|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
3.07e-120 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 377.09 E-value: 3.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 44 GGRPQRCMPEFVNAAFNVTVVATNTCGTP-PEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQT 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 123 MLAGVQYpssINLTLHLGKAFDITYVRLKFHTSRPeSFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGgDEQQ 202
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 203 ALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFND-PKVLKSYYYAISDFA 281
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 145309326 282 VGG 284
Cdd:smart00136 236 VGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
9.19e-115 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 361.51 E-value: 9.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 50 CMPEFVNAAFNVTVVATNTCGT-PPEEYCVQTGVTGVtKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLagVQ 128
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLnGPERYCILSGLEGG-KKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 129 YPSsINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGfiRTGGDEQQALCTDE 208
Cdd:pfam00055 78 YEN-VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309326 209 FSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGG 284
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
553-678 |
2.00e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.87 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 553 SYFPRYFIAPAKFLGKQVLSYGQNLSFSFRVD--RRDTRLSAEDLVLEGAGLRVSVPliAQGNSYPSE-TTVKYVFRLHE 629
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHP--AEGPPLPDElTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145309326 630 ATDYPWRPALTPfEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLASARP 678
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
558-688 |
2.71e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 142.79 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 558 YFIAPAKFLGKQVLSYGQNLSFSFRVDRRD---TRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTvKYVFRLHEATdyp 634
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPgggSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQ-TYSVRLHEEN--- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 635 WR----PALTPFEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLASARPGP-GVPATWVE 688
Cdd:pfam00052 77 WRdsdgAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGsGPPASWVE 136
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1040-1581 |
9.93e-18 |
|
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: 89.40 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1040 DKVADHRVKLQELESLIANLGTG-DEMVTdqAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQIS--- 1115
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNiEKMIL--AFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSlll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1116 --------RLQNIRNTIEET----GNLAEQARAHVENTERLIEIA---SRELEKAKVAAANVSVTQPESTGDPNNMT--- 1177
Cdd:pfam05483 247 iqitekenKMKDLTFLLEESrdkaNQLEEKTKLQDENLKELIEKKdhlTKELEDIKMSLQRSMSTQKALEEDLQIATkti 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1178 --LLAEEARKLAERHKQEADDIVRVakTANDTSTEAYNLLLRTlagenqtafEIEELNRKYEQAKNISQDLEKQAARVHE 1255
Cdd:pfam05483 327 cqLTEEKEAQMEELNKAKAAHSFVV--TEFEATTCSLEELLRT---------EQQRLEKNEDQLKIITMELQKKSSELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1256 EAKRAGDKAVEIyasvaqlspldsETLEneanniKMEAENlEQLIDQKlKDYEDLREDMRGKELEVKNLLEKGKTE---- 1331
Cdd:pfam05483 396 MTKFKNNKEVEL------------EELK------KILAED-EKLLDEK-KQFEKIAEELKGKEQELIFLLQAREKEihdl 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1332 --QQTA-------------------DQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRK 1390
Cdd:pfam05483 456 eiQLTAiktseehylkevedlktelEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1391 IPAINQTITEANEKTREAQQalgsaaadatEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ--- 1467
Cdd:pfam05483 536 IENLEEKEMNLRDELESVRE----------EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQien 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1468 -------LQEAEKELKRKqDDADQDMMMAGMASQAAQEAEINARKAKnsvtsLLSIINDLLEQLGQLDTVDLNKLNEIEG 1540
Cdd:pfam05483 606 knknieeLHQENKALKKK-GSAENKQLNAYEIKVNKLELELASAKQK-----FEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 145309326 1541 TLNKAKDEMKVsdldRKVSDLENEAKKQE-AAIMD-----YNRDIEE 1581
Cdd:pfam05483 680 AKAIADEAVKL----QKEIDKRCQHKIAEmVALMEkhkhqYDKIIEE 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1035-1572 |
1.35e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1035 YRLVKDKVADHRVKLQELESLIANLgtgdeMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQI 1114
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1115 SRLQNIRNTIEE-TGNLAEQARAHVENTERLIEIASRELE-KAKVAAANVSVTQpestgdpnnmtlLAEEARKLAERHKQ 1192
Cdd:COG1196 309 ERRRELEERLEElEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAE------------AEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1193 EADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKA---VEIYA 1269
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAeeeAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1270 SVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDY--EDLREDMRGKELEVKNLLEKgktEQQTADQLLARADAAKA 1347
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllLEAEADYEGFLEGVKAALLL---AGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1348 LAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTRE---AQQALGSAAADATEAKN 1424
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1425 KAH------EAERIASAVQKNATSTKAEAERTFAEVTDLDNEVN-----------NMLKQLQEAEKELKRKQDDADQDMM 1487
Cdd:COG1196 614 RYYvlgdtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSaggsltggsrrELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1488 MAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRkvSDLENEAKK 1567
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL--EELERELER 771
|
....*
gi 145309326 1568 QEAAI 1572
Cdd:COG1196 772 LEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1181-1597 |
7.04e-15 |
|
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: 80.49 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1181 EEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRA 1260
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1261 GDKAVEIYASVAQLSPLDSETLEneannikmEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKgkteqqtadqlla 1340
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEE------------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1341 radaakalaeeaakkGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALgsaaADAT 1420
Cdd:TIGR02168 819 ---------------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1421 EAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ----LQEAEKELKRKQDD-ADQDMMMAGMASQA 1495
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQERlSEEYSLTLEEAEAL 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1496 AQEAEINARKAKNSVTSLlsiiNDLLEQLGqldTVDLNKLNEIEgTLNKAKDEmkvsdLDRKVSDLeNEAKKQ-EAAIMD 1574
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRL----ENKIKELG---PVNLAAIEEYE-ELKERYDF-----LTAQKEDL-TEAKETlEEAIEE 1025
|
410 420
....*....|....*....|...
gi 145309326 1575 YNRDIEEIMKDIrnLEDIRKTLP 1597
Cdd:TIGR02168 1026 IDREARERFKDT--FDQVNENFQ 1046
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
935-980 |
1.74e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 1.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 935 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGFGPEGC 980
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
445-492 |
2.53e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.53 E-value: 2.53e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 445 CSCDPSGS-IDECNIETGRCVCKDNVEGFNCERCKPGFFNLESSNPRGC 492
Cdd:pfam00053 1 CDCNPHGSlSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1072-1594 |
2.64e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVnntlSSQISRLQNIRNTIEETGNLAEQARAHVE-------NTERL 1144
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKL----EKEVKELEELKEEIEELEKELESLEGSKRkleekirELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1145 IEIASRELEKAKVAAANVSVTQPEstgdpnnmtllAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQ 1224
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEK-----------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1225 TAfEIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVEIYASVAQLSP------LDS-----ETLENEANNIKMEA 1293
Cdd:PRK03918 337 EE-RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPeklekeLEElekakEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1294 ENLEQLIDQKLKDYEDLREDMR-----GKEL---EVKNLLEKGKTEQQTAdqllaradaakalaeeaakkgRDTLQEAND 1365
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGkcpvcGRELteeHRKELLEEYTAELKRI---------------------EKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1366 ILNNLKDFDRRVnDNKTAAEEALRKIPAINQTITEANEK------------TREAQQALGSAAADATEAKNKAHEAERIA 1433
Cdd:PRK03918 474 KERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKlkkynleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1434 SAVQKNAT--STKAEAERTFAEV-TDLDN-------EVNNMLKQLQE----------AEKELKRKQDDADQDMMMAGMAS 1493
Cdd:PRK03918 553 ELKKKLAEleKKLDELEEELAELlKELEElgfesveELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1494 QAAQEAEINARKAKNSVTSLLSIINDllEQLGQLDTVDLNKLNEIEG------TLNKAKDEMKvSDLDrkvsDLENEAKK 1567
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGlraeleELEKRREEIK-KTLE----KLKEELEE 705
|
570 580
....*....|....*....|....*..
gi 145309326 1568 QEAAIMDynrdIEEIMKDIRNLEDIRK 1594
Cdd:PRK03918 706 REKAKKE----LEKLEKALERVEELRE 728
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
934-981 |
1.52e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.52e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 934 RCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGF--GPEGCK 981
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
935-983 |
1.33e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.53 E-value: 1.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 935 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGFGPEGCKPC 983
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-445 |
2.97e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 398 CHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPC 445
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
444-493 |
5.97e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 5.97e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 444 PCSCDPSGSI-DECNIETGRCVCKDNVEGFNCERCKPGFFNLeSSNPRGCT 493
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
724-771 |
7.40e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 7.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 724 CACNGH---SETCDPETGVCNCRDNTAGPHCEKCSDGYYGDSTAGTssDCQ 771
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
445-492 |
2.30e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 445 CSCDPSGSIDE-CNIETGRCVCKDNVEGFNCERCKPGFFNlesSNPRGC 492
Cdd:smart00180 1 CDCDPGGSASGtCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-442 |
2.35e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 398 CHCSPVGSLSTQCDS-YGRCSCKPGVMGDKCDRCQPGFHSLTEAGC 442
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
724-763 |
2.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 2.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 145309326 724 CACNGH---SETCDPETGVCNCRDNTAGPHCEKCSDGYYGDST 763
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
883-933 |
4.30e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 4.30e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 883 ACNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNLQS-GQGCE 933
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-443 |
5.18e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 5.18e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 397 SCHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEA--GCR 443
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
982-1029 |
1.10e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 1.10e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 982 PCDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYFYNRSWP-GCQ 1029
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
884-932 |
1.13e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.13e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 884 CNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNLQ--SGQGC 932
Cdd:pfam00053 1 CDCNPHGS--LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
724-765 |
1.94e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 1.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 145309326 724 CACNG---HSETCDPETGVCNCRDNTAGPHCEKCSDGYYGDSTAG 765
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
884-932 |
2.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 884 CNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNlQSGQGC 932
Cdd:smart00180 1 CDCDPGGS--ASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
983-1028 |
2.50e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.50e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 145309326 983 CDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYfYNRSWPGC 1028
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
983-1029 |
6.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 6.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 145309326 983 CDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQ 1029
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1063-1506 |
8.42e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1063 DEMVTDQafEDRLKEAEREVMDLLRE-----AQDVKDVDQNLMDRLQRVNNTLSSqisRLQNIRNTIEETGNLAEQARAH 1137
Cdd:NF041483 86 DQLRADA--ERELRDARAQTQRILQEhaehqARLQAELHTEAVQRRQQLDQELAE---RRQTVESHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1138 VEN-TERLIEIASRELEKAkVAAANVSVTQpestgdpnnmtlLAEEARKL----AERHKQEADDIVRVAKT--------- 1203
Cdd:NF041483 161 TESqARRLLDESRAEAEQA-LAAARAEAER------------LAEEARQRlgseAESARAEAEAILRRARKdaerllnaa 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1204 ---ANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQ----AKNISQDLEKQAARVHEEAKRAGDKAVEIYASV----- 1271
Cdd:NF041483 228 stqAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQrmqeAEEALREARAEAEKVVAEAKEAAAKQLASAESAneqrt 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1272 ----AQLSPLDSE-TLENEAnnIKMEAEnleqlidQKLKDYEDLREDMrgkeleVKNLLEKGKT--EQQTADQLLARADA 1344
Cdd:NF041483 308 rtakEEIARLVGEaTKEAEA--LKAEAE-------QALADARAEAEKL------VAEAAEKARTvaAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1345 AKALAEEAAKKGRDTLQ----------------------EANDILNNLKDF---DRRVNDNKTA--AEEALR-------- 1389
Cdd:NF041483 373 AEEVLTKASEDAKATTRaaaeeaerirreaeaeadrlrgEAADQAEQLKGAakdDTKEYRAKTVelQEEARRlrgeaeql 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1390 ---------KI--PAINQTITEANEKTREAQQALGSAAADATEAKNKAH-EAERIASAVQKNATS-----------TKAE 1446
Cdd:NF041483 453 raeavaegeRIrgEARREAVQQIEEAARTAEELLTKAKADADELRSTATaESERVRTEAIERATTlrrqaeetlerTRAE 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1447 AERTFAEVTDLDNEV----NNMLKQLQ------------EAEKELKRKQDDADQDMMMAGMA-SQAAQEAEINARKA 1506
Cdd:NF041483 533 AERLRAEAEEQAEEVraaaERAARELReeteraiaarqaEAAEELTRLHTEAEERLTAAEEAlADARAEAERIRREA 609
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
828-875 |
2.24e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 145309326 828 CQCSDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNPLAP 875
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1091-1302 |
3.34e-08 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 56.53 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1091 DVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPEST 1170
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1171 G-----------------------DPNNMTLL-------------------AEEARKLAERHKQEADDIVRVAKTANDTS 1208
Cdd:smart00283 81 SaveeleessdeigeivsviddiaDQTNLLALnaaieaarageagrgfavvADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1209 TEAYNLLLRT---------LAGENQTAFE-----IEELNrkyEQAKNISQDLEKQAARVHEEAkragdKAVEIYASVAQL 1274
Cdd:smart00283 161 NEAVAAMEESsseveegveLVEETGDALEeivdsVEEIA---DLVQEIAAATDEQAAGSEEVN-----AAIDEIAQVTQE 232
|
250 260
....*....|....*....|....*...
gi 145309326 1275 SPLDSETLENEANNIKMEAENLEQLIDQ 1302
Cdd:smart00283 233 TAAMSEEISAAAEELSGLAEELDELVER 260
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1069-1605 |
3.70e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.22 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1069 QAFEDRL-KEAEREVMDLL----REAQDVKDVDQNLMDRLQRvnntlssQISRLqniRNTIEETgnlAEQARAHV-ENTE 1142
Cdd:NF041483 752 QAEAQRLvEEADRRATELVsaaeQTAQQVRDSVAGLQEQAEE-------EIAGL---RSAAEHA---AERTRTEAqEEAD 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1143 RLIEIASRELEKAKVAAANVSVTQPESTgdpnnmtllaEEARKLAERHKQEAddIVRVAKTANDTS-------TEAYNll 1215
Cdd:NF041483 819 RVRSDAYAERERASEDANRLRREAQEET----------EAAKALAERTVSEA--IAEAERLRSDASeyaqrvrTEASD-- 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1216 lrTLAGENQTAFEIEELNRkyEQAKNISQDLEKQAARVHEEAKRAGDKAVEiyASVAQLSPLDSETLENEANNIKMEAEN 1295
Cdd:NF041483 885 --TLASAEQDAARTRADAR--EDANRIRSDAAAQADRLIGEATSEAERLTA--EARAEAERLRDEARAEAERVRADAAAQ 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1296 LEQLIDQKLKDYEDLREDMRgkelevknllEKGKTEQQTADQLLARADAAKALAEEAAKKGR-DTLQEANDILNnlkdfD 1374
Cdd:NF041483 959 AEQLIAEATGEAERLRAEAA----------ETVGSAQQHAERIRTEAERVKAEAAAEAERLRtEAREEADRTLD-----E 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1375 RRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQAlgsAAADATEAKNKA--------HEAERIAS--AVQKNATSTK 1444
Cdd:NF041483 1024 ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEE---ALRTTTEAEAQAdtmvgaarKEAERIVAeaTVEGNSLVEK 1100
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1445 AEAE---------------RTFAEvtDLDNEVNNMLKQLQEaekelkRKQDDADQDMMMAG------MASQAAQEAEINA 1503
Cdd:NF041483 1101 ARTDadellvgarrdataiRERAE--ELRDRITGEIEELHE------RARRESAEQMKSAGercdalVKAAEEQLAEAEA 1172
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1504 rKAKnsvtSLLSIINDlleqlgQLDTVDLNKLNEIEGTLNKAkdEMKVSDLDRKVSDLENEAKKQ-EAAIMDYNRDI--- 1579
Cdd:NF041483 1173 -KAK----ELVSDANS------EASKVRIAAVKKAEGLLKEA--EQKKAELVREAEKIKAEAEAEaKRTVEEGKRELdvl 1239
|
570 580 590
....*....|....*....|....*....|
gi 145309326 1580 ----EEIMKDIRNLEDIRKTLPSgcFNTPS 1605
Cdd:NF041483 1240 vrrrEDINAEISRVQDVLEALES--FEAPS 1267
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
828-876 |
6.56e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 828 CQCSDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNPLAPN 876
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1042-1507 |
7.45e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.45 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1042 VADHRVklqELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQ-DVKDVDQNLMDRLQRVNNTLSSQISRLQNI 1120
Cdd:NF041483 336 LADARA---EAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASeDAKATTRAAAEEAERIRREAEAEADRLRGE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1121 RNTIEE----------------TGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTgdpnnmtllAEEAR 1184
Cdd:NF041483 413 AADQAEqlkgaakddtkeyrakTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEA---------ARTAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1185 KLAERHKQEADDIVRVAKTANDTsteaynllLRTLAGENQTAF--EIEE-LNRKYEQAKNISQDLEKQAARVHEEAKRAg 1261
Cdd:NF041483 484 ELLTKAKADADELRSTATAESER--------VRTEAIERATTLrrQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERA- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1262 dkAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLL-----EKGKTEQQTAD 1336
Cdd:NF041483 555 --ARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrteaaERIRTLQAQAE 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1337 QLLARADAAKALAEEAAKKGRDTL---------QEANDILNNLKDFDRRVNDNKTAAEE--ALRKIPAINQTITEANEKT 1405
Cdd:NF041483 633 QEAERLRTEAAADASAARAEGENVavrlrseaaAEAERLKSEAQESADRVRAEAAAAAErvGTEAAEALAAAQEEAARRR 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1406 REAQQALGSAAADATEAKNKAHEA--ERIASAvQKNATSTKAEAERTFAEV----TDLDNEVNNMLKQLQEAEKELkrkQ 1479
Cdd:NF041483 713 REAEETLGSARAEADQERERAREQseELLASA-RKRVEEAQAEAQRLVEEAdrraTELVSAAEQTAQQVRDSVAGL---Q 788
|
490 500
....*....|....*....|....*...
