|
Name |
Accession |
Description |
Interval |
E-value |
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
39-712 |
0e+00 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 546.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 39 GSSAGKIVAASLLTVGGGLGGTILYAKWDPKFRSSIEKSVPYSDQLFDMVLGAPPSPpvpiQKKPETVKPLQISSLSEAT 118
Cdd:pfam09731 1 KSGFGKFFVALVLIVGVGYGGVVLYAYKDDNFRDFFEEYIPYGEEVVLYALGEDPPL----APKPKTFRPLQPSVVSAVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 119 KDSKQPKAKAKKSDPAPPPSVEEAPApapalqsleaeecckecTEPEPAVKERPAEEvtarlAQQDKAELDALAALTAGL 198
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVA-----------------EEEKEATKDAAEAK-----AQLPKSEQEKEKALEEVL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 199 EETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERAravddagealfkakgelEKLRS 278
Cdd:pfam09731 135 KEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALA-----------------EKLKE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 279 VIDKAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSELVNEAKAQFQQELANITPEIQANWKGL 358
Cdd:pfam09731 198 VINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKED 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 359 SgKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLEdQKAQERAVISALEHSRE----DMRLEQEKKV 434
Cdd:pfam09731 278 N-LLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEE-LDKLAEELSARLEEVRAadeaQLRLEFERER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 435 QEVREVMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEILNSKMMEQEthyrrltqeqlDTFTLDMNAAYARLKG 514
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEER-----------AGRLLKLNELLANLKG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 515 IEEAIDSHVIAEEEARKAHQLWLSVEALNYTLKSAGADSPTEPLEGAVRAIKESCAENEFAQALAIAIPEESLNRGIYSE 594
Cdd:pfam09731 425 LEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASDDEVVKAALASLPEEAYQRGVYTE 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 595 ASLRARFYDIRRLARRVALIDETRNSLYQYFLSYLQSVLLFERDQeappAKLAPEDLDTFKLLAYATYSIERGDLELAAK 674
Cdd:pfam09731 505 AALRERFRRVAKEVRKVSLIDPEGAGLLSHALSYLLSKLMFKPKQ----GEADPAGDDVESILARAEYYLEEGDLDSAAR 580
|
650 660 670
....*....|....*....|....*....|....*...
gi 528499599 675 FVNQLRGESQRVAQDWLKEARLTLETKQVISLLSAYAN 712
Cdd:pfam09731 581 EMNSLKGWSKKLASDWLKEARRRLEVQQALELLQAEAA 618
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-535 |
1.37e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 246 QALNEALNERARAVDDAGEALFKAKGELEKLRSVIDKAKQsKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKI 325
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 326 VSQYSELVNEAKAQFQQELANITPEIQAnwkglsgklSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKL 405
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEE---------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 406 EDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAhtdhlRDVLKVQEQELREEAQEILNSKMME 485
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-----EALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 528499599 486 QETHYRRLTQEQLDTFTLDMNAAYARLKGIEEAIDSHVIAEEEARKAHQL 535
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
100-487 |
9.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 100 QKKPETVKPLQISSLSEATKDSKQPKAKAKKSDPApppsvEEAPAPAPalQSLEAEECCKECTEPEPAVK-ERPAEEVTA 178
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAE--EAKKADEAKKKAEEAKKADEaKKKAEEAKK 1497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 179 RLAQQDKAELDALAA--LTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERA 256
Cdd:PTZ00121 1498 KADEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 257 RAVDDAGEALFKAKGELEKLRSVIDKAKQSKIDSARPqilAAEENLHSmivdldkvvTKVQTAQSEAKIVSQYSELVNEA 336
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK---AEEAKIKA---------EELKKAEEEKKKVEQLKKKEAEE 1645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 337 KAQFQQ----ELANITPEIQANWKGLSGKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLED-QKAQ 411
Cdd:PTZ00121 1646 KKKAEElkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAE 1725
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528499599 412 ERAVISALEHSREDMrlEQEKKVQEVRevMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEILNSKMMEQE 487
Cdd:PTZ00121 1726 EENKIKAEEAKKEAE--EDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
