|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
146-456 |
1.95e-148 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 427.80 E-value: 1.95e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLM 225
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSM 305
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 306 DNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ- 384
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQk 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940128062 385 -TLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 456
Cdd:pfam00038 241 aSLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-142 |
1.25e-34 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 127.46 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 14 GFSSGSAVAGGVKRVAFSSASMS------GGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128062 88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-453 |
3.53e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPRNLDpfFETYINALRKNLDTLSNDKGRLQSELKL 224
Cdd:TIGR02168 674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 225 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDvdaaymiKVELEAKMESLKDEINfmrvLYEAELSQMQTHVSDTSVVLS 304
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 305 MDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQ--QLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENik 382
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE-- 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 383 kqtLQASVADAE-QRGEL--ALKDAYTKRADLETALQKAKEDLA----RLMRDYQELMNVKLALDVEIATYRKLLEGE 453
Cdd:TIGR02168 899 ---LSEELRELEsKRSELrrELEELREKLAQLELRLEGLEVRIDnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-451 |
2.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 201 INALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINf 280
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 281 mrvLYEAELSQMQTHVSDTSVVLSMDNNRnldldgiIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKST 360
Cdd:COG1196 334 ---ELEEELEELEEELEEAEEELEEAEAE-------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 361 KNEISELNRMIQRIRSEIENIKKQTLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALD 440
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|.
gi 1940128062 441 VEIATYRKLLE 451
Cdd:COG1196 484 EELAEAAARLL 494
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
134-454 |
2.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTT---------TTSPRNLDPFFETYINA 203
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 204 LRKNLDTLSNDKGRLQSE---LKLMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 280 FMRVlyeAELSQMQTHVSDTSVVLSmdnnrNLDLDGIiaevRAQYEEIARKSKAEVESWYQIKVQQLQMSA--------- 350
Cdd:PRK01156 557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksirei 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 351 DQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQA-SVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDY 429
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
330 340
....*....|....*....|....*
gi 1940128062 430 QELMNVKLALDVEIATYRKLLEGEE 454
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMK 729
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
146-456 |
1.95e-148 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 427.80 E-value: 1.95e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLM 225
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSM 305
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 306 DNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ- 384
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQk 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940128062 385 -TLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 456
Cdd:pfam00038 241 aSLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-142 |
1.25e-34 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 127.46 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 14 GFSSGSAVAGGVKRVAFSSASMS------GGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940128062 88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-453 |
3.53e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPRNLDpfFETYINALRKNLDTLSNDKGRLQSELKL 224
Cdd:TIGR02168 674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 225 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDvdaaymiKVELEAKMESLKDEINfmrvLYEAELSQMQTHVSDTSVVLS 304
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 305 MDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQ--QLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENik 382
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE-- 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 383 kqtLQASVADAE-QRGEL--ALKDAYTKRADLETALQKAKEDLA----RLMRDYQELMNVKLALDVEIATYRKLLEGE 453
Cdd:TIGR02168 899 ---LSEELRELEsKRSELrrELEELREKLAQLELRLEGLEVRIDnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-425 |
1.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 144 TAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLqqqttttspRNLDPFFETYINALRKNLDTLSNDKGRLQSELK 223
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------RLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 224 LMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQthvsdtsvvl 303
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE---------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 304 smdnnrnldldgiiaEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQH--GDSLKSTKNEISELNRMIQR-----IRS 376
Cdd:TIGR02168 376 ---------------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEaelkeLQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1940128062 377 EIENIKKQ--TLQASVADAEQRGELALKdaytKRADLETALQKAKEDLARL 425
Cdd:TIGR02168 441 ELEELEEEleELQEELERLEEALEELRE----ELEEAEQALDAAERELAQL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-451 |
2.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 201 INALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINf 280
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 281 mrvLYEAELSQMQTHVSDTSVVLSMDNNRnldldgiIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKST 360
Cdd:COG1196 334 ---ELEEELEELEEELEEAEEELEEAEAE-------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 361 KNEISELNRMIQRIRSEIENIKKQTLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALD 440
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|.