gi 145309326 1480 DDADQDmmMAGMASQAAQEAEINARKAK 1507
Cdd:NF041483 789 EQAEEE--IAGLRSAAEHAAERTRTEAQ 814
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-330 |
7.91e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 7.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 285 RCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRR 330
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1067-1506 |
1.25e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.68 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1067 TDQAFEDRLKEAEREVMDLLREAQDvkdvdqnlmdRLQRVNNTLSSQISRLQNIRntiEETGNLAEQARAhvENTERLIE 1146
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEE----------RLTAAEEALADARAEAERIR---REAAEETERLRT--EAAERIRT 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1147 I---ASRELEKAKV-AAANVSVTQPESTgdpNNMTLLAEEARKLAERHK---QEADDIVR--VAKTANDTSTEAYNLLLR 1217
Cdd:NF041483 627 LqaqAEQEAERLRTeAAADASAARAEGE---NVAVRLRSEAAAEAERLKseaQESADRVRaeAAAAAERVGTEAAEALAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1218 TLAGENQTAFEIEEL--------NRKYEQAKNISQDL-----------EKQAARVHEEA-KRAGD-------KAVEIYAS 1270
Cdd:NF041483 704 AQEEAARRRREAEETlgsaraeaDQERERAREQSEELlasarkrveeaQAEAQRLVEEAdRRATElvsaaeqTAQQVRDS 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1271 VAQLSPLDSETL-------ENEANNIKMEAENLEQLI--------DQKLKDYEDLREDMRGKELEVKNLLEKGKTE---- 1331
Cdd:NF041483 784 VAGLQEQAEEEIaglrsaaEHAAERTRTEAQEEADRVrsdayaerERASEDANRLRREAQEETEAAKALAERTVSEaiae 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1332 -----QQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKD-----FDRRVNDNKTAAEEALRKIPA-----INQ 1396
Cdd:NF041483 864 aerlrSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSdaaaqADRLIGEATSEAERLTAEARAeaerlRDE 943
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1397 TITEANEKTREAQQALGSAAADAT-EAKN-KAHEAERIASAvQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ-----LQ 1469
Cdd:NF041483 944 ARAEAERVRADAAAQAEQLIAEATgEAERlRAEAAETVGSA-QQHAERIRTEAERVKAEAAAEAERLRTEAREeadrtLD 1022
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 145309326 1470 EAEKEL-KRKQDDADQ-DMMMAGMASQAAQ---EAEINARKA 1506
Cdd:NF041483 1023 EARKDAnKRRSEAAEQaDTLITEAAAEADQltaKAQEEALRT 1064
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-820 |
5.44e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 5.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 772 PCPCPGGSSCAVVPKTKEVVCTnCPTGTTGKRCELCDDGYFGDPLGRNG 820
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
342-396 |
5.75e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.96 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 342 CDCNGR---SQECYFdpelyrstgHGGHCTnCQDNTDGAHCERCRENFFRLGNNEACS 396
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
828-872 |
5.94e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 5.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 145309326 828 CQCsdNIDPNAVGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNP 872
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1394-1497 |
1.21e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1394 INQTITEANEKTREAQQALGSAAADATEAKNkahEAERIASAVQKNATSTKAEAertfaeVTDLDNEVNNMLKQlqeAEK 1473
Cdd:cd06503 35 IAESLEEAEKAKEEAEELLAEYEEKLAEARA---EAQEIIEEARKEAEKIKEEI------LAEAKEEAERILEQ---AKA 102
|
90 100
....*....|....*....|....*.
gi 145309326 1474 ELKRKQDDADQDM--MMAGMASQAAQ 1497
Cdd:cd06503 103 EIEQEKEKALAELrkEVADLAVEAAE 128
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
341-389 |
2.20e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 2.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 341 PCDCNGR---SQECYFdpelyrstgHGGHCTnCQDNTDGAHCERCRENFFRL 389
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
286-327 |
4.40e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 4.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 145309326 286 CKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRP 327
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
286-328 |
1.79e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 145309326 286 CKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPW 328
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1377-1571 |
2.69e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1377 VNDNKTAAEEaLRkipaiNQTITEA----NEKTREAQQALGSAAAdateaknkahEAERIASAVQKNATStKAEAERTfa 1452
Cdd:NF041483 147 VNENVAWAEQ-LR-----ARTESQArrllDESRAEAEQALAAARA----------EAERLAEEARQRLGS-EAESARA-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1453 evtdldnevnnmlkqlqEAEKELKRKQDDADQdmmMAGMASQAAQEAEINARKAKNSVTSLlsiINDLLEQLGQLDTVDL 1532
Cdd:NF041483 208 -----------------EAEAILRRARKDAER---LLNAASTQAQEATDHAEQLRSSTAAE---SDQARRQAAELSRAAE 264
|
170 180 190
....*....|....*....|....*....|....*....
gi 145309326 1533 NKLNEIEGTLNKAKDEMkvsdlDRKVSDLENEAKKQEAA 1571
Cdd:NF041483 265 QRMQEAEEALREARAEA-----EKVVAEAKEAAAKQLAS 298
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
342-388 |
5.66e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.14 E-value: 5.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 342 CDCNGR---SQECYFDpelyrstghGGHCTnCQDNTDGAHCERCRENFFR 388
Cdd:smart00180 1 CDCDPGgsaSGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
3.07e-120 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 377.09 E-value: 3.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 44 GGRPQRCMPEFVNAAFNVTVVATNTCGTP-PEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQT 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 123 MLAGVQYpssINLTLHLGKAFDITYVRLKFHTSRPeSFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGgDEQQ 202
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 203 ALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFND-PKVLKSYYYAISDFA 281
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 145309326 282 VGG 284
Cdd:smart00136 236 VGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
9.19e-115 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 361.51 E-value: 9.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 50 CMPEFVNAAFNVTVVATNTCGT-PPEEYCVQTGVTGVtKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLagVQ 128
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLnGPERYCILSGLEGG-KKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 129 YPSsINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGfiRTGGDEQQALCTDE 208
Cdd:pfam00055 78 YEN-VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309326 209 FSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGG 284
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
553-678 |
2.00e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.87 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 553 SYFPRYFIAPAKFLGKQVLSYGQNLSFSFRVD--RRDTRLSAEDLVLEGAGLRVSVPliAQGNSYPSE-TTVKYVFRLHE 629
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHP--AEGPPLPDElTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145309326 630 ATDYPWRPALTPfEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLASARP 678
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
558-688 |
2.71e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 142.79 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 558 YFIAPAKFLGKQVLSYGQNLSFSFRVDRRD---TRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTvKYVFRLHEATdyp 634
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPgggSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQ-TYSVRLHEEN--- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 635 WR----PALTPFEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLASARPGP-GVPATWVE 688
Cdd:pfam00052 77 WRdsdgAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGsGPPASWVE 136
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1040-1581 |
9.93e-18 |
|
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: 89.40 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1040 DKVADHRVKLQELESLIANLGTG-DEMVTdqAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQIS--- 1115
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNiEKMIL--AFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSlll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1116 --------RLQNIRNTIEET----GNLAEQARAHVENTERLIEIA---SRELEKAKVAAANVSVTQPESTGDPNNMT--- 1177
Cdd:pfam05483 247 iqitekenKMKDLTFLLEESrdkaNQLEEKTKLQDENLKELIEKKdhlTKELEDIKMSLQRSMSTQKALEEDLQIATkti 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1178 --LLAEEARKLAERHKQEADDIVRVakTANDTSTEAYNLLLRTlagenqtafEIEELNRKYEQAKNISQDLEKQAARVHE 1255
Cdd:pfam05483 327 cqLTEEKEAQMEELNKAKAAHSFVV--TEFEATTCSLEELLRT---------EQQRLEKNEDQLKIITMELQKKSSELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1256 EAKRAGDKAVEIyasvaqlspldsETLEneanniKMEAENlEQLIDQKlKDYEDLREDMRGKELEVKNLLEKGKTE---- 1331
Cdd:pfam05483 396 MTKFKNNKEVEL------------EELK------KILAED-EKLLDEK-KQFEKIAEELKGKEQELIFLLQAREKEihdl 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1332 --QQTA-------------------DQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRK 1390
Cdd:pfam05483 456 eiQLTAiktseehylkevedlktelEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1391 IPAINQTITEANEKTREAQQalgsaaadatEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ--- 1467
Cdd:pfam05483 536 IENLEEKEMNLRDELESVRE----------EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQien 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1468 -------LQEAEKELKRKqDDADQDMMMAGMASQAAQEAEINARKAKnsvtsLLSIINDLLEQLGQLDTVDLNKLNEIEG 1540
Cdd:pfam05483 606 knknieeLHQENKALKKK-GSAENKQLNAYEIKVNKLELELASAKQK-----FEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 145309326 1541 TLNKAKDEMKVsdldRKVSDLENEAKKQE-AAIMD-----YNRDIEE 1581
Cdd:pfam05483 680 AKAIADEAVKL----QKEIDKRCQHKIAEmVALMEkhkhqYDKIIEE 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1035-1572 |
1.35e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1035 YRLVKDKVADHRVKLQELESLIANLgtgdeMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQI 1114
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1115 SRLQNIRNTIEE-TGNLAEQARAHVENTERLIEIASRELE-KAKVAAANVSVTQpestgdpnnmtlLAEEARKLAERHKQ 1192
Cdd:COG1196 309 ERRRELEERLEElEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAE------------AEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1193 EADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKA---VEIYA 1269
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAeeeAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1270 SVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDY--EDLREDMRGKELEVKNLLEKgktEQQTADQLLARADAAKA 1347
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllLEAEADYEGFLEGVKAALLL---AGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1348 LAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTRE---AQQALGSAAADATEAKN 1424
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1425 KAH------EAERIASAVQKNATSTKAEAERTFAEVTDLDNEVN-----------NMLKQLQEAEKELKRKQDDADQDMM 1487
Cdd:COG1196 614 RYYvlgdtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSaggsltggsrrELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1488 MAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRkvSDLENEAKK 1567
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL--EELERELER 771
|
....*
gi 145309326 1568 QEAAI 1572
Cdd:COG1196 772 LEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1181-1597 |
7.04e-15 |
|
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: 80.49 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1181 EEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRA 1260
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1261 GDKAVEIYASVAQLSPLDSETLEneannikmEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKgkteqqtadqlla 1340
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEE------------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1341 radaakalaeeaakkGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALgsaaADAT 1420
Cdd:TIGR02168 819 ---------------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1421 EAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ----LQEAEKELKRKQDD-ADQDMMMAGMASQA 1495
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQERlSEEYSLTLEEAEAL 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1496 AQEAEINARKAKNSVTSLlsiiNDLLEQLGqldTVDLNKLNEIEgTLNKAKDEmkvsdLDRKVSDLeNEAKKQ-EAAIMD 1574
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRL----ENKIKELG---PVNLAAIEEYE-ELKERYDF-----LTAQKEDL-TEAKETlEEAIEE 1025
|
410 420
....*....|....*....|...
gi 145309326 1575 YNRDIEEIMKDIrnLEDIRKTLP 1597
Cdd:TIGR02168 1026 IDREARERFKDT--FDQVNENFQ 1046
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
935-980 |
1.74e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 1.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 935 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGFGPEGC 980
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
445-492 |
2.53e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.53 E-value: 2.53e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 445 CSCDPSGS-IDECNIETGRCVCKDNVEGFNCERCKPGFFNLESSNPRGC 492
Cdd:pfam00053 1 CDCNPHGSlSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1072-1594 |
2.64e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVnntlSSQISRLQNIRNTIEETGNLAEQARAHVE-------NTERL 1144
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKL----EKEVKELEELKEEIEELEKELESLEGSKRkleekirELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1145 IEIASRELEKAKVAAANVSVTQPEstgdpnnmtllAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQ 1224
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEK-----------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1225 TAfEIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVEIYASVAQLSP------LDS-----ETLENEANNIKMEA 1293
Cdd:PRK03918 337 EE-RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPeklekeLEElekakEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1294 ENLEQLIDQKLKDYEDLREDMR-----GKEL---EVKNLLEKGKTEQQTAdqllaradaakalaeeaakkgRDTLQEAND 1365
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGkcpvcGRELteeHRKELLEEYTAELKRI---------------------EKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1366 ILNNLKDFDRRVnDNKTAAEEALRKIPAINQTITEANEK------------TREAQQALGSAAADATEAKNKAHEAERIA 1433
Cdd:PRK03918 474 KERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKlkkynleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1434 SAVQKNAT--STKAEAERTFAEV-TDLDN-------EVNNMLKQLQE----------AEKELKRKQDDADQDMMMAGMAS 1493
Cdd:PRK03918 553 ELKKKLAEleKKLDELEEELAELlKELEElgfesveELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1494 QAAQEAEINARKAKNSVTSLLSIINDllEQLGQLDTVDLNKLNEIEG------TLNKAKDEMKvSDLDrkvsDLENEAKK 1567
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGlraeleELEKRREEIK-KTLE----KLKEELEE 705
|
570 580
....*....|....*....|....*..
gi 145309326 1568 QEAAIMDynrdIEEIMKDIRNLEDIRK 1594
Cdd:PRK03918 706 REKAKKE----LEKLEKALERVEELRE 728
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1051-1609 |
7.62e-14 |
|
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: 77.08 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1051 ELESLIANLGTGDEMVTDQaFEDRLK----EAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEE 1126
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQ-HQDRIEqlisEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1127 TgnlAEQARAHVENTERLIEIASRELEKaKVAAANVSVTQPESTGD-----------------------PNNMTLLAEEA 1183
Cdd:pfam15921 325 T---VSQLRSELREAKRMYEDKIEELEK-QLVLANSELTEARTERDqfsqesgnlddqlqklladlhkrEKELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1184 RKLAERHKQEADDIVRVAKTANDTSTEAYNL--LLRTLAGENQTAFE-----IEELNRKYEQAKNISQDLE--KQAAR-V 1253
Cdd:pfam15921 401 KRLWDRDTGNSITIDHLRRELDDRNMEVQRLeaLLKAMKSECQGQMErqmaaIQGKNESLEKVSSLTAQLEstKEMLRkV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1254 HEE--AKRAG----------------DKAVEIYASVAQLSPLDS---------ETLENEAN---NIKMEAENLEQLIDQK 1303
Cdd:pfam15921 481 VEEltAKKMTlessertvsdltaslqEKERAIEATNAEITKLRSrvdlklqelQHLKNEGDhlrNVQTECEALKLQMAEK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1304 LKDYEDLREDMRGKELEVKN--------LLEKGKTEQQTADQllaradaakalaeeaakkgRDTLQEANdILNNLKD--- 1372
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQhgrtagamQVEKAQLEKEINDR-------------------RLELQEFK-ILKDKKDaki 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1373 --FDRRVNDNK-------TAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAK----NKAHEAERIASAVQKN 1439
Cdd:pfam15921 621 reLEARVSDLElekvklvNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrNKSEEMETTTNKLKMQ 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1440 ATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKEL--KRKQDDADQDMMmagmasQAAQEAEINARKAKNsvtsLLSII 1517
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItaKRGQIDALQSKI------QFLEEAMTNANKEKH----FLKEE 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1518 NDLLEQlgQLDTVDLNKlNEIEGTLNKAKDEMKvsDLDRKVSDLE---NEAKKQEAAIMDY--NRDIEEIMKDIRNLEDI 1592
Cdd:pfam15921 771 KNKLSQ--ELSTVATEK-NKMAGELEVLRSQER--RLKEKVANMEvalDKASLQFAECQDIiqRQEQESVRLKLQHTLDV 845
|
650
....*....|....*..