169-366 |
1.03e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.06 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 169 KERpAEEVTARLAQQDKAELDALAALTAGLEET----LGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKS 244
Cdd:NF012221 1564 KER-AEADRQRLEQEKQQQLAAISGSQSQLESTdqnaLETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGES 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 245 TQALNEALNER-----ARAVDDAGEalfKAKGELEKLRSVIdKAKQSKIDSARPQ----ILAAEENLHSMIVDLDKVVTK 315
Cdd:NF012221 1643 GDQWRNPFAGGlldrvQEQLDDAKK---ISGKQLADAKQRH-VDNQQKVKDAVAKseagVAQGEQNQANAEQDIDDAKAD 1718
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528499599 316 VQTAQSEA--------KIVSQYSELVNEAKAQFQQELA---NITPEIQANWKGLsgKLSADD 366
Cdd:NF012221 1719 AEKRKDDAlakqneaqQAESDANAAANDAQSRGEQDASaaeNKANQAQADAKGA--KQDESD 1778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-446 |
1.07e-03 |
|
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: 42.35 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 181 AQQDKAEldALAALTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERARAVD 260
Cdd:TIGR02168 207 RQAEKAE--RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 261 DAGEALFKAKGELEKLRSVIDKAKQSKIDSARPQILAAE--ENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSELVNEAKA 338
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 339 QFQQELANITPEIQANWKGLSGKLSA-------------------DDLNSLIAHAHRRIDQLNRELAEQRVREqIHIEVA 399
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQlelqiaslnneierlearlERLEDRRERLQQEIEELLKKLEEAELKE-LQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528499599 400 LEQQKLEDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMR 446
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
383-487 |
6.19e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 383 RELAEQRVREQIhieVALEQQKLEDQKAQeravisaLEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAhtdhLRD 462
Cdd:cd16269 198 KEIEAERAKAEA---AEQERKLLEEQQRE-------LEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA----LES 263
|
90 100
....*....|....*....|....*
gi 528499599 463 VLKVQEQELREEAQEIlnSKMMEQE 487
Cdd:cd16269 264 KLKEQEALLEEGFKEQ--AELLQEE 286
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
39-712 |
0e+00 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 546.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 39 GSSAGKIVAASLLTVGGGLGGTILYAKWDPKFRSSIEKSVPYSDQLFDMVLGAPPSPpvpiQKKPETVKPLQISSLSEAT 118
Cdd:pfam09731 1 KSGFGKFFVALVLIVGVGYGGVVLYAYKDDNFRDFFEEYIPYGEEVVLYALGEDPPL----APKPKTFRPLQPSVVSAVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 119 KDSKQPKAKAKKSDPAPPPSVEEAPApapalqsleaeecckecTEPEPAVKERPAEEvtarlAQQDKAELDALAALTAGL 198
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVA-----------------EEEKEATKDAAEAK-----AQLPKSEQEKEKALEEVL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 199 EETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERAravddagealfkakgelEKLRS 278
Cdd:pfam09731 135 KEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALA-----------------EKLKE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 279 VIDKAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSELVNEAKAQFQQELANITPEIQANWKGL 358
Cdd:pfam09731 198 VINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKED 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 359 SgKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLEdQKAQERAVISALEHSRE----DMRLEQEKKV 434
Cdd:pfam09731 278 N-LLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEE-LDKLAEELSARLEEVRAadeaQLRLEFERER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 435 QEVREVMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEILNSKMMEQEthyrrltqeqlDTFTLDMNAAYARLKG 514
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEER-----------AGRLLKLNELLANLKG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 515 IEEAIDSHVIAEEEARKAHQLWLSVEALNYTLKSAGADSPTEPLEGAVRAIKESCAENEFAQALAIAIPEESLNRGIYSE 594
Cdd:pfam09731 425 LEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASDDEVVKAALASLPEEAYQRGVYTE 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 595 ASLRARFYDIRRLARRVALIDETRNSLYQYFLSYLQSVLLFERDQeappAKLAPEDLDTFKLLAYATYSIERGDLELAAK 674
Cdd:pfam09731 505 AALRERFRRVAKEVRKVSLIDPEGAGLLSHALSYLLSKLMFKPKQ----GEADPAGDDVESILARAEYYLEEGDLDSAAR 580
|
650 660 670
....*....|....*....|....*....|....*...
