|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
161-474 |
1.02e-154 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 445.90 E-value: 1.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 161 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIkQNLDPLFEQYINNLRRQLDGVLGERGRLDSELRN 240
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEP-SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 241 MQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLS 320
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 321 MDNNRSLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQ 400
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20911031 401 CANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECR 474
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
127-158 |
2.69e-17 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 79.31 E-value: 2.69e-17
10 20 30
....*....|....*....|....*....|..
gi 20911031 127 PVCPPGGIQEVTVNQNLLTPLNLQIDPTIQRV 158
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-450 |
5.10e-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: 59.30 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 158 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIKQNLDplFEQYINNLRRQLDGVLGERGRLDSE 237
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 238 LRNMQDLVEDYKNK---YEDEINKRTT----AENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDA---ELSQ 307
Cdd:TIGR02168 749 IAQLSKELTELEAEieeLEERLEEAEEelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 308 MQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDI---ANRSRTEAESWYQtKYEELQQTAGRHGDDLRNTKHEISEMN 384
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLN-ERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20911031 385 RMIQRLRSEIDNVKKQCANLQNAIAEAEQR-----------GELALKDARNKLTELEEALQKAKQDMARLLREYQEL 450
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-476 |
3.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 150 QIDPTIQRVRtEEREQIKTLNNKFASFIDKVRflEQQNKVLDTKWALLQEQGTKTIKQNldplFEQYI-----NNLRRQL 224
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQALLKEKRE----YEGYEllkekEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 225 DGVLGERGRLDSELRNMQDLVEDYKNKYE------DEINKRTTA--ENEFVMLKKDVDAAYMNKVELEARVDALMDEINF 296
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 297 MK---MFFDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIanRSRTEAESwyqTKYEELQQTAGRHGDDL 373
Cdd:TIGR02169 320 AEerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD---KEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 374 RNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRG---ELALKDARNKLTELEEALQKAKQDMARLLREYQEL 450
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340
....*....|....*....|....*.
gi 20911031 451 MNTKLALDVEIATYRKLLEGEECRLS 476
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
214-474 |
8.09e-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: 52.43 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 214 EQYINNLRRQLDG---VLGERGRLDSELrnmqdLVEdyKNKYEDEINKRTTAENEFVMLKKDVDAAYMnkvELEARVDal 290
Cdd:pfam15921 561 DKVIEILRQQIENmtqLVGQHGRTAGAM-----QVE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVS-- 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 291 mdeinfmkmffDAELSQMQThVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRTEA--ESWYQTKYEELQQTAGR 368
Cdd:pfam15921 629 -----------DLELEKVKL-VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 369 HGDDLRNTKHEISE---------------------MNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELaLKDARNKLT 427
Cdd:pfam15921 697 LKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLS 775
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 20911031 428 ELEEALQKAKQDMA---RLLREYQELMNTKLAlDVEIATYRKLLEGEECR 474
Cdd:pfam15921 776 QELSTVATEKNKMAgelEVLRSQERRLKEKVA-NMEVALDKASLQFAECQ 824
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-466 |
9.90e-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: 51.98 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 329 LDSIIAEVKAQYEDIANRSRTEAESWYQTKYE--ELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQN 406
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20911031 407 AIAEAEQRGELA---LKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 466
Cdd:TIGR02168 324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-476 |
1.36e-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: 51.61 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 220 LRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEInfmkm 299
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 300 ffdAELSQMQTHVsdtsvvlsmdNNRSLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHE 379
Cdd:TIGR02169 754 ---ENVKSELKEL----------EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 380 ISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGEL----------ALKDARNKLTELEEALQKAKQDMARLLREYQE 449
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeeleeELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260
....*....|....*....|....*..