gi 145309326 1593 RKTLPSGCFNTPSIeKP 1609
Cdd:pfam15921 846 KELQGPGYTSNSSM-KP 861
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1073-1590 |
8.75e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1073 DRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEiasrEL 1152
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----EL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1153 EKAKVAAANVSVtQPEStgdpnnmtlLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNllLRTLAGENQTAFEIEEL 1232
Cdd:PRK03918 234 EELKEEIEELEK-ELES---------LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1233 NRKYEQAKNisqDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDS--ETLENEANNIKMEAENLEQlIDQKLKDYEDL 1310
Cdd:PRK03918 302 YEEYLDELR---EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKklKELEKRLEELEERHELYEE-AKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1311 REDMRGKELE-VKNLLEKGKTEQQTAdqllaradaakalaeeaakkgRDTLQEANDILNNLKdfdRRVNDNKTAAEE--- 1386
Cdd:PRK03918 378 KKRLTGLTPEkLEKELEELEKAKEEI---------------------EEEISKITARIGELK---KEIKELKKAIEElkk 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1387 ALRKIPAINQTITEANEKT--REAQQALGSAAADATEAKNKAHEAERIASAVQKN-ATSTKAEAERTFAE-VTDLDNEVN 1462
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEqLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1463 NM-LKQLQEAEKE---LKRKQDDADQDmmMAGMASQAAQEAEINARKA-----KNSVTSLLSIINDLLEQLGQLDTVDLN 1533
Cdd:PRK03918 514 KYnLEELEKKAEEyekLKEKLIKLKGE--IKSLKKELEKLEELKKKLAelekkLDELEEELAELLKELEELGFESVEELE 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1534 -KLNEIEG------TLNKAKDEMKvsDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLE 1590
Cdd:PRK03918 592 eRLKELEPfyneylELKDAEKELE--REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
934-981 |
1.52e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.52e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 934 RCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGF--GPEGCK 981
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1058-1594 |
1.71e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1058 NLGTGDEMVTDQAFEDRLKEaeREVMDLlreaqDVKDVDQNLMDRLQRVNNTLSSQISRLQN---------IRNTIEETG 1128
Cdd:PTZ00121 1025 NIEKIEELTEYGNNDDVLKE--KDIIDE-----DIDGNHEGKAEAKAHVGQDEGLKPSYKDFdfdakednrADEATEEAF 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1129 NLAEQARAhvENTERLIEiaSRELEKAKVAAANVSVTQPESTgdpnnmtllAEEARKLAERHKQEADDIVRVAKTANDT- 1207
Cdd:PTZ00121 1098 GKAEEAKK--TETGKAEE--ARKAEEAKKKAEDARKAEEARK---------AEDARKAEEARKAEDAKRVEIARKAEDAr 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1208 -------STEAYNLLLRTLAGENQTAFEIE--ELNRKYEQAKNISQDLEKQAARVHEEAKRAGD-KAVEIYASVAQLSPL 1277
Cdd:PTZ00121 1165 kaeearkAEDAKKAEAARKAEEVRKAEELRkaEDARKAEAARKAEEERKAEEARKAEDAKKAEAvKKAEEAKKDAEEAKK 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1278 DSETLENEANNIKMEAENLEQLIDQKLKDYEDLR--EDMRGKElEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKK 1355
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAE-EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1356 GRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTiTEANEKTREAQQALGSAAADATEAKNKAHEAERIASA 1435
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1436 VQKNATST-KAEAERTFAEVTDLDNE----VNNMLKQLQEAEK--ELKRKQDDADQDMMMAGMASQA--AQEAEINARKA 1506
Cdd:PTZ00121 1403 DKKKADELkKAAAAKKKADEAKKKAEekkkADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1507 KNSvtsllsiindllEQLGQLDTVDLNKLNEiegtLNKAKDEMKVSDLDRKVSDLE--NEAKK-QEAAIMDYNRDIEEIM 1583
Cdd:PTZ00121 1483 KKA------------DEAKKKAEEAKKKADE----AKKAAEAKKKADEAKKAEEAKkaDEAKKaEEAKKADEAKKAEEKK 1546
|
570
....*....|...
gi 145309326 1584 K--DIRNLEDIRK 1594
Cdd:PTZ00121 1547 KadELKKAEELKK 1559
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1090-1596 |
5.26e-13 |
|
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: 73.99 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1090 QDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETgnlAEQARAHVENTERLIEIASRELEKAKVAAANVSVtqpes 1169
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAE---LKQKENKLQENRKIIEAQRKAIQELQFENEKVSL----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1170 tgdpnnmtllaeearKLaERHKQEADDIVRvaktANDTSTEAYNLLLRTLA--GENQTAFEIEElnrkyEQAKNISQDL- 1246
Cdd:pfam05483 135 ---------------KL-EEEIQENKDLIK----ENNATRHLCNLLKETCArsAEKTKKYEYER-----EETRQVYMDLn 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1247 ---EKQAARVHEEAKRAGDKAVEIYASVAQlsplDSETLENEANNIKMEAENLEQLI----------DQKLKDYEDLRED 1313
Cdd:pfam05483 190 nniEKMILAFEELRVQAENARLEMHFKLKE----DHEKIQHLEEEYKKEINDKEKQVsllliqitekENKMKDLTFLLEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1314 MRGKeleVKNLLEKGKTEQQTADQLLARadaakalaeeaakkgRDTL-QEANDILNNLKdfdRRVNDNKTAAEEALRKIP 1392
Cdd:pfam05483 266 SRDK---ANQLEEKTKLQDENLKELIEK---------------KDHLtKELEDIKMSLQ---RSMSTQKALEEDLQIATK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1393 AINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQ----KNATSTK---AEAERTFAEVTDLDNEVNNML 1465
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQqrleKNEDQLKiitMELQKKSSELEEMTKFKNNKE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1466 KQLQEAEKELKRKQDDADQDMMMAGMASQ------------AAQEAEINARKAKnsVTSLLSIINDLLEQLGQLDT-VDL 1532
Cdd:pfam05483 405 VELEELKKILAEDEKLLDEKKQFEKIAEElkgkeqelifllQAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTeLEK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1533 NKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1072-1591 |
8.83e-13 |
|
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: 73.52 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVM----DLLREAQDVKDVDQNLMDRLQRVNN------TLSSQISRLQN--------IRNTIEETGNLAEQ 1133
Cdd:TIGR04523 32 DTEEKQLEKKLKtiknELKNKEKELKNLDKNLNKDEEKINNsnnkikILEQQIKDLNDklkknkdkINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1134 ARAHVENTERL-IEIASRELEKAKVAAaNVSVTQPESTGDPNNMTLLAEEARKLaERHKQE--------ADDIVRVAKTA 1204
Cdd:TIGR04523 112 IKNDKEQKNKLeVELNKLEKQKKENKK-NIDKFLTEIKKKEKELEKLNNKYNDL-KKQKEElenelnllEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1205 NDTSTE--AYNLLLRTLAGENQtafEIEELNRKYEQAKNISQDLEKQaarVHEEAKRAGDKAVEIYASVAQLspldsETL 1282
Cdd:TIGR04523 190 DKIKNKllKLELLLSNLKKKIQ---KNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEISNTQTQL-----NQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1283 ENEANNIKMEAENLEQLIDQ---KLKDYEDlredmrgkelEVKNLlekgKTEQQTADQllaradaakalaeeaakkgrdt 1359
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQnnkKIKELEK----------QLNQL----KSEISDLNN---------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1360 lQEANDILNNLKDFDRRVNDNKTAAEEALRKIpaiNQTITEANEKTREAQQALGSAAAD----ATEAKNKAHEAERIASA 1435
Cdd:TIGR04523 303 -QKEQDWNKELKSELKNQEKKLEEIQNQISQN---NKIISQLNEQISQLKKELTNSESEnsekQRELEEKQNEIEKLKKE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1436 VQ------KNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEaEKELKRKQddadQDMMMAGMASQAAQEAEINARKA--K 1507
Cdd:TIGR04523 379 NQsykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ-EKELLEKE----IERLKETIIKNNSEIKDLTNQDSvkE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1508 NSVTSLLSIINDLLEQLGQLdtvdLNKLNEIEGTLNKAKDEMK------------VSDLDRKVSDLENEAKKQEAAIMDY 1575
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQKELKskekelkklneeKKELEEKVKDLTKKISSLKEKIEKL 529
|
570
....*....|....*.
gi 145309326 1576 NRDIEEIMKDIRNLED 1591
Cdd:TIGR04523 530 ESEKKEKESKISDLED 545
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
935-983 |
1.33e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.53 E-value: 1.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 935 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCEVNHFGFGPEGCKPC 983
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1596 |
1.85e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1035 YRLVKDKV--ADHRVKLQELESLIANLgtgdemvtdQAFEDRLKEAEREVMDLLREAQDV-KDVDQnLMDRLQRVNNTLS 1111
Cdd:TIGR02168 215 YKELKAELreLELALLVLRLEELREEL---------EELQEELKEAEEELEELTAELQELeEKLEE-LRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1112 SQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAK----VAAANVSVTQPESTGDPNNMTLLAEEARKLA 1187
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1188 ERhKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQT----AFEIEELNRKYEQAKNISQDLEKQAARVH--------E 1255
Cdd:TIGR02168 365 AE-LEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLKKLEEAElkelqaelE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1256 EAKRAGDKAVEIYASVAQLSPLDSETLEnEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLL---------- 1325
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLknqsglsgil 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1326 ----------------------------------------------EKGKTEQQTADQLLARADAAKALAEEAAKKGR-- 1357
Cdd:TIGR02168 523 gvlselisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnELGRVTFLPLDSIKGTEIQGNDREILKNIEGFlg 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1358 --------------------------DTLQEANDILNNLKDFDRRVND-----------NKTAAEEAL------RKIPAI 1394
Cdd:TIGR02168 603 vakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSsilerrREIEEL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1395 NQTITEANEKTREAQQALGSAAADATEAKN-------KAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ 1467
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1468 LQEAEKELKRKQDDADqdmmmAGMASQAAQEAEINarKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKD 1547
Cdd:TIGR02168 763 IEELEERLEEAEEELA-----EAEAEIEELEAQIE--QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 145309326 1548 EMK-VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:TIGR02168 836 TERrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-445 |
2.97e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 398 CHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPC 445
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1179-1484 |
3.48e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1179 LAEEARKlAERHK--QEADDIVRVAKTANdtsteAYNLLLRTLAGENQtafEIEELNRKYEQAK----NISQDLEKQAAR 1252
Cdd:COG1196 205 LERQAEK-AERYRelKEELKELEAELLLL-----KLRELEAELEELEA---ELEELEAELEELEaelaELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1253 VHEEAKRAGDKAVEIYASVAQLSPLDSET--LENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKT 1330
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1331 EQQTADQLLARAdaakalaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQ 1410
Cdd:COG1196 356 AEAELAEAEEAL--------------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1411 ALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEvnnmLKQLQEAEKELKRKQDDADQ 1484
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAA 491
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
444-493 |
5.97e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 5.97e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 444 PCSCDPSGSI-DECNIETGRCVCKDNVEGFNCERCKPGFFNLeSSNPRGCT 493
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
724-771 |
7.40e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 7.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 724 CACNGH---SETCDPETGVCNCRDNTAGPHCEKCSDGYYGDSTAGTssDCQ 771
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1075-1560 |
1.02e-11 |
|
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: 70.05 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1075 LKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQ-----ARAHVENTERLIEIAS 1149
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1150 RELEKA--KVAAANVSVTQPEST---GDPNNMTLlaeeARKLAERHKQeaddiVRVAKTANDT-STEAYNLllrtlagEN 1223
Cdd:TIGR04523 328 NQISQNnkIISQLNEQISQLKKEltnSESENSEK----QRELEEKQNE-----IEKLKKENQSyKQEIKNL-------ES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1224 QtafeIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVE-------------------IYASVAQLSPLDS----- 1279
Cdd:TIGR04523 392 Q----INDLESKIQNQEKLNQQKDEQI-KKLQQEKELLEKEIErlketiiknnseikdltnqDSVKELIIKNLDNtresl 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1280 ----ETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLAradaakalaeeaakk 1355
Cdd:TIGR04523 467 etqlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES--------------- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1356 grdtlqEANDILNNLKDFDRRVN-DNKTAAEEALRK-IPAINQTITEANE-------KTREAQQALGSAAADATEAKNKA 1426
Cdd:TIGR04523 532 ------EKKEKESKISDLEDELNkDDFELKKENLEKeIDEKNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIKEI 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1427 HEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDadqdmmmagmasqaaqEAEINaRKA 1506
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK----------------WPEII-KKI 668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309326 1507 KNSVTSLLSIIN---DLLEQLG---------QLDTVDLNKLNE----IEGTLNKAKDEMK-----VSDLDRKVSD 1560
Cdd:TIGR04523 669 KESKTKIDDIIElmkDWLKELSlhykkyitrMIRIKDLPKLEEkykeIEKELKKLDEFSKeleniIKNFNKKFDD 743
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
445-492 |
2.30e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 445 CSCDPSGSIDE-CNIETGRCVCKDNVEGFNCERCKPGFFNlesSNPRGC 492
Cdd:smart00180 1 CDCDPGGSASGtCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-442 |
2.35e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 398 CHCSPVGSLSTQCDS-YGRCSCKPGVMGDKCDRCQPGFHSLTEAGC 442
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
724-763 |
2.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 2.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 145309326 724 CACNGH---SETCDPETGVCNCRDNTAGPHCEKCSDGYYGDST 763
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
883-933 |
4.30e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 4.30e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 883 ACNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNLQS-GQGCE 933
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-443 |
5.18e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 5.18e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 397 SCHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEA--GCR 443
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1039-1596 |
7.03e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1039 KDKVADHRVKLQELESLIANLGTGDEMVTD-----QAFEDRLKEAEREVMDLLREAQDVKDV-------DQNLMDRLQRV 1106
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAEtererEELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1107 NNTLSSQISRLQNIRNTIEETGNLAEQARahvENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKL 1186
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLR---EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1187 AERHKQEADDIVRVaktandtstEAYNLLLRtlagenqtafeiEELNRKYEQAKNISQDLEKQAARVHE-EAKRAGDKAV 1265
Cdd:PRK02224 397 RERFGDAPVDLGNA---------EDFLEELR------------EERDELREREAELEATLRTARERVEEaEALLEAGKCP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1266 EIYASVAQlSPlDSETLENEannikmeaenleqliDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADqllaradaa 1345
Cdd:PRK02224 456 ECGQPVEG-SP-HVETIEED---------------RERVEELEAELEDLEEEVEEVEERLERAEDLVEAED--------- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1346 kalaeeaakkgrdtlqEANDILNNLKDFDRRVNDNKTAAEEAlrkipainqtiTEANEKTREAQQALGSAAADATEAKNK 1425
Cdd:PRK02224 510 ----------------RIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1426 AHE-----AERIASAVQKNATsTKAEAER------TFAEVTDLDNEV---NNMLKQLQE---------AEKELKRKQDDA 1482
Cdd:PRK02224 563 AEEeaeeaREEVAELNSKLAE-LKERIESlerirtLLAAIADAEDEIerlREKREALAElnderrerlAEKRERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1483 DQDmmmaGMASQAAQEAEINARKAKNSVTSLLSII----NDLLEQLGQLDtvdlnklNEIEgTLNKAKDEMKvsDLDRKV 1558
Cdd:PRK02224 642 EFD----EARIEEAREDKERAEEYLEQVEEKLDELreerDDLQAEIGAVE-------NELE-ELEELRERRE--ALENRV 707
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 145309326 1559 SDLE---NEAKKQEAAIMDYNRDIEEimkdiRNLEDIRKTL 1596
Cdd:PRK02224 708 EALEalyDEAEELESMYGDLRAELRQ-----RNVETLERML 743
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
982-1029 |
1.10e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 1.10e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 982 PCDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYFYNRSWP-GCQ 1029
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
884-932 |
1.13e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.13e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 884 CNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNLQ--SGQGC 932
Cdd:pfam00053 1 CDCNPHGS--LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1046-1532 |
1.14e-10 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 66.08 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1046 RVKLQELESLIAN--------LGTGDEmvtdqAFEDRLKEAEREVmdllreaqdvkdvdQNLMDRLQRVNNTLSSQISRL 1117
Cdd:COG5278 49 LRALEELLSALLDaetgqrgyLLTGDE-----SFLEPYEEARAEI--------------DELLAELRSLTADNPEQQARL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1118 QNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDI 1197
Cdd:COG5278 110 DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1198 VRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPL 1277
Cdd:COG5278 190 ELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1278 DSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGR 1357
Cdd:COG5278 270 LAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1358 DTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQ 1437
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1438 KNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLSII 1517
Cdd:COG5278 430 EALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALL 509
|
490
....*....|....*
gi 145309326 1518 NDLLEQLGQLDTVDL 1532
Cdd:COG5278 510 LAAAEAALAAALAAA 524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1524 |
1.52e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1036 RLVKDKVADHRVKLQELESLianlgtgdemvtdqafEDRLKEAEREVMDLLREAQDVKDVDQNLMD--RLQRVNNTLSSQ 1113
Cdd:COG4717 81 KEAEEKEEEYAELQEELEEL----------------EEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1114 ISRLQNIRNTIEETgnlaEQARAHVENTERLIEIASRELEKAKvaaanvsvtQPESTGDPNNMTLLAEEARKLAERhKQE 1193
Cdd:COG4717 145 PERLEELEERLEEL----RELEEELEELEAELAELQEELEELL---------EQLSLATEEELQDLAEELEELQQR-LAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1194 ADDIVRVAKTANDTSTEAYNLLLRTLagenqtafEIEELNRKYEQAKNISQDLekqAARVHEEAKRAGDKAVEIY----- 1268
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1269 ASVAQLSPLDSETLENEANNIKMEAENL------EQLIDQKLKDYedLREDMRGKELEVKNLLEKGKTEQQTADQLLAra 1342
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELqalpalEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLRE-- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1343 daakalaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGsaaadatea 1422
Cdd:COG4717 356 --------------AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE--------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1423 knkAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEIN 1502
Cdd:COG4717 413 ---ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
490 500
....*....|....*....|..