gi 528499599 675 FVNQLRGESQRVAQDWLKEARLTLETKQVISLLSAYAN 712
Cdd:pfam09731 581 EMNSLKGWSKKLASDWLKEARRRLEVQQALELLQAEAA 618
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-535 |
1.37e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 246 QALNEALNERARAVDDAGEALFKAKGELEKLRSVIDKAKQsKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKI 325
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 326 VSQYSELVNEAKAQFQQELANITPEIQAnwkglsgklSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKL 405
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEE---------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 406 EDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAhtdhlRDVLKVQEQELREEAQEILNSKMME 485
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-----EALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 528499599 486 QETHYRRLTQEQLDTFTLDMNAAYARLKGIEEAIDSHVIAEEEARKAHQL 535
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
100-487 |
9.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 100 QKKPETVKPLQISSLSEATKDSKQPKAKAKKSDPApppsvEEAPAPAPalQSLEAEECCKECTEPEPAVK-ERPAEEVTA 178
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAE--EAKKADEAKKKAEEAKKADEaKKKAEEAKK 1497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 179 RLAQQDKAELDALAA--LTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERA 256
Cdd:PTZ00121 1498 KADEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 257 RAVDDAGEALFKAKGELEKLRSVIDKAKQSKIDSARPqilAAEENLHSmivdldkvvTKVQTAQSEAKIVSQYSELVNEA 336
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK---AEEAKIKA---------EELKKAEEEKKKVEQLKKKEAEE 1645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 337 KAQFQQ----ELANITPEIQANWKGLSGKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLED-QKAQ 411
Cdd:PTZ00121 1646 KKKAEElkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAE 1725
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528499599 412 ERAVISALEHSREDMrlEQEKKVQEVRevMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEILNSKMMEQE 487
Cdd:PTZ00121 1726 EENKIKAEEAKKEAE--EDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
99-498 |
4.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 99 IQKKPETVKPLQisslsEATKDSKQPKAKAKKSDPApppsvEEAPAPAPALQSlEAEECCKECTEPEPAVKERPAEEVTA 178
Cdd:PTZ00121 1383 AKKKAEEKKKAD-----EAKKKAEEDKKKADELKKA-----AAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 179 RLAQQDKAELDALAALTAGLEETLGSSAKVTLQAIGAQEAALTAiAAHTDKLREAMDSETPPDEkstqaLNEAlnERARA 258
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADE-----AKKA--EEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 259 VDDAGEALFKAKGEleKLRSVIDKAKQSKIDSARpQILAAEENlhsmivdldKVVTKVQTAQSEAKIVSQYSELVNEAKA 338
Cdd:PTZ00121 1524 ADEAKKAEEAKKAD--EAKKAEEKKKADELKKAE-ELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 339 QFQQELANITPEIQanwkglsgKLSADDLNSLiAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLED-QKAQERAVIS 417
Cdd:PTZ00121 1592 ARIEEVMKLYEEEK--------KMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 418 ALEHSREDMrlEQEKKVQEVREVMEAEmrtqlrRQAAAHTDHLRDVLKVQEQELREEAQEILNSKMMEQETHYRRLTQEQ 497
Cdd:PTZ00121 1663 AAEEAKKAE--EDKKKAEEAKKAEEDE------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
.