gi 20911031 450 LMNTKLALDVEIATYRKLLEGEECRLS 476
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
302-450 |
2.99e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 302 DAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDI-ANRSRteAESWYQTKYEELQQTAGRHGD---DLRNTK 377
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSR--LQALLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20911031 378 HEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGelalKDARNKLTELEEALQKAkqdmarLLREYQEL 450
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVA------LAQRVQEL 192
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
282-484 |
3.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 282 ELEARVDALMDEINFMKmffdAELSQMQTHVSDtsvvlsmdnnrsldLDSIIAEVKAQYEDIANRsrteaeswyQTKYEE 361
Cdd:COG1579 28 ELPAELAELEDELAALE----ARLEAAKTELED--------------LEKEIKRLELEIEEVEAR---------IKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 362 lQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMA 441
Cdd:COG1579 81 -QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 20911031 442 RLLREYQELMNTklaLDVEI-ATYRKLLEgeecRLSGEGVGPVN 484
Cdd:COG1579 160 ELEAEREELAAK---IPPELlALYERIRK----RKNGLAVVPVE 196
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
151-472 |
3.81e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 151 IDPT-IQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQ------GTKTIKQNLDPLFEQYINNLRR- 222
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 223 --QLDGVLGERGRLDSE---LRNMQDLVEDYK-NKYEDEINKRTTAENEfvmLKKDVDAAYMNKvELEARVDALMDEINF 296
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 297 MKMffdAELSQMQTHVSDTSVVLSmdnnrSLDLDSIIA---EVKAQYEDIANRSRtEAESWYQTKYEELQQTAGRHGDD- 372
Cdd:PRK01156 558 LKL---EDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEa 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 373 --LRNTKHEISEMNRMIQRLRSEIDNVKKQCANLqNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQEL 450
Cdd:PRK01156 629 nnLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL 707
|
330 340
....*....|....*....|..
gi 20911031 451 MNTKLALDVEIATYRKLLEGEE 472
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
134-466 |
6.04e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 134 IQEVTVNQNLLTPLNL-QIDPTIQRVRTEEREQIKTlnnkfasFIDKVRFLEQQNKVLDTKwalLQEQGTKTIKqnldpl 212
Cdd:pfam15921 304 IQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRM-------YEDKIEELEKQLVLANSE---LTEARTERDQ------ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 213 FEQYINNLRRQLDGVLGERGRLDSELRnmqdlVEDYKNK--YEDEINKRTTAENefvmLKKDVDAAYMNKVELEARVDAL 290
Cdd:pfam15921 368 FSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKrlWDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 291 MDEINfmkmffdaelSQMQTHVSDTSvvlsmDNNRSLD-LDSIIAEVKAQYEDIanRSRTEAESWYQTKYEELQQTAGRH 369
Cdd:pfam15921 439 KSECQ----------GQMERQMAAIQ-----GKNESLEkVSSLTAQLESTKEML--RKVVEELTAKKMTLESSERTVSDL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 370 GDDLRNTKHEISEMNRMIQRLRSEID-------NVKKQCANLQNAIAEAEqrgelALKDARNKLTELEEALQKAKQDMAR 442
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDlklqelqHLKNEGDHLRNVQTECE-----ALKLQMAEKDKVIEILRQQIENMTQ 576
|
330 340
....*....|....*....|....