gi 145309326 1503 ARKAKNSVtsLLSIINDLLEQL 1524
Cdd:COG4717 490 EEWAALKL--ALELLEEAREEY 509
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
724-765 |
1.94e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 1.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 145309326 724 CACNG---HSETCDPETGVCNCRDNTAGPHCEKCSDGYYGDSTAG 765
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
884-932 |
2.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 884 CNCNLYGTmkQQSSCNPVTGQCECLPHVTGQDCGACDPGFYNlQSGQGC 932
Cdd:smart00180 1 CDCDPGGS--ASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
983-1028 |
2.50e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.50e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 145309326 983 CDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYfYNRSWPGC 1028
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1073-1596 |
3.21e-10 |
|
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: 65.47 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1073 DRLKEAEREvmdllreaqDVKDVDQNlMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARaHVENTERL--IEIASR 1150
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEEN-IERLDLIIDEKRQQLERLRREREKAERYQALLKEKR-EYEGYELLkeKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1151 ELEK--AKVAAANVSVTQPESTGDPNNMTL--LAEEARKLAERHKQEADD-IVRVAKTANDTSTE---------AYNLLL 1216
Cdd:TIGR02169 238 QKEAieRQLASLEEELEKLTEEISELEKRLeeIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEiaslersiaEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1217 RTLAGENQTAFeiEELNRKYEQAKNISQDLEKQAAR---VHEEAK-----------RAGDKAVEIYASVAQLSPLDS--E 1280
Cdd:TIGR02169 318 EDAEERLAKLE--AEIDKLLAEIEELEREIEEERKRrdkLTEEYAelkeeledlraELEEVDKEFAETRDELKDYREklE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1281 TLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTL 1360
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1361 QEANDILNNLKDFDR--------------RVNDNKtAAEEALRK-IPAINQTITEANEKTREAQQALGSAA--------- 1416
Cdd:TIGR02169 476 EEYDRVEKELSKLQRelaeaeaqaraseeRVRGGR-AVEEVLKAsIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvv 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1417 ---ADATEAKN--KAHEA-------------------------------------ERIASAV------------------ 1436
Cdd:TIGR02169 555 eddAVAKEAIEllKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdPKYEPAFkyvfgdtlvvedieaarr 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1437 -------------------------------QKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQD 1485
Cdd:TIGR02169 635 lmgkyrmvtlegelfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1486 MMMAGMAS----QAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDlNKLNEIEGTLNKAKDEM----------KV 1551
Cdd:TIGR02169 715 SRKIGEIEkeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALndlearlshsRI 793
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 145309326 1552 SDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1415-1590 |
4.02e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.70 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1415 AAADATEAKNKAHeAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmaGMASQ 1494
Cdd:COG3883 1 ALALALAAPTPAF-ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----LQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1495 AAQEAEINARKAK-----------NSVTSLLSII------NDLLEQLGQLDTV-------------DLNKLNEIEGTLNK 1544
Cdd:COG3883 75 AEAEAEIEERREElgeraralyrsGGSVSYLDVLlgsesfSDFLDRLSALSKIadadadlleelkaDKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145309326 1545 AKDEM--KVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLE 1590
Cdd:COG3883 155 KLAELeaLKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1041-1596 |
4.35e-10 |
|
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: 64.70 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1041 KVADHRVKLQELESLIANLgtgDEMVTDQAfeDRLKEAEREVMDLlreAQDVKDVDQNLMDR---LQRVNNTLSS---QI 1114
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINEL---EEEKEDKA--LEIKKQEWKLEQL---AADLSKYEQELYDLkeeYDRVEKELSKlqrEL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1115 SRLQNIRNTIEETGN-------LAEQARAHVENTER-LIEIASR---ELEKAKVAAANVSVTQPESTgdpnnmtllAEEA 1183
Cdd:TIGR02169 493 AEAEAQARASEERVRggraveeVLKASIQGVHGTVAqLGSVGERyatAIEVAAGNRLNNVVVEDDAV---------AKEA 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1184 RKLAERHKQEADDIVRVAKTAndtsteAYNLLLRTLAGENQTAFEIE--ELNRKYEQA-KNISQD--------------- 1245
Cdd:TIGR02169 564 IELLKRRKAGRATFLPLNKMR------DERRDLSILSEDGVIGFAVDlvEFDPKYEPAfKYVFGDtlvvedieaarrlmg 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1246 -----------LEKQAARV--HEEAKRAGDKAVEIYASVAQLSPlDSETLENEANNIKMEAENLEQLIDQKLKDYEDLRE 1312
Cdd:TIGR02169 638 kyrmvtlegelFEKSGAMTggSRAPRGGILFSRSEPAELQRLRE-RLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1313 DMRGKELE----------VKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRvndnkT 1382
Cdd:TIGR02169 717 KIGEIEKEieqleqeeekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----S 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1383 AAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVN 1462
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1463 NM---LKQLQEAEKELKRKQDDADQDMmmaGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIE 1539
Cdd:TIGR02169 872 ELeaaLRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1540 GTLNKAKDEMKVSDLDRKVSDLENEAKKqeaAIMDYnrdiEEIMKDIRNLEDIRKTL 1596
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNML---AIQEY----EEVLKRLDELKEKRAKL 998
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1044-1574 |
4.35e-10 |
|
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: 64.74 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1044 DHRVKlqELESLIANLGTgdEMVTDQAFEDRLKEAEREVMDLL--REAQdvkdvdqnlMDRLQRVNNTLSSQISRLQNIR 1121
Cdd:pfam05483 292 DHLTK--ELEDIKMSLQR--SMSTQKALEEDLQIATKTICQLTeeKEAQ---------MEELNKAKAAHSFVVTEFEATT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1122 NTIEETGNlAEQARahVENTERLIEIASRELEKAkvaaanvSVTQPESTGDPNNMTLLAEEARK-LAERHK--QEADDIV 1198
Cdd:pfam05483 359 CSLEELLR-TEQQR--LEKNEDQLKIITMELQKK-------SSELEEMTKFKNNKEVELEELKKiLAEDEKllDEKKQFE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1199 RVAKTANDTSTEAYNLLlrtlagenQT-AFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSpL 1277
Cdd:pfam05483 429 KIAEELKGKEQELIFLL--------QArEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL-L 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1278 DSETLENEANNIKME---------------------AENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTAD 1336
Cdd:pfam05483 500 ENKELTQEASDMTLElkkhqediinckkqeermlkqIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1337 QLLARADAAkalaeeaakkgrdtLQEANDILNNLKdfdRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAA 1416
Cdd:pfam05483 580 YEVLKKEKQ--------------MKILENKCNNLK---KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1417 ADATEAKNKAHEaerIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDadqdmMMAGMASQAA 1496
Cdd:pfam05483 643 LELASAKQKFEE---IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE-----MVALMEKHKH 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1497 Q--------EAEINARKAKNSVTSLLSIindlleqlgQLDTvdlnKLNEIEGTLNKAKDEMKVSDLDRKvsDLENEAKKQ 1568
Cdd:pfam05483 715 QydkiieerDSELGLYKNKEQEQSSAKA---------ALEI----ELSNIKAELLSLKKQLEIEKEEKE--KLKMEAKEN 779
|
....*.
gi 145309326 1569 EAAIMD 1574
Cdd:pfam05483 780 TAILKD 785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1074-1445 |
5.87e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1074 RLKEAEREvmdlLREAQDvkdvdqNLmDRLQRVNNTLSSQISRLQnirntieetgnlaEQARAhvenTERLIEIaSRELE 1153
Cdd:TIGR02168 173 RRKETERK----LERTRE------NL-DRLEDILNELERQLKSLE-------------RQAEK----AERYKEL-KAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1154 KAKVAAANVSVTQPESTGDPNNmtllaEEARKLAERHKQEADDIvrvaktanDTSTEAYNLLlRTLAGENQTafEIEELN 1233
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQ-----EELKEAEEELEELTAEL--------QELEEKLEEL-RLEVSELEE--EIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1234 RKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL------SPLDSETLENEANNIKMEAENLEQLID------ 1301
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEEKLEELKEELESLEAELEeleael 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1302 ----QKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEAndilnNLKDFDRRV 1377
Cdd:TIGR02168 368 eeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAEL 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1378 NDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKA 1445
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1038-1588 |
8.39e-10 |
|
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: 63.98 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1038 VKDKVADHRVKLQELESlianlgTGDEMVTDQAFEDRLKEAER-EVMDLLREAQDVKDVDQNLMD----RLQRVNNTLSS 1112
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQM------ERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCLKEDMLEdsntQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1113 QISRLQNIRNTI----EETGN-LAEQ---ARAHVENTERLIEIASRELE------KAKV--AAANVSVTQPESTgdpNNM 1176
Cdd:pfam15921 182 HEGVLQEIRSILvdfeEASGKkIYEHdsmSTMHFRSLGSAISKILRELDteisylKGRIfpVEDQLEALKSESQ---NKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1177 TLLAEEAR----KLAERHKQEADDIVRVAKTAndtsteaynlllRTLAGENQTAFEIEElnrkyEQAKNIS-------QD 1245
Cdd:pfam15921 259 ELLLQQHQdrieQLISEHEVEITGLTEKASSA------------RSQANSIQSQLEIIQ-----EQARNQNsmymrqlSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1246 LEKQAARVH---EEAKRAGDKAVEIYASvaQLSPLDSETLE--NEANNIKMEAENLEqliDQKLKDYEDLREdmRGKELE 1320
Cdd:pfam15921 322 LESTVSQLRselREAKRMYEDKIEELEK--QLVLANSELTEarTERDQFSQESGNLD---DQLQKLLADLHK--REKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1321 V-----KNLLEKGKTEQQTADQLLARADAAKALaeeaakkgrdtLQEANDILNNLKDFDRRVNDNKTAA----EEALRKI 1391
Cdd:pfam15921 395 LekeqnKRLWDRDTGNSITIDHLRRELDDRNME-----------VQRLEALLKAMKSECQGQMERQMAAiqgkNESLEKV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1392 PAINQTITEANEKTREAQQALgsaaadaTEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEA 1471
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1472 EKE---LKRKQDDADQ-DMMMAGmasqAAQEAEINARKAKNsVTSLLS----IINDLLEQLGQLDT-VDLNKLNEIEGTL 1542
Cdd:pfam15921 537 KNEgdhLRNVQTECEAlKLQMAE----KDKVIEILRQQIEN-MTQLVGqhgrTAGAMQVEKAQLEKeINDRRLELQEFKI 611
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1543 NKAKDEMKVSDLDRKVSDLE-------NEAKKQEAAIMDYNRDIEEIMKDIRN 1588
Cdd:pfam15921 612 LKDKKDAKIRELEARVSDLElekvklvNAGSERLRAVKDIKQERDQLLNEVKT 664
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1414-1596 |
1.06e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1414 SAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMAS 1493
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1494 QAAQEAEINArkakNSVTSLLSI--INDLLEQLGQLDTV---DLNKLNEIEGTLNKAKDemKVSDLDRKVSDLENEAKKQ 1568
Cdd:COG3883 93 RALYRSGGSV----SYLDVLLGSesFSDFLDRLSALSKIadaDADLLEELKADKAELEA--KKAELEAKLAELEALKAEL 166
|
170 180
....*....|....*....|....*...
gi 145309326 1569 EAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1357-1596 |
3.15e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.69 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAV 1436
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1437 QKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLSI 1516
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1517 INDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIE-EIMKDIRNLEDIRKT 1595
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELElAILVEKDTEEEELEI 280
|
.
gi 145309326 1596 L 1596
Cdd:COG4372 281 A 281
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1046-1435 |
4.33e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1046 RVKLQELESLIANLGTGdemVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIE 1125
Cdd:COG4372 7 KVGKARLSLFGLRPKTG---ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1126 ETGNLAEQARAHVENTERLIEIASRELEKAKVAAANvsvtqpestgdpnnmtlLAEEARKLAERHKQEADDIVRVAKTAN 1205
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-----------------LQKERQDLEQQRKQLEAQIAELQSEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1206 DTSTEaynllLRTLAGE-NQTAFEIEELNRKYEQAKNisQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLEN 1284
Cdd:COG4372 147 EREEE-----LKELEEQlESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1285 EANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEAN 1364
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309326 1365 DILNnlKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASA 1435
Cdd:COG4372 300 LLLN--LAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
983-1029 |
6.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 6.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 145309326 983 CDCHPEGSLSLQC-KDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQ 1029
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1048-1460 |
7.23e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 60.31 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1048 KLQELESLIANLGTGDemvTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEET 1127
Cdd:COG5278 119 WLAELEQVIALRRAGG---LEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1128 GNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDT 1207
Cdd:COG5278 196 LARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1208 STEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEAN 1287
Cdd:COG5278 276 ALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1288 NIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDIL 1367
Cdd:COG5278 356 AAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1368 NNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEA 1447
Cdd:COG5278 436 EEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEA 515
|
410
....*....|...
gi 145309326 1448 ERTFAEVTDLDNE 1460
Cdd:COG5278 516 ALAAALAAALASA 528
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1063-1506 |
8.42e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1063 DEMVTDQafEDRLKEAEREVMDLLRE-----AQDVKDVDQNLMDRLQRVNNTLSSqisRLQNIRNTIEETGNLAEQARAH 1137
Cdd:NF041483 86 DQLRADA--ERELRDARAQTQRILQEhaehqARLQAELHTEAVQRRQQLDQELAE---RRQTVESHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1138 VEN-TERLIEIASRELEKAkVAAANVSVTQpestgdpnnmtlLAEEARKL----AERHKQEADDIVRVAKT--------- 1203
Cdd:NF041483 161 TESqARRLLDESRAEAEQA-LAAARAEAER------------LAEEARQRlgseAESARAEAEAILRRARKdaerllnaa 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1204 ---ANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQ----AKNISQDLEKQAARVHEEAKRAGDKAVEIYASV----- 1271
Cdd:NF041483 228 stqAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQrmqeAEEALREARAEAEKVVAEAKEAAAKQLASAESAneqrt 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1272 ----AQLSPLDSE-TLENEAnnIKMEAEnleqlidQKLKDYEDLREDMrgkeleVKNLLEKGKT--EQQTADQLLARADA 1344
Cdd:NF041483 308 rtakEEIARLVGEaTKEAEA--LKAEAE-------QALADARAEAEKL------VAEAAEKARTvaAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1345 AKALAEEAAKKGRDTLQ----------------------EANDILNNLKDF---DRRVNDNKTA--AEEALR-------- 1389
Cdd:NF041483 373 AEEVLTKASEDAKATTRaaaeeaerirreaeaeadrlrgEAADQAEQLKGAakdDTKEYRAKTVelQEEARRlrgeaeql 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1390 ---------KI--PAINQTITEANEKTREAQQALGSAAADATEAKNKAH-EAERIASAVQKNATS-----------TKAE 1446
Cdd:NF041483 453 raeavaegeRIrgEARREAVQQIEEAARTAEELLTKAKADADELRSTATaESERVRTEAIERATTlrrqaeetlerTRAE 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1447 AERTFAEVTDLDNEV----NNMLKQLQ------------EAEKELKRKQDDADQDMMMAGMA-SQAAQEAEINARKA 1506
Cdd:NF041483 533 AERLRAEAEEQAEEVraaaERAARELReeteraiaarqaEAAEELTRLHTEAEERLTAAEEAlADARAEAERIRREA 609
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1357-1598 |
1.00e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEANDILNNLKDFDRRVNDNKTAAE--EALRKIPAINQTITEAnEKTREAQQALGSAAAdateaknkAHEAERIAS 1434
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAA-RERLAELEYLRAALR--------LWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1435 AVQKNATSTKAEAERTFAEVTDLDNEvnnmLKQLQEAEKELKRKQDDADQDmmmagmasQAAQ-EAEI-NARKAKNSVTS 1512
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEAR----LDALREELDELEAQIRGNGGD--------RLEQlEREIeRLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1513 LLSIINDLLEQLGQldtvdlnKLNEIEGTLNKAKDEMK--VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLE 1590
Cdd:COG4913 360 RRARLEALLAALGL-------PLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
....*...
