGAMQvekAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLElEKVKLVNAG-SERLRAVKDIKQERDQL 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118251 728 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASE 807
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526118251 808 MRGRSEQFEKTAELLKEKMEHligacRDKEakiKELLKKLE-QLSEEVLAIRGENARLALQLQ 869
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTN-----ANKE---KHFLKEEKnKLSQELSTVATEKNKMAGELE 793
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
62-91 |
7.96e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.93 E-value: 7.96e-03
10 20 30
....*....|....*....|....*....|
gi 526118251 62 DGRTPLMIASLGGHAAICSQLLQRGARVNV 91
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| |