gi 528499599 498 L 498
Cdd:PTZ00121 1735 A 1735
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
169-366 |
1.03e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.06 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 169 KERpAEEVTARLAQQDKAELDALAALTAGLEET----LGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKS 244
Cdd:NF012221 1564 KER-AEADRQRLEQEKQQQLAAISGSQSQLESTdqnaLETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGES 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 245 TQALNEALNER-----ARAVDDAGEalfKAKGELEKLRSVIdKAKQSKIDSARPQ----ILAAEENLHSMIVDLDKVVTK 315
Cdd:NF012221 1643 GDQWRNPFAGGlldrvQEQLDDAKK---ISGKQLADAKQRH-VDNQQKVKDAVAKseagVAQGEQNQANAEQDIDDAKAD 1718
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528499599 316 VQTAQSEA--------KIVSQYSELVNEAKAQFQQELA---NITPEIQANWKGLsgKLSADD 366
Cdd:NF012221 1719 AEKRKDDAlakqneaqQAESDANAAANDAQSRGEQDASaaeNKANQAQADAKGA--KQDESD 1778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
97-542 |
3.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 97 VPIQKKPETVKPLQISSLSEATKDSKQPKaKAKKSDPAPPPSVEEAPAPAPALQSLEAEECCKECTEPEPAVKE---RPA 173
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAAR-KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavKKA 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 174 EEVTARLAQQDKAELDALAALTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALn 253
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA- 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 254 ERARAVDDAGEALFKAKGELEKLRSVI------DKAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVS 327
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAeeakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 328 QYSELVNEA-----KAQFQQELANITPEIQANWKGLSGKLSADDLNSLiAHAHRRIDQLNRELAEQRVREQIHiEVALEQ 402
Cdd:PTZ00121 1392 KADEAKKKAeedkkKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAK-KKAEEA 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 403 QKLED--QKAQERAVISALEHSREDMR---------LEQEKKVQEVREVMEAEMRTQLRR-QAAAHTDHLRDVLKVQEQE 470
Cdd:PTZ00121 1470 KKADEakKKAEEAKKADEAKKKAEEAKkkadeakkaAEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKAD 1549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528499599 471 LREEAQEILNSKMMEQETHYRRLTQEQLDTFTLDMNAAYARLKGIEEAI----DSHVIAEEEARKAHQLWLSVEAL 542
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyeEEKKMKAEEAKKAEEAKIKAEEL 1625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-466 |
8.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 167 AVKERPAEEVTARLAQQDK--AELDALAALTAGLEETLGSSAKVTLQAIGAQEAAlTAIAAHTDKLREAmdsETPPDEks 244
Cdd:COG4913 613 AALEAELAELEEELAEAEErlEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELERL---DASSDD-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 245 TQALNEALNERARAVDDAGEALFKAKGELEKLRSVIDKAKQsKIDSARPQILAAEENLHS-MIVDLDKVVTKVQTAQSEA 323
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-ELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 324 KIVSQYSELVNEAKAQF---QQELANITPEIQANWKGLSGKLSAD----------------------------------- 365
Cdd:COG4913 766 ELRENLEERIDALRARLnraEEELERAMRAFNREWPAETADLDADleslpeylalldrleedglpeyeerfkellnensi 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 366 ----DLNSLIAHAHR----RIDQLNRELAEQRVREQIHIEVALEQQKLEDQKAQERAVISALEHSREDMRLEQEKKVQEV 437
Cdd:COG4913 846 efvaDLLSKLRRAIReikeRIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAAL 925
|
330 340 350
....*....|....*....|....*....|
gi 528499599 438 REVMEaemrtQLRRQAAAHTDH-LRDVLKV 466
Cdd:COG4913 926 KRLIE-----RLRSEEEESDRRwRARVLDV 950
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
78-195 |
1.13e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 45.06 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 78 VPYSDQLFDMVLGAPPSPPVPiqKKPETVKPLQISSLSEATKDSKQPKAKAKKSDPAP-PPSVEEAPAPAPALQSLeaee 156
Cdd:PTZ00144 109 VEVGAPLSEIDTGGAPPAAAP--AAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAaAKPPEPAPAAKPPPTPV---- 182
|
90 100 110
....*....|....*....|....*....|....*....