gi 145309326 1591 DIRKTLPS 1598
Cdd:COG4913 433 RRKSNIPA 440
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1061-1609 |
1.45e-08 |
|
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: 59.75 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1061 TGDEMVTD---QAFEDRLKEAERevMDLLREAqdVKDVDQNLMDR----LQRVNNTLSSQISRLQNIRNTIEETGNLAEQ 1133
Cdd:pfam15921 408 TGNSITIDhlrRELDDRNMEVQR--LEALLKA--MKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1134 ARAH---VENTERLIE--IASRELEKAKVAAANVSVTQPESTGDPNNMTL--LAEEARKLaeRHKQEADDIVRVAKTAND 1206
Cdd:pfam15921 484 LTAKkmtLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELqhLKNEGDHL--RNVQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1207 TSTEAYNLLLRTLA------GENQTAFEIE------ELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVE----IYAS 1270
Cdd:pfam15921 562 KVIEILRQQIENMTqlvgqhGRTAGAMQVEkaqlekEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAG 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1271 VAQLSPL-----DSETLENEANNIKMEAENLEQlidqklkDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARAdaa 1345
Cdd:pfam15921 642 SERLRAVkdikqERDQLLNEVKTSRNELNSLSE-------DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT--- 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1346 kalaeeaakkgRDTLQ--EAND--ILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKT---REAQQALGSAAAD 1418
Cdd:pfam15921 712 -----------RNTLKsmEGSDghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflKEEKNKLSQELST 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1419 ATEAKNK-AHEAERIASAVQK------NATSTKAEAERTFAEVTDLdnevnnmlKQLQEAEKELKRKQDDAD-QDMMMAG 1490
Cdd:pfam15921 781 VATEKNKmAGELEVLRSQERRlkekvaNMEVALDKASLQFAECQDI--------IQRQEQESVRLKLQHTLDvKELQGPG 852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1491 MASQAAQEAEI-----NARKAKN-----SVTSLLSIINDLLEQLGQLDTVDLNKL-NEIEGTLNKAKDEM--KVSD---- 1553
Cdd:pfam15921 853 YTSNSSMKPRLlqpasFTRTHSNvpssqSTASFLSHHSRKTNALKEDPTRDLKQLlQELRSVINEEPTVQlsKAEDkgra 932
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1554 -----LDRKVSD--LENEAK-----------KQEAAIMDYNRDIEEIMKDIRNLEDirktlPSGCFNTPSIEKP 1609
Cdd:pfam15921 933 pslgaLDDRVRDciIESSLRsdichsssnslQTEGSKSSETCSREPVLLHAGELED-----PSSCFTFPSTASP 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1086-1479 |
1.53e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1086 LREAQDVKDVDQNLMdRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVT 1165
Cdd:COG1196 218 LKEELKELEAELLLL-KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1166 QPESTGDpnnMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLrtlagenqtafEIEELNRKYEQAKNISQD 1245
Cdd:COG1196 297 LARLEQD---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-----------ELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1246 LEKQAARVHEEAKRAGDKAVEIYASVAQlspldsetLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLL 1325
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLE--------ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1326 EKGKTEQQTAdqllaradaakalaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEAN--E 1403
Cdd:COG1196 435 EEEEEEEEAL---------------------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarL 493
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1404 KTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKA-EAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQ 1479
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1229-1567 |
1.71e-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: 59.69 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1229 IEELNRKYEQaknisqdLEKQAarvhEEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQlidqklkDYE 1308
Cdd:TIGR02168 195 LNELERQLKS-------LERQA----EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEE-------ELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1309 DLREDMRGKELEVKNL-LEKGKTEQQTADQllaradaakalaeeaakkgRDTLQEANDILNNL-------KDFDRRVNDN 1380
Cdd:TIGR02168 257 ELTAELQELEEKLEELrLEVSELEEEIEEL-------------------QKELYALANEISRLeqqkqilRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1381 KTAAEEALRKIPA-INQTITEANEKTREAQQALG---SAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTD 1456
Cdd:TIGR02168 318 LEELEAQLEELESkLDELAEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1457 LDNEVNNMLKQLQEAEKELKRKQD---DADQDMMMAGMASQAAQEAEIN-----ARKAKNSVTSLLSIINDLLEQLGQLD 1528
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQeieELLKKLEEAELKELQAELEELEeeleeLQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 145309326 1529 TVDLNKLNEIEGTLNKAKDEM-KVSDLDRKVSDLENEAKK 1567
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQeNLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1259-1581 |
2.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1259 RAGDKAVEIyasVAQLSPL--DSETLEnEANNIKMEAENLE-QLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTA 1335
Cdd:COG1196 190 RLEDILGEL---ERQLEPLerQAEKAE-RYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1336 DQllaradaakalaeeaakkgrdTLQEANDILNNLkdfDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSA 1415
Cdd:COG1196 266 EA---------------------ELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1416 AADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQA 1495
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1496 AQEAEINARKAKNSVTSLLSIINDLLEQLGQLDT-VDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMD 1574
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEeEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
....*..
gi 145309326 1575 YNRDIEE 1581
Cdd:COG1196 482 LLEELAE 488
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
828-875 |
2.24e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 145309326 828 CQCSDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNPLAP 875
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1037-1588 |
2.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1037 LVKDKVADHRVKLQELESLIANLGTGDEMvtdqafEDRLKEAEREVMDL--LRE-AQDVKDVDQNLmDRLQRVNNTLSSQ 1113
Cdd:COG4913 212 FVREYMLEEPDTFEAADALVEHFDDLERA------HEALEDAREQIELLepIRElAERYAAARERL-AELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1114 IS--RLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQpestgdpnnmtllAEEARKLAERHK 1191
Cdd:COG4913 285 FAqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1192 QEADDIVRVAktandtstEAYNLLLRTLagENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAgdkAVEIYASV 1271
Cdd:COG4913 352 RELEERERRR--------ARLEALLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA---EAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1272 AQLSPLDSE--TLENEANNIKMEAENLEQLIDQKLKDYEDlreDMR--GKELEVK-------------------NLLEKG 1328
Cdd:COG4913 419 RELRELEAEiaSLERRKSNIPARLLALRDALAEALGLDEA---ELPfvGELIEVRpeeerwrgaiervlggfalTLLVPP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1329 KTEQQTA---DQLLARAD------AAKALAEEAAKKGRDTL------------QEANDILNN------------LKDFDR 1375
Cdd:COG4913 496 EHYAAALrwvNRLHLRGRlvyervRTGLPDPERPRLDPDSLagkldfkphpfrAWLEAELGRrfdyvcvdspeeLRRHPR 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1376 RV---------------NDNKTAAEE------ALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIA- 1433
Cdd:COG4913 576 AItragqvkgngtrhekDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAe 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1434 -SAVQKNATSTKAEAERTFAEVTDLDNEvNNMLKQLQEAEKELKRKQDDADQDMmmagmasQAAQEAEINARKAKNSVTS 1512
Cdd:COG4913 656 ySWDEIDVASAEREIAELEAELERLDAS-SDDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309326 1513 LLSIINDLLEQLGQLDTVDLNKlnEIEGTLNKAKDEMKVSDLDRkvsDLENEAKKQEAAIMDYNRDIEEIMKDIRN 1588
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRA--LLEERFAAALGDAVERELRE---NLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1287-1530 |
2.88e-08 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 56.65 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1287 NNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARadaakalaeeaakkGRDTLQEANDI 1366
Cdd:pfam06008 15 YKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAK--------------AQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1367 LNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSA----------AADATEAKNKAHEAERIASAV 1436
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRmlgeirsrdfGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1437 QKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDAdQDMMmagMASQAAQEaEINARK-----AKNSVT 1511
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDA-NRLN---LANQANLR-EFQRKKeevseQKNQLE 235
|
250 260
....*....|....*....|...
gi 145309326 1512 SLLSIINDLLEQ----LGQLDTV 1530
Cdd:pfam06008 236 ETLKTARDSLDAanllLQEIDDA 258
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1049-1484 |
3.17e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 58.38 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1049 LQELESLIANLGTGDEMVTD--QAFEDRLKEAEReVMDLLRE-------AQDVKDVDQNLMDRLQrvnntlssqiSRLQN 1119
Cdd:COG5278 92 LAELRSLTADNPEQQARLDEleALIDQWLAELEQ-VIALRRAggleaalALVRSGEGKALMDEIR----------ARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1120 IRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVR 1199
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1200 VAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDS 1279
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1280 ETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDT 1359
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1360 LQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKN 1439
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 145309326 1440 ATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQ 1484
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1029-1337 |
3.30e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1029 QECPACYRLVKDKVADHRVKLQELESLIANLGTGDEmVTDQAFEDRLKEAEREVMDLLREAQDvkdvdqnLMDRLQRVNN 1108
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEE-------LQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1109 TLSSQISRLQNIRNTIEETGN--LAEQARAHVENTERLIEIAS--------------RELEKAKVAAANVSVTQPESTGD 1172
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENelEAAALEERLKEARLLLLIAAallallglggsllsLILTIAGVLFLVLGLLALLFLLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1173 PNNMTLLAEEARKLAERHKQEA------DDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQA---KNIS 1243
Cdd:COG4717 294 AREKASLGKEAEELQALPALEEleeeelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleQEIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1244 QDLEK----------QAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLEN-EANNIKMEAENLEQLIDQKLKDYEDLRE 1312
Cdd:COG4717 374 ALLAEagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELRE 453
|
330 340
....*....|....*....|....*
gi 145309326 1313 DMRGKELEVKNLLEKGKTEQQTADQ 1337
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQEL 478
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1091-1302 |
3.34e-08 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 56.53 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1091 DVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPEST 1170
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1171 G-----------------------DPNNMTLL-------------------AEEARKLAERHKQEADDIVRVAKTANDTS 1208
Cdd:smart00283 81 SaveeleessdeigeivsviddiaDQTNLLALnaaieaarageagrgfavvADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1209 TEAYNLLLRT---------LAGENQTAFE-----IEELNrkyEQAKNISQDLEKQAARVHEEAkragdKAVEIYASVAQL 1274
Cdd:smart00283 161 NEAVAAMEESsseveegveLVEETGDALEeivdsVEEIA---DLVQEIAAATDEQAAGSEEVN-----AAIDEIAQVTQE 232
|
250 260
....*....|....*....|....*...
gi 145309326 1275 SPLDSETLENEANNIKMEAENLEQLIDQ 1302
Cdd:smart00283 233 TAAMSEEISAAAEELSGLAEELDELVER 260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1036-1477 |
4.14e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1036 RLVKDKVADHRVKLQELESLIANLGTgdemvTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQIS 1115
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEE-----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1116 RLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANvsvtqpestgdpnnmtlLAEEARKLAERHKQEAD 1195
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-----------------LEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1196 DIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQ-AKNISQDLEKQAARVHEEAKRAGDK----------- 1263
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElAEAAARLLLLLEAEADYEGFLEGVKaalllaglrgl 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1264 ----AVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLID------------------------QKLKDYEDLREDMR 1315
Cdd:COG1196 523 agavAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEylkaakagratflpldkiraraalAAALARGAIGAAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1316 GKELEVKNLLEKGKTEQQT---ADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIP 1392
Cdd:COG1196 603 LVASDLREADARYYVLGDTllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1393 AINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNE-----------V 1461
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpeppdL 762
|
490
....*....|....*.
gi 145309326 1462 NNMLKQLQEAEKELKR 1477
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1394-1566 |
5.72e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.22 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1394 INQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIAS--------AVQKN----AT-------STKAEAERTFAEV 1454
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGredlARealerkaELEAQAEALEAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1455 TDLDNEVNNMLKQLQEAEKELKRKQddADQDMMMAGMASQAAQEAeinarkaknsvtsllsiINDLLEQLGQLDTVDL-- 1532
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELK--AKKDTLKARAKAAKAQEK-----------------VNEALSGIDSDDATSAle 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 145309326 1533 ---NKLNEIEGTLNkAKDEMKV-SDLDRKVSDLENEAK 1566
Cdd:COG1842 169 rmeEKIEEMEARAE-AAAELAAgDSLDDELAELEADSE 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1429-1591 |
7.18e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1429 AERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmagMASQAAQ-EAEINARKAK 1507
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ------AREELEQlEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1508 -NSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEmkVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDI 1586
Cdd:COG4372 75 lEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE--LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
....*
gi 145309326 1587 RNLED 1591
Cdd:COG4372 153 KELEE 157
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1094-1337 |
8.38e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1094 DVDQNLMDRLQRVNNTLSSQISRLQNIRNT-IEETGNLAEQARAHVENTERLIEIAsRELeKAKVAAANVSVTQpestgd 1172
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEA-QEL-REKRDELNEKVKE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1173 pnnmtlLAEEARKLAER---HKQEADDIVRVAKTANDTST------EAYNLLLR-------TLAGENQTAFEIEELNRKY 1236
Cdd:COG1340 76 ------LKEERDELNEKlneLREELDELRKELAELNKAGGsidklrKEIERLEWrqqtevlSPEEEKELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1237 EQAKNI-------------SQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSP-LDS-----ETLENEANNIKMEAENLE 1297
Cdd:COG1340 150 EKAKKAlekneklkelraeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKeADElrkeaDELHKEIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 145309326 1298 QLIDQKLKDYEDLREdmrgkelEVKNLLEKGKTEQQTADQ 1337
Cdd:COG1340 230 EEIIELQKELRELRK-------ELKKLRKKQRALKREKEK 262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1136-1528 |
8.79e-08 |
|
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: 57.39 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1136 AHVENTERLIEIASRELEKAKVAAANVSVTQPEstgdpnnmtlLAEEARKLA-ERHKQEADDIVRVAKTandtSTEAYNL 1214
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDE----------KRQQLERLRrEREKAERYQALLKEKR----EYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1215 LLRTLAGENQtafeIEELNRkyeQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDsetlENEANNIKMEAE 1294
Cdd:TIGR02169 229 LKEKEALERQ----KEAIER---QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----EEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1295 NLE---QLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLqeaNDILNNLK 1371
Cdd:TIGR02169 298 ELEaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1372 DFD-------RRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTK 1444
Cdd:TIGR02169 375 EVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1445 AEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQL 1524
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
....