gi 20911031 443 LLREYQElmnTKLALDVEIATYRK 466
Cdd:pfam15921 577 LVGQHGR---TAGAMQVEKAQLEK 597
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-448 |
6.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 372 DLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQR-----GELA-----LKDARNKLTELEEALQKAKQDMA 441
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleQELAaleaeLAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 20911031 442 RLLREYQ 448
Cdd:COG4942 108 ELLRALY 114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-469 |
1.38e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 154 TIQRVRTEEREQIKTLNNKF-------ASFIDKVRFLEQQNKVLDTKWALLQEQgTKTIKQNLDPLfEQYINNLRRQLDG 226
Cdd:TIGR04523 58 NLDKNLNKDEEKINNSNNKIkileqqiKDLNDKLKKNKDKINKLNSDLSKINSE-IKNDKEQKNKL-EVELNKLEKQKKE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 227 VLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVD--AAYMNKVELEARVDAL----MDEINFMKMF 300
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELllsnLKKKIQKNKS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 301 FDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANrSRTEAESWYQTKYEELQQTagrhgddlrNTKheI 380
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD-EQNKIKKQLSEKQKELEQN---------NKK--I 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 381 SEMNRMIQRLRSEIDNVKKQ-CANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDV 459
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
330
....*....|
gi 20911031 460 EIATYRKLLE 469
Cdd:TIGR04523 364 ELEEKQNEIE 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
324-476 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 324 NRSLDLDSIIAEVKAQYEDIANRsRTEAEswyqTKYEELQQT-AGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQC- 401
Cdd:COG4913 295 AELEELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLa 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 402 -------------ANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLL 468
Cdd:COG4913 370 alglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
....*...
gi 20911031 469 EgEECRLS 476
Cdd:COG4913 450 A-EALGLD 456
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
178-446 |
2.37e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 178 DKVRFLEQQNKVLDTKWALLQEQgtktIKqnldpLFEQYINNLRRQLDGVLgergrldSELRNMQD-LVEDYKNkYEDEI 256
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----IK-----TYNKNIEEQRKKNGENI-------ARKQNKYDeLVEEAKT-IKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 257 NKRTTAENEFVMLKKDVDAAyMNKVELE-ARVDALMDEIN-FMKMFFDAEL--SQMQThvsdtsvvLSMDNNRSLDLDSI 332
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAA-LNKLNTAaAKIKSKIEQFQkVIKMYEKGGVcpTCTQQ--------ISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 333 IAEVKAQYEDIanrsrteaeswyQTKYEELQQtagrhgddlrnTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAE 412
Cdd:PHA02562 308 LKELQHSLEKL------------DTAIDELEE-----------IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK 364
|
250 260 270
....*....|....*....|....*....|....*..
gi 20911031 413 ---QRGELALKDARNKLTELEEALQKAKQDMARLLRE 446
Cdd:PHA02562 365 aaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-472 |
2.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 333 IAEVKAQYEDIANRSRTEAESW--YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAE 410
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20911031 411 AEQRGELA---LKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 472
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
214-489 |
2.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 214 EQYIN-NLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDeinkrTTAENEFVMLKKDVDAAYMNKVELEARVDALMD 292
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 293 EINFMKmffdAELSQMQTHVSDTSVVLSMDNNrsldlDSIIAEVKAQYEDIanrsrteaeswyQTKYEELQQTAGrhgdd 372
Cdd:COG3206 234 ELAEAE----ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL------------EAELAELSARYT----- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 373 lrntkheisEMNRMIQRLRSEIDNVKKQcanLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARL---LREYQE 449
Cdd:COG3206 288 ---------PNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRR 355
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 20911031 450 LMNtklalDVEIA--TYRKLLEG-EECRLSgEGVGPVNISVVT 489
Cdd:COG3206 356 LER-----EVEVAreLYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
324-472 |
3.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 324 NRSLDLDSIIAEVKAQYEDIANRSRT-----EAESWYQtKYEELQQTAGRHGDDLRNTKHEISEmnrmIQRLRSEIDNVK 398
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEE----LRELEEELEELE 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20911031 399 KQCANLQNAIAEAEQRGELAlkdARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 472
Cdd:COG4717 170 AELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-449 |
3.57e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 333 IAEVKAQYEDIANRsRTEAESWYQTKYEELQQTAGRHgdDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAE 412
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 20911031 413 QRGELA-----LKDARNKLTELEE---ALQKAKQDMARLLREYQE 449
Cdd:COG4717 467 EDGELAellqeLEELKAELRELAEewaALKLALELLEEAREEYRE 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