gi 528499599 157 cckecTEPEPAVKERPAEEVTARLAQQDKAELDALAALT 195
Cdd:PTZ00144 183 -----ARADPRETRVPMSRMRQRIAERLKASQNTCAMLT 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
365-643 |
1.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 365 DDLNSLIAHAHRRIDQLNRELAEQRvREQIHIEVALEQQK---------LEDQKAQERAVISALEHSREDMRLEQEKKVQ 435
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELE-AELAELEAELEELRleleeleleLEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 436 -EVREVMEAEMRTQLRRQAAAHTDHLRDVLkvQEQELREEAQEILNSKMMEQETHYRRLTQEQLDTFTLDMNAAYARLKG 514
Cdd:COG1196 314 lEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 515 IEEAID-----SHVIAEEEARKAHQLWLSVEALNYTLKSAGADSPTEPLEGAVRAIKESCAENEFAQALAiaipEESLNR 589
Cdd:COG1196 392 LRAAAElaaqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL----LELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528499599 590 GIYSEASLRARFYDIRRLARRVALIDETRNSLYQYFLSYLQSVLLFERDQEAPP 643
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-472 |
3.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 215 AQEAALTAIAAHTDKLREAmdsetppdeKSTQALNEALNERARaVDDAGEALFKAKGELEKLRSVIDKAKQsKIDSARPQ 294
Cdd:COG4913 249 EQIELLEPIRELAERYAAA---------RERLAELEYLRAALR-LWFAQRRLELLEAELEELRAELARLEA-ELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 295 ILAAEENLHSMIVDLDKV-VTKVQTAQSEAKIVSQYSELVNEAKAQFQQELANItpeiqanwkGLSGKLSADDLNSLIAH 373
Cdd:COG4913 318 LDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAL---------GLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 374 AHRRIDQLNRELAeqRVREQIHiEVALEQQKLEDQKAQERAVISALEHSREDMRLEQEkkvqevrevmeaEMRTQLRRQA 453
Cdd:COG4913 389 AAALLEALEEELE--ALEEALA-EAEAALRDLRRELRELEAEIASLERRKSNIPARLL------------ALRDALAEAL 453
|
250 260
....*....|....*....|..
gi 528499599 454 AAHTDHLR---DVLKVQEQELR 472
Cdd:COG4913 454 GLDEAELPfvgELIEVRPEEER 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-446 |
1.07e-03 |
|
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: 42.35 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 181 AQQDKAEldALAALTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERARAVD 260
Cdd:TIGR02168 207 RQAEKAE--RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 261 DAGEALFKAKGELEKLRSVIDKAKQSKIDSARPQILAAE--ENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSELVNEAKA 338
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 339 QFQQELANITPEIQANWKGLSGKLSA-------------------DDLNSLIAHAHRRIDQLNRELAEQRVREqIHIEVA 399
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQlelqiaslnneierlearlERLEDRRERLQQEIEELLKKLEEAELKE-LQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528499599 400 LEQQKLEDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMR 446
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
237-531 |
1.16e-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: 42.52 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 237 ETPPDEKSTQALNEALNERARAVDDAGEALFKAKGELEKLRSVIDKAkQSKIDSARPQILAAEENLHSMIVDLDKVVTKV 316
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA-SREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 317 QTAQSEAK---------IVSQYSELVNE---AKAQFQQELANITPEIQANWKGLSGKLSA------DDLNSLIAHAHRRI 378
Cdd:pfam12128 670 NKALAERKdsanerlnsLEAQLKQLDKKhqaWLEEQKEQKREARTEKQAYWQVVEGALDAqlallkAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 379 DQLN----RELAEQRVREQIHIEVALE----QQKLEDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEA--EMRTQ 448
Cdd:pfam12128 750 KALEtwykRDLASLGVDPDVIAKLKREirtlERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAisELQQQ 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 449 LRRQAAahtDHLRDVLKVQEQELREEAQEILnskmMEQETHYRRLTQEQLDTFTLDMNAAYA------RLKGIEEAIDSH 522
Cdd:pfam12128 830 LARLIA---DTKLRRAKLEMERKASEKQQVR----LSENLRGLRCEMSKLATLKEDANSEQAqgsigeRLAQLEDLKLKR 902
|
....*....