gi 145309326 1525 GQLD 1528
Cdd:TIGR02169 531 GSVG 534
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1207-1507 |
9.51e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1207 TSTEAYNLLLRTLAGE-NQTAFEIEELNRK----YEQAKNISQDLEKQAARVHE---EAKRAGDKAVEIYASVAQLSpld 1278
Cdd:COG1340 1 SKTDELSSSLEELEEKiEELREEIEELKEKrdelNEELKELAEKRDELNAQVKElreEAQELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1279 setleNEANNIKmeaENLEQLIDqKLKDYEDLREDMRGKELEVKNL------LEKgktEQQTADQllaradaakalaeea 1352
Cdd:COG1340 78 -----EERDELN---EKLNELRE-ELDELRKELAELNKAGGSIDKLrkeierLEW---RQQTEVL--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1353 akkgrdTLQEANDILNNLKDFDRRVNDNKtAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERI 1432
Cdd:COG1340 131 ------SPEEEKELVEKIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309326 1433 ASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADqdmmmagmASQAAQEAEINARKAK 1507
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQR--------ALKREKEKEELEEKAE 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1069-1591 |
1.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1069 QAFEDRLKEAEREVMDLLREAQDVKDVDQnlmdrLQRVNNTLSSQISRLQNIrntiEETGNLAEQARAHVENTERLIEIA 1148
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADE-----AKKKAEEDKKKADELKKA----AAAKKKADEAKKKAEEKKKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1149 SRELEKAKVAAANvsvTQPESTGDPNNMTLLAEEARKLAE-----RHKQEADDIVRVAKTANDTSTEAynlllRTLAGEN 1223
Cdd:PTZ00121 1438 KKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEakkkaEEAKKADEAKKKAEEAKKKADEA-----KKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1224 QTAFEIE--ELNRKYEQAKNISQDLEKQAARVHEEAKRAGD--KAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQL 1299
Cdd:PTZ00121 1510 KKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1300 ----IDQKLKDYEDLR----------EDMRGKELEVK----------NLLEKGKTEQQTADQLLARADAAKALAEEAAKK 1355
Cdd:PTZ00121 1590 eearIEEVMKLYEEEKkmkaeeakkaEEAKIKAEELKkaeeekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1356 GRDTLQEANDILNNLKDFDRRVNDNKTAAEEAlRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERiasa 1435
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---- 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1436 vqknatstKAEAERTfaevtdlDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLS 1515
Cdd:PTZ00121 1745 --------KAEEAKK-------DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1516 II---NDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKvsDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLED 1591
Cdd:PTZ00121 1810 IIeggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1373-1581 |
1.70e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1373 FDRRVNDNK-TAAEEALRKIpaINQTITEANEKTREAQqalgsaaadaTEAKNKAHEAeriasavqknatstKAEAERtf 1451
Cdd:PRK12704 24 VRKKIAEAKiKEAEEEAKRI--LEEAKKEAEAIKKEAL----------LEAKEEIHKL--------------RNEFEK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1452 aEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmagmasqaaQEAEINARkaKNSVTSLLSIINDLLEQLGQLDTVD 1531
Cdd:PRK12704 76 -ELRERRNELQKLEKRLLQKEENLDRKLELLEK------------REEELEKK--EKELEQKQQELEKKEEELEELIEEQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 145309326 1532 LNKLNEIEG-TLNKAKDEMkvsdldrkVSDLENEAKKQEAAIMdynRDIEE 1581
Cdd:PRK12704 141 LQELERISGlTAEEAKEIL--------LEKVEEEARHEAAVLI---KEIEE 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1030-1456 |
1.83e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1030 ECPACYRLVKDkvaDHRVKLqeleslianlgtgdemvtdqafedrLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNT 1109
Cdd:PRK03918 437 KCPVCGRELTE---EHRKEL-------------------------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1110 LSSQiSRLQNIRNTIEETGNLAEQARAHveNTERLiEIASRELEKAKvaaanvsvtqPESTGDPNNMTLLAEEARKLAER 1189
Cdd:PRK03918 489 LKKE-SELIKLKELAEQLKELEEKLKKY--NLEEL-EKKAEEYEKLK----------EKLIKLKGEIKSLKKELEKLEEL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1190 HKQEA---DDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEkqaaRVHEEAKRAGDKAVE 1266
Cdd:PRK03918 555 KKKLAeleKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE----REEKELKKLEEELDK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1267 IYASVAQlspldsetLENEANNIKMEAENLEQLIDQklKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQllaradaak 1346
Cdd:PRK03918 631 AFEELAE--------TEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREE--------- 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1347 alaeeaakkgrdtlqeandILNNLKDFDRRVNDNKTAAEEaLRKIPAINQTITEANEKTREAQqalgsaaadaTEAKNKA 1426
Cdd:PRK03918 692 -------------------IKKTLEKLKEELEEREKAKKE-LEKLEKALERVEELREKVKKYK----------ALLKERA 741
|
410 420 430
....*....|....*....|....*....|.
gi 145309326 1427 -HEAERIASAVqknatstkaeaertFAEVTD 1456
Cdd:PRK03918 742 lSKVGEIASEI--------------FEELTE 758
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1027-1589 |
2.31e-07 |
|
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: 55.82 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1027 GCqeCPACYRLVKDKVadhrvKLQELESLIANLgtgdemvtDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRV 1106
Cdd:TIGR00606 678 SC--CPVCQRVFQTEA-----ELQEFISDLQSK--------LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1107 NNTLSSQISRLQNIRNTIEETGNlaeqaraHVENTERLIEIASRELEKAKVAAANVSVtqpestgdpnnMTLLAEEARKL 1186
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKN-------DIEEQETLLGTIMPEEESAKVCLTDVTI-----------MERFQMELKDV 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1187 AERHKQEAddivrvAKTANDTSTEAYNLLLRTLAGENQtafEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVE 1266
Cdd:TIGR00606 805 ERKIAQQA------AKLQGSDLDRTVQQVNQEKQEKQH---ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1267 IYASVAQLSPLdSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKElevkNLLEKGKTEQQTADQLLaradaak 1346
Cdd:TIGR00606 876 IGTNLQRRQQF-EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE----ELISSKETSNKKAQDKV------- 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1347 alaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKT-AAEEALRKIPAINQTITEANEKTREAQQALGSAAADAteakNK 1425
Cdd:TIGR00606 944 ----------NDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI----DT 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1426 AHEAERIasaVQKNATSTKaeaertfaevtdldneVNNMLKQLQEaekelKRKQDDADQDMMMAGMASQAAQEAEINARK 1505
Cdd:TIGR00606 1010 QKIQERW---LQDNLTLRK----------------RENELKEVEE-----ELKQHLKEMGQMQVLQMKQEHQKLEENIDL 1065
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1506 AKNSVTSLLSIINDLLEQLGQLDT-VDLNKLNEIEGTLNKAKDEMKVSDLdrKVSDLENEAKKQEAAIMDYNRD-IEEIM 1583
Cdd:TIGR00606 1066 IKRNHVLALGRQKGYEKEIKHFKKeLREPQFRDAEEKYREMMIVMRTTEL--VNKDLDIYYKTLDQAIMKFHSMkMEEIN 1143
|
....*.
gi 145309326 1584 KDIRNL 1589
Cdd:TIGR00606 1144 KIIRDL 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1209-1580 |
2.62e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1209 TEAYNLLLRTLAGENQTAFEIEELNRKY----EQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLEN 1284
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQElklkEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1285 EANNIKMEAENLEQLIDQKLKDY---EDLREDMRGKELEVKNLLEKGKTEQQTADQLLARAdaakalaeeaakkgRDTLQ 1361
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENkeeEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD--------------EEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1362 EANDILNNLkdfDRRVNDNKTAAEEaLRKIPAINQTITEANEKTREAQQALgsaaadatEAKNKAHEAERIASAvQKNAT 1441
Cdd:pfam02463 318 ESEKEKKKA---EKELKKEKEEIEE-LEKELKELEIKREAEEEEEEELEKL--------QEKLEQLEEELLAKK-KLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1442 STKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTSLLSIindLL 1521
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK---LL 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1522 EQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIE 1580
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1598 |
2.68e-07 |
|
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: 55.41 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1288 NIKMEAENLEQLIDQKLKDyedLREDMRGKELEVKNlLEKGKTEQQTadqllaradaakalaeeaakkgrdTLQEANDIL 1367
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKT---IKNELKNKEKELKN-LDKNLNKDEE------------------------KINNSNNKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1368 NNLK----DFDRRVNDNKTaaeealrKIPAINQTITEANE--KTREAQQALgsaaadateAKNKAHEAERIASAVQKNAT 1441
Cdd:TIGR04523 78 KILEqqikDLNDKLKKNKD-------KINKLNSDLSKINSeiKNDKEQKNK---------LEVELNKLEKQKKENKKNID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1442 STKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKR-KQDDADQDMMMAGMASQ-AAQEAEINARKAKNS-VTSLLSIIN 1518
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNIDKIKNKlLKLELLLSNLKKKIQkNKSLESQIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1519 DLLEQLGQL-DTVDL--NKLNEIEGTLNKAKDEMKVsdldrkVSDLENEAKKQeaaIMDYNRDIEEIMKDIRNLEDIRKT 1595
Cdd:TIGR04523 222 ELKKQNNQLkDNIEKkqQEINEKTTEISNTQTQLNQ------LKDEQNKIKKQ---LSEKQKELEQNNKKIKELEKQLNQ 292
|
...
gi 145309326 1596 LPS 1598
Cdd:TIGR04523 293 LKS 295
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1049-1608 |
2.99e-07 |
|
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: 55.83 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1049 LQELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQ-DVKDVDQNLmdrlqrvnntlSSQISRLQNIRNTIEet 1127
Cdd:TIGR01612 1076 LEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKdDIKNLDQKI-----------DHHIKALEEIKKKSE-- 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1128 gNLAEQARAHVENTErlieiasrelekaKVAAANVSVTQPESTGDP-NNMTLLAEEARKLAERHKQEADDIVRVAKtaND 1206
Cdd:TIGR01612 1143 -NYIDEIKAQINDLE-------------DVADKAISNDDPEEIEKKiENIVTKIDKKKNIYDEIKKLLNEIAEIEK--DK 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1207 TSTEAYNLLLRTLaGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEA 1286
Cdd:TIGR01612 1207 TSLEEVKGINLSY-GKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1287 NN-----IKMEAENLEQLIDQKLKDYEDLRE-----DMRgKELEvKNLLEkgkTEQQTADQLLARADAAKALAEEAAKKG 1356
Cdd:TIGR01612 1286 DKdhhiiSKKHDENISDIREKSLKIIEDFSEesdinDIK-KELQ-KNLLD---AQKHNSDINLYLNEIANIYNILKLNKI 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAiNQTITEANEKTREA--QQALGSAAADATEAKNKAHEAERIAS 1434
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTldDKDIDECIKKIKELKNHILSEESNID 1439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1435 AVQKNATSTKAEAERTFAEVTDLDNEVNNMLK---------------QLQEAEKELKRKQDDADQDmmmagmaSQAAQEA 1499
Cdd:TIGR01612 1440 TYFKNADENNENVLLLFKNIEMADNKSQHILKikkdnatndhdfninELKEHIDKSKGCKDEADKN-------AKAIEKN 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1500 EINARKAKNSVTSLLS-----IINDLLEQLGQLDTVDLNKLNEIEG--TLNKAKDEMKVSDLDRKVSDLENEA---KKQE 1569
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEIKKEKFRIEDDAaknDKSN 1592
|
570 580 590
....*....|....*....|....*....|....*....
gi 145309326 1570 AAIMDYNRDIEEIMKDIRNLEDIRKTLPSGCFNTPSIEK 1608
Cdd:TIGR01612 1593 KAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK 1631
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1036-1593 |
3.51e-07 |
|
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: 55.18 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1036 RLVKDKVADHRVKLQELESLIANLGT----GDEMVTDqaFEDRLKEAE--REVMDLLREAQDVKDVD-QNLMDRLQRVNN 1108
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKlknkHEAMISD--LEERLKKEEkgRQELEKAKRKLEGESTDlQEQIAELQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1109 TLSSQISR----LQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSV-------------TQPESTG 1171
Cdd:pfam01576 233 ELRAQLAKkeeeLQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKqrrdlgeelealkTELEDTL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1172 DPNNMTllaeeaRKLAERHKQEaddiVRVAKTANDTSTEAYNLLLRTLAGENQTAFEieELNRKYEQAKNISQDLEKqaa 1251
Cdd:pfam01576 313 DTTAAQ------QELRSKREQE----VTELKKALEEETRSHEAQLQEMRQKHTQALE--ELTEQLEQAKRNKANLEK--- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1252 rvheeAKRAGDKavEIYASVAQLSPLDSETLENEANNIKMEAEnLEQLiDQKLKDYEDLREDMRGKELEVKNLLEKGKTE 1331
Cdd:pfam01576 378 -----AKQALES--ENAELQAELRTLQQAKQDSEHKRKKLEGQ-LQEL-QARLSESERQRAELAEKLSKLQSELESVSSL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1332 QQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRkipainqtitEANEKTREAQQA 1411
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE----------EEEEAKRNVERQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1412 LGSAAADATEAKNKAHE-------AERIASAVQKNATST------KAEA----ERTfaeVTDLDNEVNNMLKQLQEAEK- 1473
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEdagtleaLEEGKKRLQRELEALtqqleeKAAAydklEKT---KNRLQQELDDLLVDLDHQRQl 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1474 --ELKRKQDDADQdmMMA---GMASQAAQE---AEINARKAKNSVTSLLSIINDLLEQLGQLDTVdlNKL--NEIEGTLN 1543
Cdd:pfam01576 596 vsNLEKKQKKFDQ--MLAeekAISARYAEErdrAEAEAREKETRALSLARALEEALEAKEELERT--NKQlrAEMEDLVS 671
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 145309326 1544 kAKDemkvsDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIR 1593
Cdd:pfam01576 672 -SKD-----DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1069-1605 |
3.70e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.22 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1069 QAFEDRL-KEAEREVMDLL----REAQDVKDVDQNLMDRLQRvnntlssQISRLqniRNTIEETgnlAEQARAHV-ENTE 1142
Cdd:NF041483 752 QAEAQRLvEEADRRATELVsaaeQTAQQVRDSVAGLQEQAEE-------EIAGL---RSAAEHA---AERTRTEAqEEAD 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1143 RLIEIASRELEKAKVAAANVSVTQPESTgdpnnmtllaEEARKLAERHKQEAddIVRVAKTANDTS-------TEAYNll 1215
Cdd:NF041483 819 RVRSDAYAERERASEDANRLRREAQEET----------EAAKALAERTVSEA--IAEAERLRSDASeyaqrvrTEASD-- 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1216 lrTLAGENQTAFEIEELNRkyEQAKNISQDLEKQAARVHEEAKRAGDKAVEiyASVAQLSPLDSETLENEANNIKMEAEN 1295
Cdd:NF041483 885 --TLASAEQDAARTRADAR--EDANRIRSDAAAQADRLIGEATSEAERLTA--EARAEAERLRDEARAEAERVRADAAAQ 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1296 LEQLIDQKLKDYEDLREDMRgkelevknllEKGKTEQQTADQLLARADAAKALAEEAAKKGR-DTLQEANDILNnlkdfD 1374
Cdd:NF041483 959 AEQLIAEATGEAERLRAEAA----------ETVGSAQQHAERIRTEAERVKAEAAAEAERLRtEAREEADRTLD-----E 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1375 RRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQAlgsAAADATEAKNKA--------HEAERIAS--AVQKNATSTK 1444
Cdd:NF041483 1024 ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEE---ALRTTTEAEAQAdtmvgaarKEAERIVAeaTVEGNSLVEK 1100
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1445 AEAE---------------RTFAEvtDLDNEVNNMLKQLQEaekelkRKQDDADQDMMMAG------MASQAAQEAEINA 1503
Cdd:NF041483 1101 ARTDadellvgarrdataiRERAE--ELRDRITGEIEELHE------RARRESAEQMKSAGercdalVKAAEEQLAEAEA 1172
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1504 rKAKnsvtSLLSIINDlleqlgQLDTVDLNKLNEIEGTLNKAkdEMKVSDLDRKVSDLENEAKKQ-EAAIMDYNRDI--- 1579
Cdd:NF041483 1173 -KAK----ELVSDANS------EASKVRIAAVKKAEGLLKEA--EQKKAELVREAEKIKAEAEAEaKRTVEEGKRELdvl 1239
|
570 580 590
....*....|....*....|....*....|
gi 145309326 1580 ----EEIMKDIRNLEDIRKTLPSgcFNTPS 1605
Cdd:NF041483 1240 vrrrEDINAEISRVQDVLEALES--FEAPS 1267
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1289-1598 |
4.01e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1289 IKMEAENLEQL---IDQKLKDYEDLREDMRGKELEVKNL---LEKGKTEQQTADQLlaradaakalaeeaakkgrdtLQE 1362
Cdd:COG4372 26 IAALSEQLRKAlfeLDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEE---------------------LEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1363 ANDILnnlkdfdrrvndnktaaEEALRKIPAINQTITEANEKTREAQQALgsaAADATEAKNKAHEAERIASAVQKNATS 1442
Cdd:COG4372 85 LNEQL-----------------QAAQAELAQAQEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1443 TKAEAErtfaEVTDLDNEVNNMLKQLQEAEKELKR-KQDDADQDmmMAGMASQAAQEAEINARKAKNSVTSLLSIINDLL 1521
Cdd:COG4372 145 IAEREE----ELKELEEQLESLQEELAALEQELQAlSEAEAEQA--LDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1522 EQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPS 1598
Cdd:COG4372 219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1393-1485 |
6.16e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.11 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1393 AINQTITEANEKTREAQQALGSAAADATEAKnkaHEAERIASAVQKNATSTKAEAE-RTFAEV--------TDLDNEVNN 1463
Cdd:PRK07352 54 AILQALKEAEERLRQAAQALAEAQQKLAQAQ---QEAERIRADAKARAEAIRAEIEkQAIEDMarlkqtaaADLSAEQER 130
|
90 100 110
....*....|....*....|....*....|.