160-435 |
3.78e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 160 TEEREQIKTLNNKFASFIDKVRFLE-------------QQNKVLDTkWALLQEQGTKTIKQNLDPLFEQYiNNLRRQLDG 226
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMEtatvelhlsnienKKNELLDI-IVEIKKHIHGEINKDLNKILEDF-KNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 227 VLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEfvmLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDAELS 306
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLN 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 307 QMQTHVsdtsvvlSMDNNRSLDLDSiiaeVKAQYEDIANRSRTEAESWYQTKYEelqqtagrhgDDLRNTKHEISEMNRM 386
Cdd:TIGR01612 847 KVDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAEISDDKLNDYE----------KKFNDSKSLINEINKS 905
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 20911031 387 IQRLRSEIDNVKKQCANLQNAIAEAEqrgelALKDARNKLTELEEALQK 435
Cdd:TIGR01612 906 IEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
217-422 |
3.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 217 INNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAymnKVELEARVDALMDEINF 296
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 297 MK----------MFFDAE-LSQMQTHVSDTSVVLSMDNNrsldldsIIAEVKAQYEDIANrsrteAESWYQTKYEELQQT 365
Cdd:COG3883 95 LYrsggsvsyldVLLGSEsFSDFLDRLSALSKIADADAD-------LLEELKADKAELEA-----KKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 20911031 366 AGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALKDA 422
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-450 |
4.37e-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: 42.83 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 371 DDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRgelaLKDARNKLTELEEALQKAKQDMARLLREYQEL 450
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-454 |
4.45e-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: 43.17 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 223 QLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMffd 302
Cdd:pfam05483 409 ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL--- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 303 aelsqMQTHVSDTSVVLSMDNNR-SLDLDSIIAEVKAQYEDIANRSRTE------------AESWYQTKYEELQQTAGRH 369
Cdd:pfam05483 486 -----KNIELTAHCDKLLLENKElTQEASDMTLELKKHQEDIINCKKQEermlkqienleeKEMNLRDELESVREEFIQK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 370 GDDL-----------RNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGElALKDARN-----------KLT 427
Cdd:pfam05483 561 GDEVkckldkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK-ALKKKGSaenkqlnayeiKVN 639
|
250 260
....*....|....*....|....*..
gi 20911031 428 ELEEALQKAKQDMARLLREYQELMNTK 454
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
261-466 |
5.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 261 TAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKmffdAELSQMQTHVSDTSVvlSMDNNRSlDLDSIIAEVKAQY 340
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 341 EDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNT---KHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQrgel 417
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 20911031 418 ALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 466
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
332-449 |
5.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 332 IIAEVKAQYEDIanrsRTEAESWYQTKYEELQQTAGR-------HGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANL 404
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKLEKRllqkeenLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 20911031 405 QNAIAEAEQRGE----LALKDARNKLteLEEALQKAKQDMARLLREYQE 449
Cdd:PRK12704 134 EELIEEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-450 |
5.84e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 329 LDSIIAEVKAQYEDIANRSRTEAESW--YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQN 406
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 20911031 407 AIAEAEQRGELA---LKDARNKLTELEEALQKAKQDMARLLREYQEL 450
Cdd:COG1196 324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
156-451 |
6.01e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 156 QRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIKQNLDPlfEQYINNLRRQLDgVLGERGRL- 234
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH--EARIRELEEDIK-TLTQRVLEr 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 235 DSELRNMQDLVEDYKNKYEDE-------INKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFD----- 302
Cdd:pfam07888 149 ETELERMKERAKKAGAQRKEEeaerkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrk 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 303 -AELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQyedianRSRTEAE---------------------------SW 354
Cdd:pfam07888 229 eAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAElhqarlqaaqltlqladaslalregraRW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 355 YQTKyEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEidNVKkqcanLQNAIAEAEQRGELALKDARNKLTELEEALQ 434
Cdd:pfam07888 303 AQER-ETLQQSAEADKDRIEKLSAELQRLEERLQEERME--REK-----LEVELGREKDCNRVQLSESRRELQELKASLR 374
|
330
....*....|....*..