gi 528499599 523 VIAEEEARK 531
Cdd:pfam12128 903 DYLSESVKK 911
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
90-173 |
2.11e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 40.94 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 90 GAPPSPPvpiqKKPETVKPLQISSLsEATKDSKQPKAKAKKSDPAPPPSVEEAPAPAPALQSLEAEECCKECTE--PEPA 167
Cdd:PRK12373 240 PVPPSEA----ARPKSADAETNAAL-KTPATAPKAAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAAAAAKPALEdkPRPL 314
|
....*.
gi 528499599 168 VKERPA 173
Cdd:PRK12373 315 GIARPG 320
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-666 |
2.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 169 KERPAEEVTARLAQQDKAELDALAALTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSetppdEKSTQAL 248
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-----EAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 249 NEALNERARAVDDAGEALFKAKGELEklrsvidkAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQ 328
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELL--------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 329 YSELVNEAKAQFQQELANITPEIQANwkglsgKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEV-ALEQQKLED 407
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEAL------LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAeADYEGFLEG 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 408 QKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAHTDHLRDVLKvqeQELREEAQEILNSKMMEQE 487
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---AAKAGRATFLPLDKIRARA 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 488 THYRRLTQEQLDTFTLDMNAAYARLKGIEEAIDSHVIAEE-EARKAHQLWLSVEALNYTLKSAGADSPT-EPLEGAVRAI 565
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlVAARLEAALRRAVTLAGRLREVTLEGEGgSAGGSLTGGS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 566 KESCAENEFAQALAIAIPEESLNRGIYSEASLRARFYDIRRLARRVALIDETRNSLYQYFLSYLQSVLLFERDQEAPPAK 645
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
490 500
....*....|....*....|.
gi 528499599 646 LAPEDLDTFKLLAYATYSIER 666
Cdd:COG1196 747 LLEEEALEELPEPPDLEELER 767
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
492-713 |
2.43e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.42 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 492 RLTQEQLDTFTLDMNAAYARLKGIEEAIDSHVIAEEEARKAHQLWLSVEALNYTLKSAGadsptePLEGAVRAIKESCAE 571
Cdd:COG4223 49 ALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQ------PFAAELAALEALAPD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 572 NEFAQALaiaipEESLNRGIYSEASLRARFYDIRRLARRVALIDETRNSLYQYFLSYLQSVL----LFERDQEAPPAkla 647
Cdd:COG4223 123 APALAAL-----AAFAATGVPTLAALRAEFPAAARAALAAARAPEADASWLDRLLAFARSLVtvrrVGPVEGDDPDA--- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528499599 648 pedldtfkLLAYATYSIERGDLELAAKFVNQLRGESQRVAQDWLKEARLTLETKQVISLLSAYANA 713
Cdd:COG4223 195 --------ILARAEAALAAGDLAGALAELEALPEAAQAAAAPWIAKAEARLAADAALQALAAQALA 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-497 |
3.14e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 334 NEAKAQFQQELANITPEIQANWKGLSG-----KLSADDLNSL---IAHAHRRIDQLNRELAEQRVR-EQIHIEVALEQQK 404
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAlkkeeKALLKQLAALerrIAALARRIRALEQELAALEAElAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 405 LEDQKAQERAVISAL----EHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEiLN 480
Cdd:COG4942 99 LEAQKEELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE-LE 177
|
170
....*....|....*..