gi 1940128062 441 VEIATYRKLLE 451
Cdd:COG1196 484 EELAEAAARLL 494
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
134-454 |
2.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTT---------TTSPRNLDPFFETYINA 203
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 204 LRKNLDTLSNDKGRLQSE---LKLMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 280 FMRVlyeAELSQMQTHVSDTSVVLSmdnnrNLDLDGIiaevRAQYEEIARKSKAEVESWYQIKVQQLQMSA--------- 350
Cdd:PRK01156 557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksirei 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 351 DQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQA-SVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDY 429
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
330 340
....*....|....*....|....*
gi 1940128062 430 QELMNVKLALDVEIATYRKLLEGEE 454
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMK 729
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
162-412 |
7.65e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 162 DKVRFLEQQNKVLETKWNLLQQQTTTtsprnldpfFETYINALRKnldtLSNDKgrlQSELKLMQDSVEDFKTKYEEEIN 241
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRK----KNGEN---IARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 242 KRTAAENDFVVLKKDVDAAY----MIKVELEAKMESLKDEINFMRvlyeaELSQMQTHVSDTSvvlsmdnnrnlDLDGII 317
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 318 AEVRAQYEEIARKSKAEveswyQIKVQQLQMSADQHGD---SLKSTKNEISELNRMIQRIRSEIENIKKQTLQASVADAE 394
Cdd:PHA02562 302 TKIKDKLKELQHSLEKL-----DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
|
250 260
....*....|....*....|...
gi 1940128062 395 QRGELA-----LKDAYTKRADLE 412
Cdd:PHA02562 377 NAEELAklqdeLDKIVKTKSELV 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-438 |
3.85e-05 |
|
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: 46.59 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 119 QEVTINQSLLTPLQVEIDPEIQKIRTAEREqIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQttttsprnldpffe 198
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------------- 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 199 tyINALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaymIKVELEAKMESLKDEI 278
Cdd:TIGR02168 791 --IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 279 NFMRVLYEAELSQMQTHVsdtsvvlsmdnNRNLDLDGIIAEVRAQYEEIARKSKaEVESwyqiKVQQLQmsadqhgDSLK 358
Cdd:TIGR02168 862 EELEELIEELESELEALL-----------NERASLEEALALLRSELEELSEELR-ELES----KRSELR-------RELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 359 STKNEISELNRMIQRIRSEIENIKKQtlqasvadAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLA 438
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQER--------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-409 |
1.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 198 ETYINALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKMESLKDe 277
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 278 inFMRVLYEAELSqmqthVSDTSVVLSMDN-----NRNLDLD-------GIIAEVRAQYEEIARKsKAEVESwyqiKVQQ 345
Cdd:COG3883 91 --RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSkiadadaDLLEELKADKAELEAK-KAELEA----KLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1940128062 346 LQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQASVADAEQRGELALKDAYTKRA 409
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-451 |
1.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 266 ELEAKMESLKDEINFMrvlyEAELSQMQTHVSDTSVVLSMDNNRnLDLDGI---IAEVRAQYEEIaRKSKAEVESWYQiK 342
Cdd:COG4913 621 ELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERL-DASSDDLAALEE-Q 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 343 VQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQAS-------VADAEQRGELALKDAYTKR------- 408
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlelRALLEERFAAALGDAVERElrenlee 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1940128062 409 --ADLETALQKAKEDLARLMRDYQEL-MNVKLALDVEIAT---YRKLLE 451
Cdd:COG4913 774 riDALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-432 |
3.73e-04 |
|
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: 43.52 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 204 LRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEI-NFMR 282
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIeNVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 283 VL--YEAELSQMQTHVSdtSVVLSMDNNRNLDLDGIIAEVRAQYEEIarksKAEVESWYQI------KVQQLQMSADQHG 354
Cdd:TIGR02169 759 ELkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKL----EEEVSRIEARlreieqKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 355 DSLKSTKNEISELNRMIQRIRSEIENIKKQtlQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQEL 432
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGK--KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
264-451 |
7.14e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 264 KVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVE-----SW 338