gi 20911031 435 KAKQDMARLLREYQELM 451
Cdd:pfam07888 375 VAQKEKEQLQAEKQELL 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-469 |
6.15e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 159 RTEE-REQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgtktiKQNLDPLFEQyINNLRRQLDGVLGERGRLDSE 237
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 238 LRNMQDLVEDYKNKYED------EINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDaELSQMQTH 311
Cdd:PRK03918 261 IRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 312 VSDTSVVLSMDNNR------SLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNR 385
Cdd:PRK03918 340 LEELKKKLKELEKRleeleeRHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 386 MIQRLRSEIDNVKK---QCANLQNAIAEaEQRGELaLKDARNKLTELEEALQKAKQDMARLLREYQELmNTKLALDVEIA 462
Cdd:PRK03918 420 EIKELKKAIEELKKakgKCPVCGRELTE-EHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELI 496
|
....*..
gi 20911031 463 TYRKLLE 469
Cdd:PRK03918 497 KLKELAE 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-471 |
6.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 328 DLDSIIAEVKAQYEDIANRSRT----EAESWYQTKYEELQQTAGRHGD---DLRNTKHEISEMNRMIQRLRSEIDNVKKQ 400
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20911031 401 CANLQNAIAEAEQRgelaLKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGE 471
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
329-466 |
7.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 329 LDSIIAEVKAQYEDIANRSRTEAEswYQTKYEELQQTAGRHGDDLRN--TKHEISEMNRMIQRLRSEIDNVKKQCANLQN 406
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 407 AIAEAEQRGELALKDARnkLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 466
Cdd:COG4717 454 ELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-451 |
1.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 181 RFLEQQNKVLDTKWALLQEQGTKTIKQNLDPLfEQYINNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEdEInkrT 260
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLNGL-ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-EL---E 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 261 TAENEFVMLKKDVDAAYMNKVEL-------EARVDALMDEINfmKMFFDAELSQMqthvSDTSVVLSMDnnrslDLDSII 333
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeevrdlRERLEELEEERD--DLLAEAGLDDA----DAEAVEARRE-----ELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 334 AEVKAQYEDI---ANRSRTEAESW------YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANL 404
Cdd:PRK02224 324 EELRDRLEECrvaAQAHNEEAESLredaddLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 20911031 405 QNAIAEAEQRGELALK---DARNKLTELEEALQKAKQDmarlLREYQELM 451
Cdd:PRK02224 404 PVDLGNAEDFLEELREerdELREREAELEATLRTARER----VEEAEALL 449
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-454 |
1.45e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 144 LTPLNLQIDPTIQRVRTEERE------QIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgtKTIKQNLDPLFEQYI 217
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVElnklekQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ--KEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 218 NNLRRQLDGVLGERGRLDSELRNMQDLVEDYKnKYEDEINKrttAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFM 297
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 298 KmffdAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRsrtEAESWYQTKYEELQQTAgrhgDDLRNTK 377
Cdd:TIGR04523 259 K----DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWNKELKSELKNQE----KKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 378 HEISEMNRMIQRLRSEIDNVKKQCANL-------QNAIAEAEQRGELALKDARNKLTELEEaLQKAKQDMARLLREYQEL 450
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSesensekQRELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKL 406
|
....