gi 528499599 481 SKMMEQETHYRRLTQEQ 497
Cdd:COG4942 178 ALLAELEEERAALEALK 194
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
253-530 |
3.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 253 NERARAVDDAGEALFKAKGELEKLRSVIdKAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSEL 332
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHL-KSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 333 VNEAKAQFQQElanitPEIQANWKGLSGKLSADDLNSLIA-----HAHRRIDQLNRELAEQRVREQIHIEVA-LEQQKLE 406
Cdd:TIGR00606 914 LETFLEKDQQE-----KEELISSKETSNKKAQDKVNDIKEkvkniHGYMKDIENKIQDGKDDYLKQKETELNtVNAQLEE 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 407 DQKAQERAvisalehsREDMRL-EQEKKVQEVREVMEAEMRTQLRRqaaahtdhlRDVLKVQEQELREEAQEILNSKMME 485
Cdd:TIGR00606 989 CEKHQEKI--------NEDMRLmRQDIDTQKIQERWLQDNLTLRKR---------ENELKEVEEELKQHLKEMGQMQVLQ 1051
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528499599 486 QETHYRRLtQEQLDTFTLDMNAAYARLKGIEEAIdshVIAEEEAR 530
Cdd:TIGR00606 1052 MKQEHQKL-EENIDLIKRNHVLALGRQKGYEKEI---KHFKKELR 1092
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-519 |
3.61e-03 |
|
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: 40.82 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 213 IGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERARAVDDAGealfKAKGELEKLRSVIDKAKQSKidsar 292
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE----KLKERLEELEEDLSSLEQEI----- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 293 pqilaaeENLHSMIVDLDKVVtkvqtAQSEAKIvSQYSELVNEAKAQFQQElanITPEIQAnwkglsgklSADDLNSLIA 372
Cdd:TIGR02169 754 -------ENVKSELKELEARI-----EELEEDL-HKLEEALNDLEARLSHS---RIPEIQA---------ELSKLEEEVS 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 373 HAHRRIDQLNRELAEQRVREQI---HIEVALEQQK-LEDQKAQERAVISALEHSREDMRLEQEKKVQEVREV-------- 440
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYlekEIQELQEQRIdLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlk 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 441 -----MEAEMRTQLRR--QAAAHTDHLRD---VLKVQEQELREEAQEILNSKMMEQETHYRRLTQEQLdtftldmnaaYA 510
Cdd:TIGR02169 889 kerdeLEAQLRELERKieELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV----------QA 958
|
....*....