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 339 YQIKVQQLQMSADQH----GDSLKSTKNEISELNRMIQR-------IRSEIENIKKQ--TLQASVADAEQRGE------L 399
Cdd:pfam05557 84 YLEALNKKLNEKESQladaREVISCLKNELSELRRQIQRaelelqsTNSELEELQERldLLKAKASEAEQLRQnlekqqS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 400 ALKDAYTKRADLETALQKAKEDLARLMRDYQELMNV------KLALDVEIATYRKLLE 451
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIpelekeLERLREHNKHLNENIE 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
267-451 |
7.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 267 LEAKMESLKDEINFMR---VLYEAELSQMQTHVSD---TSVVLSMDNNRNLDLDgIIAEVRAQYEEiARKSKAEVESWYQ 340
Cdd:COG3206 166 LELRREEARKALEFLEeqlPELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQ-QLSELESQLAE-ARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 341 IKVQQLQMSADQHGDSLKST-----KNEISELNRM--------------IQRIRSEIENIKKQtLQASVADAEQRGELAL 401
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviqqlRAQLAELEAElaelsarytpnhpdVIALRAQIAALRAQ-LQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1940128062 402 KDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLE 451
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-454 |
9.50e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 310 NLD-LDGIIAEVRAQYE------EIARKSKA------EVESWYQI-KVQQLQMSADQHGDSLKSTKNEISELNRMIQRIR 375
Cdd:COG1196 187 NLErLEDILGELERQLEplerqaEKAERYRElkeelkELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1940128062 376 SEIENIKKQTLQASVADAEQRGELALKDAytKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEE 454
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
286-424 |
2.02e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 286 EAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKSTKN 362
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 363 EISELNRMIQRIRSEIENIKKQ--TLQASVADAEQRGelalKDAYTKRAD----LETALQKAKEDLAR 424
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQlaALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
131-460 |
2.47e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 131 LQVEIDPEIQKIRTAEREQIKTLNNKFASFIDKVRF---LEQQNKV----LETKWNLLQQQTTTTSPRN--LDPFFETYI 201
Cdd:PLN03229 434 LEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKeidLEYTEAViamgLQERLENLREEFSKANSQDqlMHPVLMEKI 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 202 NALRKNLDTLSNDKGRLQSeLKLMQDSVEDFkTKYEEEINKRTAAENdfvvLKKDVD---AAYMIKVELEAKMESLKDEI 278
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLS-LKYKLDMLNEF-SRAKALSEKKSKAEK----LKAEINkkfKEVMDRPEIKEKMEALKAEV 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 279 NfmrvlyEAELSQMQTHVSDT-SVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVEswyQIKVQQLQmsadqhgDSL 357
Cdd:PLN03229 588 A------SSGASSGDELDDDLkEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE---QTPPPNLQ-------EKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 358 KSTKNEIselNRMIQR-IRSEIENIKKQTLQASVADAEQRGELALKDAytkradLETALQKAKEDLARLMrDYQELMNVK 436
Cdd:PLN03229 652 ESLNEEI---NKKIERvIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIAEAL-NSSELKEKF 721
|
330 340
....*....|....*....|....
gi 1940128062 437 LALDVEIATYRKLLEGEECRMSGE 460
Cdd:PLN03229 722 EELEAELAAARETAAESNGSLKND 745
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
122-383 |
4.21e-03 |
|
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: 40.03 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 122 TINQSLLTPLQVEIDPEIQKIRTAEREQIK----TLNNKfasfidkvrfleqQNKVLETKWNLLQQQTTTTSpRNLDPFF 197
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsNIENK-------------KNELLDIIVEIKKHIHGEIN-KDLNKIL 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 198 ETYINAlRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYMIKVELEAKMESLKDE 277
Cdd:TIGR01612 758 EDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 278 INFMRVLYEAELSQMQTHVsdtsvvlSMDNNRNLDLDgiiaEVRAQYEEIARKSKAEVESwyqikvQQLQMSADQHGDSl 357
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFI-------NFENNCKEKID----SEHEQFAELTNKIKAEISD------DKLNDYEKKFNDS- 895
|
250 260
....*....|....*....|....*.
gi 1940128062 358 kstKNEISELNRMIQRIRSEIENIKK 383
Cdd:TIGR01612 896 ---KSLINEINKSIEEEYQNINTLKK 918
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
199-444 |
7.06e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 199 TYINAlRKNLDTLSNDKgrlQSELKLMQDSVEDFKTKYEEEINKRTAAENdfvVLKKDVDA-----------------AY 261
Cdd:pfam12128 647 ALKNA-RLDLRRLFDEK---QSEKDKKNKALAERKDSANERLNSLEAQLK---QLDKKHQAwleeqkeqkreartekqAY 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 262 MIKVE--LEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKsKAEVESWY 339
Cdd:pfam12128 720 WQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYF 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 340 QIkvqqLQMSADQHGDSLKSTKNEiselnrmiqrIRSEIENIKKQtLQASVADAEQRgelaLKDAYTKRADLETALQKAK 419
Cdd:pfam12128 799 DW----YQETWLQRRPRLATQLSN----------IERAISELQQQ-LARLIADTKLR----RAKLEMERKASEKQQVRLS 859
|
250 260
....*....|....*....|....*.
gi 1940128062 420 EDLaRLMRDYQELMN-VKLALDVEIA 444
Cdd:pfam12128 860 ENL-RGLRCEMSKLAtLKEDANSEQA 884
|
|
| |