gi 20911031 451 MNTK 454
Cdd:TIGR04523 407 NQQK 410
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
147-451 |
1.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 147 LNLQIDPTIQRVRTEEReQIKTLNNKfasfidKVRFLEQQNKVLDTKWALLQEqgtktikqnldplfeqyINNLRRQLDG 226
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEK-NILLLNQA------RLQALEDLEKILTEKEALQGK-----------------INILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 227 VlGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVM-LKKDVDAAYMNKVELEarvdalmDEINFMKmffdAEL 305
Cdd:PLN02939 182 T-DARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHsLSKELDVLKEENMLLK-------DDIQFLK----AEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 306 SqmqtHVSDT-SVVLSMDNNRSLdLDSIIAEVKAQY----EDIANRSRTEAESWYQtKYEELQqtagrhgDDLRNTKHEI 380
Cdd:PLN02939 250 I----EVAETeERVFKLEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWWE-KVENLQ-------DLLDRATNQV 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20911031 381 SEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALkdARNKLTELEEALQKAKQDMARLLREYQELM 451
Cdd:PLN02939 317 EKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL--LQQKLKLLEERLQASDHEIHSYIQLYQESI 385
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
218-443 |
1.98e-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: 41.31 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 218 NNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALmdeinfm 297
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 298 kmffDAELSQMQTHVSDTSVVLsmDNNRSL---------DLDSIIAEVK---AQYEDiaNRSRTEAESwyqTKYEELQQT 365
Cdd:pfam01576 572 ----EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 366 AGRHGDDLRNTKHEISEMNRMIQ----RLRSEIDNVKKQCANLQNAIAEAEQrgelALKDARNKLTELEEALQKAKQDMA 441
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKL 716
|
..
gi 20911031 442 RL 443
Cdd:pfam01576 717 RL 718
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
204-436 |
4.09e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 204 TIKQNLDPLFEQ-------YINNLRRQLDG-VLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAE-NEFVMLKKDVD 274
Cdd:PRK05771 13 TLKSYKDEVLEAlhelgvvHIEDLKEELSNeRLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 275 AAYmNKVE------------LEARVDALMDEINFMKMF--FDAELSQMQT--HVSDTSVVLSMDNNRSLDLDSIIAEVKA 338
Cdd:PRK05771 93 EEL-EKIEkeikeleeeiseLENEIKELEQEIERLEPWgnFDLDLSLLLGfkYVSVFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 339 QYED-------IANRSRTEAESWYQTK---YEELQ-QTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNA 407
Cdd:PRK05771 172 ISTDkgyvyvvVVVLKELSDEVEEELKklgFERLElEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 20911031 408 IAEA----EQRGELALKDAR-------------NKLTELEEALQKA 436
Cdd:PRK05771 252 LYEYleieLERAEALSKFLKtdktfaiegwvpeDRVKKLKELIDKA 297
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
214-470 |
4.66e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 39.92 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 214 EQYINNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEIN-KRTTAENEFVmlkKDVDAAYMNKVELEARvDALMD 292
Cdd:PLN03188 918 EDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLLKEKYENHPEvLRTKIELKRV---QDELEHYRNFYDMGER-EVLLE 993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 293 EINFMKM----FFDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSR---TEAESWYQTKYEELqqt 365
Cdd:PLN03188 994 EIQDLRSqlqyYIDSSLPSARKRNSLLKLTYSCEPSQAPPLNTIPESTDESPEKKLEQERlrwTEAESKWISLAEEL--- 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 366 agrhgddlrntKHEISEMNRMIQRLRSEIDnVKKQCANlqnaiaeaeqrgelalkdarnkltELEEALQKAKQDMARLLR 445
Cdd:PLN03188 1071 -----------RTELDASRALAEKQKHELD-TEKRCAE------------------------ELKEAMQMAMEGHARMLE 1114
|
250 260
....*....|....*....|....*
gi 20911031 446 EYQELMNTKLALdveIATYRKLLEG 470
Cdd:PLN03188 1115 QYADLEEKHIQL---LARHRRIQEG 1136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-476 |
4.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 346 RSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQ---RGELALKDA 422
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRREL 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 20911031 423 RNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLS 476
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-476 |
6.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20911031 357 TKYEELQQT---AGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELalKDARNKLTELEEAL 433
Cdd:COG4717 71 KELKELEEElkeAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERL 148
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 20911031 434 QKAKQDmarlLREYQELMNTKLALDVEIATYRKLLEGEECRLS 476
Cdd:COG4717 149 EELEER----LEELRELEEELEELEAELAELQEELEELLEQLS 187
|
|
| |