gi 145309326 1464 MLKQL---------QEAEKELKRKQDDADQD 1485
Cdd:PRK07352 131 VIAQLrreaaelaiAKAESQLPGRLDEDAQQ 161
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
828-876 |
6.56e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 828 CQCSDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNPLAPN 876
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1394-1571 |
6.64e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 51.99 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1394 INQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATS--TKAE---AERTFAEVTDLDN--------- 1459
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAalTKGNeelAREALAEKKSLEKqaealetql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1460 -EVNNMLKQLQEAEKELKRK--QDDADQDMMMAGMASQAAQEAeINARKAKNSVTSLLsiinDLLEQLGqldtvdlNKLN 1536
Cdd:pfam04012 107 aQQRSAVEQLRKQLAALETKiqQLKAKKNLLKARLKAAKAQEA-VQTSLGSLSTSSAT----DSFERIE-------EKIE 174
|
170 180 190
....*....|....*....|....*....|....*
gi 145309326 1537 EIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAA 1571
Cdd:pfam04012 175 EREARADAAAELASAVDLDAKLEQAGIQMEVSEDV 209
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1042-1507 |
7.45e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.45 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1042 VADHRVklqELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQ-DVKDVDQNLMDRLQRVNNTLSSQISRLQNI 1120
Cdd:NF041483 336 LADARA---EAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASeDAKATTRAAAEEAERIRREAEAEADRLRGE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1121 RNTIEE----------------TGNLAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTgdpnnmtllAEEAR 1184
Cdd:NF041483 413 AADQAEqlkgaakddtkeyrakTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEA---------ARTAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1185 KLAERHKQEADDIVRVAKTANDTsteaynllLRTLAGENQTAF--EIEE-LNRKYEQAKNISQDLEKQAARVHEEAKRAg 1261
Cdd:NF041483 484 ELLTKAKADADELRSTATAESER--------VRTEAIERATTLrrQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERA- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1262 dkAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLL-----EKGKTEQQTAD 1336
Cdd:NF041483 555 --ARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrteaaERIRTLQAQAE 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1337 QLLARADAAKALAEEAAKKGRDTL---------QEANDILNNLKDFDRRVNDNKTAAEE--ALRKIPAINQTITEANEKT 1405
Cdd:NF041483 633 QEAERLRTEAAADASAARAEGENVavrlrseaaAEAERLKSEAQESADRVRAEAAAAAErvGTEAAEALAAAQEEAARRR 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1406 REAQQALGSAAADATEAKNKAHEA--ERIASAvQKNATSTKAEAERTFAEV----TDLDNEVNNMLKQLQEAEKELkrkQ 1479
Cdd:NF041483 713 REAEETLGSARAEADQERERAREQseELLASA-RKRVEEAQAEAQRLVEEAdrraTELVSAAEQTAQQVRDSVAGL---Q 788
|
490 500
....*....|....*....|....*...
gi 145309326 1480 DDADQDmmMAGMASQAAQEAEINARKAK 1507
Cdd:NF041483 789 EQAEEE--IAGLRSAAEHAAERTRTEAQ 814
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1411-1596 |
7.67e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1411 ALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmaG 1490
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-----L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1491 MASQAAQEAEINARKAK--------------NSVTSLLS----------------IINDLLEQLGQLDTvDLNKLNEIEG 1540
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqPPLALLLSpedfldavrrlqylkyLAPARREQAEELRA-DLAELAALRA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1541 TLNKAKDEMKV--SDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:COG4942 168 ELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-330 |
7.91e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 7.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145309326 285 RCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRR 330
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1037-1592 |
9.87e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1037 LVKDKVADHRVKLQELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLreaQDVKDVDQNLmDRLQRVNNTLSSQISR 1116
Cdd:PTZ00440 820 LIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNII---KDIENMNKNI-NIIKTLNIAINRSNSN 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1117 LQNIRNTIEETGNLAEQARAHVE--NTERLIEIASRElekakvaaanvsvtqpestgdpNNMTLLAEEARKLAERhkqea 1194
Cdd:PTZ00440 896 KQLVEHLLNNKIDLKNKLEQHMKiiNTDNIIQKNEKL----------------------NLLNNLNKEKEKIEKQ----- 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1195 ddivrvaktANDTSTeaynlllrtlageNQTAFEIEELNRKYEQAK-NISQDLEKQAARVHEEAKRAGDKAVEIyasvaq 1273
Cdd:PTZ00440 949 ---------LSDTKI-------------NNLKMQIEKTLEYYDKSKeNINGNDGTHLEKLDKEKDEWEHFKSEI------ 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1274 lSPLDSE--TLENEANN-IKMEAENLEQLIDqklKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARAdaakalae 1350
Cdd:PTZ00440 1001 -DKLNVNynILNKKIDDlIKKQHDDIIELID---KLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIK-------- 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1351 eaakkgrdtLQEANDILNNLKDFDRRVndnktaaEEALRKIPAINQTITEANEKTREaqqalgsaaaDATEAKNKAHEAE 1430
Cdd:PTZ00440 1069 ---------KYKNPKIKEEIKLLEEKV-------EALLKKIDENKNKLIEIKNKSHE----------HVVNADKEKNKQT 1122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1431 RIASAVQKNATSTKAEAERTFAEVTDLDNEvNNMLKQLQEAEKELKRKQDDADQDMMmagmaSQAAQEAEINARKAKNSV 1510
Cdd:PTZ00440 1123 EHYNKKKKSLEKIYKQMEKTLKELENMNLE-DITLNEVNEIEIEYERILIDHIVEQI-----NNEAKKSKTIMEEIESYK 1196
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1511 TSLLSIINDLL-EQLGQLDTVDLN--------KLNEIEGTLNKAKDEMKVSDLDRKVSDLEnEAKKQEAA----IMDYNR 1577
Cdd:PTZ00440 1197 KDIDQVKKNMSkERNDHLTTFEYNayydkataSYENIEELTTEAKGLKGEANRSTNVDELK-EIKLQVFSylqqVIKENN 1275
|
570
....*....|....*
gi 145309326 1578 DIEEIMKDIRNLEDI 1592
Cdd:PTZ00440 1276 KMENALHEIKNMYEF 1290
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1228-1512 |
9.97e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1228 EIEELNRKYEQAKNISQDLEKQAARVHEEAkragdkaveiyasvaqlspldsETLENEANNIKMEAENLEQLIDQKLKDY 1307
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAEL----------------------EELNEEYNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1308 EDLREDMRGKELEVKNLLekgKTEQQTADQLLARadaakalaeeaakkgrDTLQEANDIlnnlkdfdrrvndnktaaEEA 1387
Cdd:COG3883 75 AEAEAEIEERREELGERA---RALYRSGGSVSYL----------------DVLLGSESF------------------SDF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1388 LRKIPAINQtITEANEKTREAQQAlgsAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ 1467
Cdd:COG3883 118 LDRLSALSK-IADADADLLEELKA---DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 145309326 1468 LQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVTS 1512
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1228-1486 |
1.09e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 51.53 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1228 EIEELN-RKYEQA--KNISQDLEkQAARVHEEAKRAGDKAVEiYASVAQLSPLDSETLEneannikmeaENLEQLIDQKL 1304
Cdd:pfam12795 1 KLDELEkAKLDEAakKKLLQDLQ-QALSLLDKIDASKQRAAA-YQKALDDAPAELRELR----------QELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1305 KDYEDLREDMRGKELEvkNLLEKGKTEQQTAdqllaradaakalaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKTAA 1384
Cdd:pfam12795 69 AAPKEILASLSLEELE--QRLLQTSAQLQEL---------------------QNQLAQLNSQLIELQTRPERAQQQLSEA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1385 EEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAE------RIASAvQKNATSTKAEAERTFAEVTDLD 1458
Cdd:pfam12795 126 RQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLEQEllsnnnRQDLL-KARRDLLTLRIQRLEQQLQALQ 204
|
250 260
....*....|....*....|....*...
gi 145309326 1459 NEVNNmlKQLQEAEKELKRKQDDADQDM 1486
Cdd:pfam12795 205 ELLNE--KRLQEAEQAVAQTEQLAEEAA 230
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1067-1506 |
1.25e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.68 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1067 TDQAFEDRLKEAEREVMDLLREAQDvkdvdqnlmdRLQRVNNTLSSQISRLQNIRntiEETGNLAEQARAhvENTERLIE 1146
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEE----------RLTAAEEALADARAEAERIR---REAAEETERLRT--EAAERIRT 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1147 I---ASRELEKAKV-AAANVSVTQPESTgdpNNMTLLAEEARKLAERHK---QEADDIVR--VAKTANDTSTEAYNLLLR 1217
Cdd:NF041483 627 LqaqAEQEAERLRTeAAADASAARAEGE---NVAVRLRSEAAAEAERLKseaQESADRVRaeAAAAAERVGTEAAEALAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1218 TLAGENQTAFEIEEL--------NRKYEQAKNISQDL-----------EKQAARVHEEA-KRAGD-------KAVEIYAS 1270
Cdd:NF041483 704 AQEEAARRRREAEETlgsaraeaDQERERAREQSEELlasarkrveeaQAEAQRLVEEAdRRATElvsaaeqTAQQVRDS 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1271 VAQLSPLDSETL-------ENEANNIKMEAENLEQLI--------DQKLKDYEDLREDMRGKELEVKNLLEKGKTE---- 1331
Cdd:NF041483 784 VAGLQEQAEEEIaglrsaaEHAAERTRTEAQEEADRVrsdayaerERASEDANRLRREAQEETEAAKALAERTVSEaiae 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1332 -----QQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKD-----FDRRVNDNKTAAEEALRKIPA-----INQ 1396
Cdd:NF041483 864 aerlrSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSdaaaqADRLIGEATSEAERLTAEARAeaerlRDE 943
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1397 TITEANEKTREAQQALGSAAADAT-EAKN-KAHEAERIASAvQKNATSTKAEAERTFAEVTDLDNEVNNMLKQ-----LQ 1469
Cdd:NF041483 944 ARAEAERVRADAAAQAEQLIAEATgEAERlRAEAAETVGSA-QQHAERIRTEAERVKAEAAAEAERLRTEAREeadrtLD 1022
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 145309326 1470 EAEKEL-KRKQDDADQ-DMMMAGMASQAAQ---EAEINARKA 1506
Cdd:NF041483 1023 EARKDAnKRRSEAAEQaDTLITEAAAEADQltaKAQEEALRT 1064
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1232-1571 |
1.42e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1232 LNRKYEQAKNISQDLEKqaarvheeakragdkaVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLR 1311
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFP----------------LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1312 EDMrgkELEVKNLLEKGKTEQQTADQllaradaakalaeeaakkgrdtLQEandilnnlkdfdrrvndNKTAAEEALRKI 1391
Cdd:TIGR00618 222 QVL---EKELKHLREALQQTQQSHAY----------------------LTQ-----------------KREAQEEQLKKQ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1392 PAINQTITEanEKTREAQQAlgsAAADATEAKNKAHEAERIAsAVQKNATSTKAEAERTFAEvtdLDNEVNNMLKQLQEA 1471
Cdd:TIGR00618 260 QLLKQLRAR--IEELRAQEA---VLEETQERINRARKAAPLA-AHIKAVTQIEQQAQRIHTE---LQSKMRSRAKLLMKR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1472 EKELKRKQDDADQDMMMagmasQAAQEAEINARKAKNSVTSLLSIINDLLE------QLGQLDTVDLNKLNEIEGTLNKA 1545
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLL-----QTLHSQEIHIRDAHEVATSIREISCQQHTltqhihTLQQQKTTLTQKLQSLCKELDIL 405
|
330 340 350
....*....|....*....|....*....|
gi 145309326 1546 KDEM-KVSDLDRKVSDLENE---AKKQEAA 1571
Cdd:TIGR00618 406 QREQaTIDTRTSAFRDLQGQlahAKKQQEL 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1357-1527 |
1.50e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEANDILNNLKDFDRRVNDNKTAAEEAL-------RKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEA 1429
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQaelealqAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1430 ERIASAvqKNATS--TKAEAERTfaeVTDLDNEvnnMLKQLQEAEKELKRKQDDAD--QDMMMAGMASQAAQEAEINARK 1505
Cdd:COG3883 106 DVLLGS--ESFSDflDRLSALSK---IADADAD---LLEELKADKAELEAKKAELEakLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....
gi 145309326 1506 AKNS--VTSLLSIINDLLEQLGQL 1527
Cdd:COG3883 178 AEQEalLAQLSAEEAAAEAQLAEL 201
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1038-1595 |
1.72e-06 |
|
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: 52.87 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1038 VKDKVADHRVKLQ-ELESLIANLGtgdemvtdqAFEDRLKEAEREVMDLLREAQDVkdvdQNLMDRLQRVNNTLSSQISR 1116
Cdd:pfam01576 427 QRAELAEKLSKLQsELESVSSLLN---------EAEGKNIKLSKDVSSLESQLQDT----QELLQEETRQKLNLSTRLRQ 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1117 LQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKaKVAAANVSVTQpestgdpnnmtllAEEARKLAER------- 1189
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK-KLEEDAGTLEA-------------LEEGKKRLQRelealtq 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1190 ---HKQEADDivRVAKTANDTSTEaYNLLLRTLAGENQTAFEIEELNRKYEQA----KNISqdlekqaARVHEEAKRAGD 1262
Cdd:pfam01576 560 qleEKAAAYD--KLEKTKNRLQQE-LDDLLVDLDHQRQLVSNLEKKQKKFDQMlaeeKAIS-------ARYAEERDRAEA 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1263 KAVEIYASVAQLSPLDSETLEN----EANNIKMEAEnLEQLIDQKlkdyedlreDMRGK---ELE-VKNLLEKGKTEQQT 1334
Cdd:pfam01576 630 EAREKETRALSLARALEEALEAkeelERTNKQLRAE-MEDLVSSK---------DDVGKnvhELErSKRALEQQVEEMKT 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1335 ADQLLaradaakalaeeaakkgRDTLQEANDI-------LNNLK-DFDRRVNDNKTAAEEALRKI-PAINQTITEANEKT 1405
Cdd:pfam01576 700 QLEEL-----------------EDELQATEDAklrlevnMQALKaQFERDLQARDEQGEEKRRQLvKQVRELEAELEDER 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1406 REAQQALGSAAADATEAKnkahEAERIASAVQKNatstKAEAERtfaevtdldnevnnMLKQLQEAEKELKRKQDD--AD 1483
Cdd:pfam01576 763 KQRAQAVAAKKKLELDLK----ELEAQIDAANKG----REEAVK--------------QLKKLQAQMKDLQRELEEarAS 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1484 QDMMMAGmasqaAQEAEinaRKAKNSVTSLLsiindlleQLGQldtvDLNKLNEIEGTLNKAKDEM--KVSDLDRKVSDL 1561
Cdd:pfam01576 821 RDEILAQ-----SKESE---KKLKNLEAELL--------QLQE----DLAASERARRQAQQERDELadEIASGASGKSAL 880
|
570 580 590
....*....|....*....|....*....|....*
gi 145309326 1562 ENEAKKQEAAIMDYNRDIEEIMKDIRNLED-IRKT 1595
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDrLRKS 915
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1078-1596 |
1.84e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1078 AEREvmDLLREAQDVKDVDQNlMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKV 1157
Cdd:PRK01156 149 AQRK--KILDEILEINSLERN-YDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1158 AAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTAND--TSTEAYNLLlrtlagENQTAFEIEELNRK 1235
Cdd:PRK01156 226 EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYykELEERHMKI------INDPVYKNRNYIND 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1236 YEQAKNISQDLEKqaarvheeakragdkaveiyasvaQLSPLDSETLENEANNIKmeAENLEQLIDQ---KLKDYEDL-- 1310
Cdd:PRK01156 300 YFKYKNDIENKKQ------------------------ILSNIDAEINKYHAIIKK--LSVLQKDYNDyikKKSRYDDLnn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1311 -REDMRGKELE----VKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNdNKTAAE 1385
Cdd:PRK01156 354 qILELEGYEMDynsyLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS-SLNQRI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1386 EALRKipaiNQTITEANEKTREAQQALGSAAADATEAKnkaheAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNML 1465
Cdd:PRK01156 433 RALRE----NLDELSRNMEMLNGQSVCPVCGTTLGEEK-----SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1466 KQLQEAEKELKRKQDDADQDMMMAG------MASQAA-QEAEINARKAKNSVTSL-LSIIN----DLLEQLGQLDTVDLN 1533
Cdd:PRK01156 504 KRKEYLESEEINKSINEYNKIESARadlediKIKINElKDKHDKYEEIKNRYKSLkLEDLDskrtSWLNALAVISLIDIE 583
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1534 KL----NEIEGTLNKAKDEMK--VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:PRK01156 584 TNrsrsNEIKKQLNDLESRLQeiEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI 652
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1050-1585 |
2.33e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.91 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1050 QELESLIANLGtgdemVTDQAFEDRLKEAEREVMDLLReaQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGN 1129
Cdd:PTZ00440 998 SEIDKLNVNYN-----ILNKKIDDLIKKQHDDIIELID--KLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKY 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1130 LAEQARAHVENTERLIEIASRELEKAKVAAANVSVTQPEstgdpnNMTLLAEEARKLAERHKQEADDIVRVAKTANDTST 1209
Cdd:PTZ00440 1071 KNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHE------HVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLK 1144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1210 EaynllLRTLAGENQTAFEIEELNRKYEQAKnISQDLEKqaarVHEEAKRAGDKAVEIYASVAQLSPLDsetleneANNI 1289