gi 528499599 511 RLKGIEEAI 519
Cdd:TIGR02169 959 ELQRVEEEI 967
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-479 |
4.28e-03 |
|
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: 40.44 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 210 LQAIGAQEAALTAIAAHTDKLREAMDSETPPDEKSTQALNEALNERARAVddagEALFKAKGELE-KLRSVIDKAKQSKI 288
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEaRLSHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 289 DSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQYSELVNEAKAQFQQELANIT---PEIQANWKGLSGKLSad 365
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALR-- 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 366 DLNSLIAHAHRRIDQLNRELAE-QRVREQIHIEVALEQQKLEDQKAQ-----------ERAVISALEHSREDMRLEqekK 433
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRElERKIEELEAQIEKKRKRLSELKAKlealeeelseiEDPKGEDEEIPEEELSLE---D 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528499599 434 VQEVREVMEAEMRT-----QLRRQAAAHTDHLRDVLKVQEQELREEAQEIL 479
Cdd:TIGR02169 956 VQAELQRVEEEIRAlepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
219-476 |
6.18e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 219 ALTAIAAHTDKLR----EAMDSETPPDEKSTQALNEALNerarAVDDAGEALFKAKgeleKLRSVID------KAKQSKI 288
Cdd:PRK10929 17 AYAATAPDEKQITqeleQAKAAKTPAQAEIVEALQSALN----WLEERKGSLERAK----QYQQVIDnfpklsAELRQQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 289 DSARPQILAAEENLHSMivDLDKVVTKV-----------QTAQSEAKIVS--------QYSE---LVNEAKAQFQQELAN 346
Cdd:PRK10929 89 NNERDEPRSVPPNMSTD--ALEQEILQVssqlleksrqaQQEQDRAREISdslsqlpqQQTEarrQLNEIERRLQTLGTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 347 ITPEIQANWKGLSGKLSAD-------DLNSLIAHAHRRIDQLNRELAEQRvREQIHIEVALEQQKLEDQKAQERAviSAL 419
Cdd:PRK10929 167 NTPLAQAQLTALQAESAALkalvdelELAQLSANNRQELARLRSELAKKR-SQQLDAYLQALRNQLNSQRQREAE--RAL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528499599 420 EHSRedMRLEQE--------KKVQEVREVMEA--------EMRTQLRRQAAAHTDHLRDVLKVqeqeLREEAQ 476
Cdd:PRK10929 244 ESTE--LLAEQSgdlpksivAQFKINRELSQAlnqqaqrmDLIASQQRQAASQTLQVRQALNT----LREQSQ 310
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
383-487 |
6.19e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 383 RELAEQRVREQIhieVALEQQKLEDQKAQeravisaLEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAhtdhLRD 462
Cdd:cd16269 198 KEIEAERAKAEA---AEQERKLLEEQQRE-------LEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA----LES 263
|
90 100
....*....|....*....|....*
gi 528499599 463 VLKVQEQELREEAQEIlnSKMMEQE 487
Cdd:cd16269 264 KLKEQEALLEEGFKEQ--AELLQEE 286
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
88-146 |
8.79e-03 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 38.45 E-value: 8.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 528499599 88 VLGAPPSPPVPIQKKPETVKPLQISSLSEATKDSKQPKAKAkKSDPAPPPSVEEAPAPA 146
Cdd:PRK11633 89 TVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPP-APKPEPKPVVEEKAAPT 146
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-478 |
8.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 173 AEEVTARLAQQDKAELDALAALTAGLEETLGSSAKVTLQAIGAQEAALTAIAAHTDKLREAMDSETppdekSTQALNEAL 252
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIV 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 253 NERARAVDDAGEAL-FKAKGELEKLR-SVIDKAKQSKIDSARPQILAAEENLHSMIVDLDKVVTKVQTAQSEAKIVSQYS 330
Cdd:COG1196 553 VEDDEVAAAAIEYLkAAKAGRATFLPlDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 331 ELVNEAKAQFQQELANITPEIQ-ANWKGLSGKLSADDLNSLIAHAHRRIDQLNRELAEQRVREQIHIEVALEQQKLEDQK 409
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEgGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528499599 410 AQERAvisalEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRQAAAHTDHLRDVLKVQEQELREEAQEI 478
Cdd:COG1196 713 EEERL-----EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
322-535 |
9.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 322 EAKIVSQYSELVNEAKAQFQQELANITPEIQANWKGLSGKLSADDLNSL----IAHAHRRIDQLNRelAEQRVREQIHIE 397
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAeearKAEDARKAEEARK--AEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 398 VALEQQKLEDQKAQERAVISALEHSREDMRLEQEKKVQEVREVMEAEMRTQLRRqaaahtdhLRDVLKVQEQELREEAQE 477
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK--------AEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528499599 478 ILNSKMMEQETHY--RRLTQEQLDTFTLDMNAAYARLKGIEEAidshviaeEEARKAHQL 535
Cdd:PTZ00121 1232 AEEAKKDAEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKA--------EEARKADEL 1283
|
|
|