Cdd:PTZ00440 1145 E-----LENMNLEDITLNEVNEIEIEYERIL-IDHIVEQ----INNEAKKSKTIMEEIESYKKDIDQVK-------KNMS 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1290 KMEAENLEQLidqklkDYEDLREDMRGKELEVKNLLEKGKTEQQTADqllaradaakalaeeaakkgRDT-LQEANDILN 1368
Cdd:PTZ00440 1208 KERNDHLTTF------EYNAYYDKATASYENIEELTTEAKGLKGEAN--------------------RSTnVDELKEIKL 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1369 NLKDFDRRVNDNKTAAEEALRKIPAINqTITEANEKTREAQQALGSAaadateakNKAHEAERiasavqknatstkaEAE 1448
Cdd:PTZ00440 1262 QVFSYLQQVIKENNKMENALHEIKNMY-EFLISIDSEKILKEILNST--------KKAEEFSN--------------DAK 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1449 RTFAEVTDLDNEVNNMLKQLQEAEKE----LKRKQDDADQDMMMAGMASQAAQEAEIN-----ARKAKNSVTSLLSIIN- 1518
Cdd:PTZ00440 1319 KELEKTDNLIKQVEAKIEQAKEHKNKiygsLEDKQIDDEIKKIEQIKEEISNKRKEINkylsnIKSNKEKCDLHVRNASr 1398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1519 -----DLLEQLGQLDTVDLNKLN--EIEGTLNKAKDEMKvsdldrKVSDLENEAKKQEAAIMDYNRDIEEIMKD 1585
Cdd:PTZ00440 1399 gkdkiDFLNKHEAIEPSNSKEVNiiKITDNINKCKQYSN------EAMETENKADENNDSIIKYEKEITNILNN 1466
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1063-1312 |
3.86e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 51.54 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1063 DEMVTDQAFEDRLKEAEREVmDLLREAQDVKDVDQNLMDRlqrvnntlssqisRLQNIRNTIEETGNLAEQARAHVENTE 1142
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGV-NFRRDMTDLKERESQEDAK-------------RAQQLKEELDKKQIDADKAQQKADFAQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1143 RLIEIASRELEKAKVAAANVSvtQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAynlLLRTLAGE 1222
Cdd:pfam05262 241 DNADKQRDEVRQKQQEAKNLP--KPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFD---LKQESKAS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1223 NQTAfEIEELNRKYEQaKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEAnnikmeaenleQLIDq 1302
Cdd:pfam05262 316 EKEA-EDKELEAQKKR-EPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLKVVDPITNLSEL-----------VLID- 381
|
250
....*....|
gi 145309326 1303 kLKDYEDLRE 1312
Cdd:pfam05262 382 -LKTEVRLRE 390
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1357-1570 |
4.23e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 49.99 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEAndiLNNLKDfdrrvndnktaAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAV 1436
Cdd:pfam12795 19 LQDLQQA---LSLLDK-----------IDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1437 QK-NATSTK-AEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNsvtSLL 1514
Cdd:pfam12795 85 QRlLQTSAQlQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAEL---AAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309326 1515 SIINDLLEQlgQLDTvdLNKLNEIegtLNKAKDEM--KVSDLDRKVSDLE---NEAKKQEA 1570
Cdd:pfam12795 162 KAQIDMLEQ--ELLS--NNNRQDL---LKARRDLLtlRIQRLEQQLQALQellNEKRLQEA 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1181-1596 |
8.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1181 EEARKLAERHKQEADDIVrvaktandtstEAYNLLLRTLAGENQtafEIEELNRKYEQAKNISQDLekqAARVHEEAKRA 1260
Cdd:PRK02224 226 EEQREQARETRDEADEVL-----------EEHEERREELETLEA---EIEDLRETIAETEREREEL---AEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1261 GDKAVEIYASVAQLSpLDSetleneannikMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLA 1340
Cdd:PRK02224 289 EELEEERDDLLAEAG-LDD-----------ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1341 radaakalaeeaakkgrdtlqEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAA---A 1417
Cdd:PRK02224 357 ---------------------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdflE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1418 DATEAKNKAHEAERIASAVQKNATSTKAEAERTFAE---------------VTDLDnEVNNMLKQLQEAEKELKRKQDDA 1482
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphVETIE-EDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1483 DQDMMMAGMASQAAQEAEINARKAKNsvtsllsiINDLLEQlgQLDTVDlnklneiegtlnkaKDEMKVSDLDRKVSDLE 1562
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEERRED--------LEELIAE--RRETIE--------------EKRERAEELRERAAELE 550
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 145309326 1563 NEAKKQEAA--------------IMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:PRK02224 551 AEAEEKREAaaeaeeeaeeareeVAELNSKLAELKERIESLERIRTLL 598
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1072-1536 |
8.37e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQ--ISRLQNIRNTIEEtgNLAEQARAHVENTERLIEias 1149
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQekIERYQADLEELEE--RLEEQNEVVEEADEQQEE--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1150 RElekAKVAAANVSVTQPESTgdpnnmtlLAEEARKLAERHK-----QEADDIVRVAKTANDtsteaynllLRTLAGENQ 1224
Cdd:PRK04863 381 NE---ARAEAAEEEVDELKSQ--------LADYQQALDVQQTraiqyQQAVQALERAKQLCG---------LPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1225 TAFeIEELNRKYEQAKNISQDLEkQAARVHEEAKRAGDKAVEIYASVA-QLSPLDS-----ETLEnEANNIKMEAENLEQ 1298
Cdd:PRK04863 441 EDW-LEEFQAKEQEATEELLSLE-QKLSVAQAAHSQFEQAYQLVRKIAgEVSRSEAwdvarELLR-RLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1299 LiDQKLKDyedlredmrgkelevknlLEKGKTEQQTADQLlaradaakalaeeaakkgrdtlqeandilnnLKDFDRRVN 1378
Cdd:PRK04863 518 L-RMRLSE------------------LEQRLRQQQRAERL-------------------------------LAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1379 DNKTAAEEAlrkipainQTITEANEKTRE-AQQALGSAAADATEAKnkaHEAERIASAVQKNAtsTKAEAERTFaevtdl 1457
Cdd:PRK04863 548 KNLDDEDEL--------EQLQEELEARLEsLSESVSEARERRMALR---QQLEQLQARIQRLA--ARAPAWLAA------ 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1458 dnevNNMLKQLQEAEKElkrkqDDADQDMMMAGMASQAAQEAEinARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLN 1536
Cdd:PRK04863 609 ----QDALARLREQSGE-----EFEDSQDVTEYMQQLLERERE--LTVERDELAARKQALDEEIERLSQPGGSEDPRLN 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1069-1274 |
1.08e-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: 49.76 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1069 QAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIA 1148
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1149 SRELEKAK------VAAANVSVTQPE-----STGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLR 1217
Cdd:COG4942 96 RAELEAQKeelaelLRALYRLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1218 TLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL 1274
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1122-1581 |
1.11e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1122 NTIEETGNLAEQARAHVENTERLIEIASRELekakvaaanvsVTQPESTgdpnNMTLLAEEARKLAERH---KQEADDIV 1198
Cdd:PTZ00440 2150 TNIDKANKLSSELSEAVTNSEEIIENIKKEI-----------IEINENT----EMNTLENTADKLKELYenlKKKKNIIN 2214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1199 RVAKTAN-------DTSTEAYNLLLRTLAGENQT-AFEIEELNRKYEQAKNISQDLEKQAARVH-----EEAKRAGDKAV 1265
Cdd:PTZ00440 2215 NIYKKINfiklqeiENSSEKYNDISKLFNNVVETqKKKLLDNKNKINNIKDKINDKEKELINVDssftlESIKTFNEIYD 2294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1266 EIYASVAQLSPLDsETLENEANNIKMEAENLEQLIDQK---LKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARA 1342
Cdd:PTZ00440 2295 DIKSNIGDLYKLE-DTNNDELKKVKLYIENITHLLNRIntlINDLDNYQDENYGKDKNIELNNENNSYIIKTKEKINNLK 2373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1343 DAAKALAEEAAKKgrDTLQEANDILNNLKDFDRRVNDNKTAAEEAL---RKIPAINQTITEANEKTREAQQALGSAAADA 1419
Cdd:PTZ00440 2374 EEFSKLLKNIKRN--NTLCNNNNIKDFISNIGKSVETIKQRFSSNLpekEKLHQIEENLNEIKNIMNETKRISNVDAFTN 2451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1420 TEAKNKAHEAERIASAVQKNATSTKAEaertfaEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmMAGMASQAAQEA 1499
Cdd:PTZ00440 2452 KILQDIDNEKNKENNNMNAEKIDDLIE------NVTSHNEKIKSELLIINDALRRVKEKKDEMNK---LFNSLTENNNNN 2522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1500 EINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDI 1579
Cdd:PTZ00440 2523 NNSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENEKLKLLEKAKIEESRKERERIESETQEDNTDEEQINRQQ 2602
|
..
gi 145309326 1580 EE 1581
Cdd:PTZ00440 2603 QE 2604
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1287-1596 |
1.21e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1287 NNIKMEAENLEQLIDQKLKDYEDLREdmrgKELEVKNLLEKGKTEqqtadqllaradaakalaeeaakkgRDTLQEAndi 1366
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKE----KRDELNEELKELAEK-------------------------RDELNAQ--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1367 lnnLKDFDRRVNDNKtaaeeALRKipAINQTITEANEKTREAQQALGSAAADATEAKNKAheAERIASAVQKNATSTKAE 1446
Cdd:COG1340 52 ---VKELREEAQELR-----EKRD--ELNEKVKELKEERDELNEKLNELREELDELRKEL--AELNKAGGSIDKLRKEIE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1447 A-ERTF-AEVTDLDNEvNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQaAQEAEINARKAKNSVTSLLSIINDLLEQL 1524
Cdd:COG1340 120 RlEWRQqTEVLSPEEE-KELVEKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309326 1525 GQLdtvdlnkLNEIEgTLNKAKDEMKvsdldRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:COG1340 198 IEL-------YKEAD-ELRKEADELH-----KEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1274-1467 |
1.23e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 48.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1274 LSPLDS-----ETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKAL 1348
Cdd:pfam06008 32 LSPENAhkiqiEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1349 AEEAAKKGRD-TLQEANDILNNLKDFD-----RRVNDNKTAAEEALRKI---------------PAINQTITEANEKTRE 1407
Cdd:pfam06008 112 DFALPSSDLSrMLAEAQRMLGEIRSRDfgtqlQNAEAELKAAQDLLSRIqtwfqspqeenkalaNALRDSLAEYEAKLSD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1408 AQQALgsaaadaTEAKNKAHEAERIASAVQKNATstkaEAERTFAEVTDLDNEVNNMLKQ 1467
Cdd:pfam06008 192 LRELL-------REAAAKTRDANRLNLANQANLR----EFQRKKEEVSEQKNQLEETLKT 240
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1046-1336 |
1.25e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1046 RVKLQELESLIAN-----LGTGDEMVTDQA----FEDRLKEAEREVMDLLREAQD----VKDVDQ---NLMDRLQRVNNT 1109
Cdd:pfam10174 351 RLRLEEKESFLNKktkqlQDLTEEKSTLAGeirdLKDMLDVKERKINVLQKKIENlqeqLRDKDKqlaGLKERVKSLQTD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1110 LSSQISRLqnirNTIEETgnLAEQARAhVEN---------TERLIEIAS--RELEKAKvaaANVSVTQPESTGDPNNMTL 1178
Cdd:pfam10174 431 SSNTDTAL----TTLEEA--LSEKERI-IERlkeqreredRERLEELESlkKENKDLK---EKVSALQPELTEKESSLID 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1179 LAEEARKLAERHKQEaDDIVRVAKTANDTSTEAYNlllrTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAK 1258
Cdd:pfam10174 501 LKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECS----KLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESG 575
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1259 RAgdkaveiYASVAQLSPLDSETlENEANNIKMEAENLEQLIDQKLKDyedlrEDMRGKELEVKNLLEKGKTEQQTAD 1336
Cdd:pfam10174 576 KA-------QAEVERLLGILREV-ENEKNDKDKKIAELESLTLRQMKE-----QNKKVANIKHGQQEMKKKGAQLLEE 640
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1393-1485 |
1.42e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 46.70 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1393 AINQTITEANEKTREAQQALGSAAADATEAKNKAH--------EAERIASAVQKNAtstKAEAERTFAEV-TDLDNEVNN 1463
Cdd:COG0711 35 KIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAeiiaearkEAEAIAEEAKAEA---EAEAERIIAQAeAEIEQERAK 111
|
90 100 110
....*....|....*....|....*....|.
gi 145309326 1464 MLKQLQE---------AEKELKRKQDDADQD 1485
Cdd:COG0711 112 ALAELRAevadlavaiAEKILGKELDAAAQA 142
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1241-1581 |
1.76e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1241 NISQDLEKQAARVHE-EAK----RAGDKAVEiyASVAQLSpLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMR 1315
Cdd:pfam19220 38 AILRELPQAKSRLLElEALlaqeRAAYGKLR--RELAGLT-RRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1316 GKELEVKNL-----LEKGKTEQQTADQLLARADAAKALAEEAAKKG-RDTLQEANDILnnlKDFDRRVNDNktaAEEALR 1389
Cdd:pfam19220 115 DKTAQAEALerqlaAETEQNRALEEENKALREEAQAAEKALQRAEGeLATARERLALL---EQENRRLQAL---SEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1390 KIPAINQTITEaNEKTREAQQAlgsaAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFA--EVTDLDNEVNNMLKQ 1467
Cdd:pfam19220 189 ELAELTRRLAE-LETQLDATRA----RLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLrmKLEALTARAAATEQL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1468 LQEAEKELKRKqddadQDMMMAgmASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDlNKLNEIEGTLNKA-- 1545
Cdd:pfam19220 264 LAEARNQLRDR-----DEAIRA--AERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAR-AELEERAEMLTKAla 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 145309326 1546 -KD------EMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEE 1581
Cdd:pfam19220 336 aKDaaleraEERIASLSDRIAELTKRFEVERAALEQANRRLKE 378
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1393-1505 |
2.14e-05 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 45.77 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1393 AINQTITEANEKTREAQQALgsaaADATEAKNKAH-EAERIASAVQKNATSTKAEAertfaeVTDLDNEVNNMLKQlqeA 1471
Cdd:pfam00430 34 LIADEIAEAEERRKDAAAAL----AEAEQQLKEARaEAQEIIENAKKRAEKLKEEI------VAAAEAEAERIIEQ---A 100
|
90 100 110
....*....|....*....|....*....|....
gi 145309326 1472 EKELKRKQDDAdqdmmMAGMASQAAQEAEINARK 1505
Cdd:pfam00430 101 AAEIEQEKDRA-----LAELRQQVVALAVQIAEK 129
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1057-1569 |
2.94e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 48.86 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1057 ANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARA 1136
Cdd:COG5271 139 TLGGGDLDLATKDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAAD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1137 ---HVENTERLIEIASRELEKAKVAAANV----SVTQPESTGDPNNMTLLAEEARKLAERHK---QEADDIVRVAKTAND 1206
Cdd:COG5271 219 ddlAAEEGASAVVEEEDASEDAVAAADETlladDDDTESAGATAEVGGTPDTDDEATDDADGleaAEDDALDAELTAAQA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1207 TSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARvhEEAKRAGDKAVEIyasVAQLSPLDSETLENEA 1286
Cdd:COG5271 299 ADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAE--DAAEEAATAEDSA---AEDTQDAEDEAAGEAA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1287 NNIKMEAENLEQLIDQKLKDYEDLREDMRGK------------ELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAK 1354
Cdd:COG5271 374 DESEGADTDAAADEADAAADDSADDEEASADggtsptsdtdeeEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1355 KGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALR--KIPAINQTITEANEKTREAQQALGSA-AADATEAKNKAHEAER 1431
Cdd:COG5271 454 DEEEEAEAELDTEEDTESAEEDADGDEATDEDDASddGDEEEAEEDAEAEADSDELTAEETSAdDGADTDAAADPEDSDE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1432 IASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSVT 1511
Cdd:COG5271 534 DALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDD 613
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1512 SLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMkvsdldrkvSDLENEAKKQE 1569
Cdd:COG5271 614 EADADADGAADEEETEEEAAEDEAAEPETDASEAADED---------ADAETEAEASA 662
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1367-1589 |
3.18e-05 |
|
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: 48.89 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1367 LNNLKDFDRRVNDNKtaaeealrkipaiNQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAE 1446
Cdd:TIGR01612 2322 LNDLKEIDQYISDKK-------------NIFLHALNENTNFNFNALKEIYDDIINRENKADEIENINNKENENIMQYIDT 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1447 AERTFAEVTDLDNEV------NNMLKQ-LQEA-EKELKRKQDDADQDMmmagmasQAAQEA--EINARKAK----NSVTS 1512
Cdd:TIGR01612 2389 ITKLTEKIQDILIFVttyendNNIIKQhIQDNdENDVSKIKDNLKKTI-------QSFQEIlnKIDEIKAQfyggNNINN 2461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1513 LLSIINDLLEQLGQLDTVDL---NKLNEIEGTL-----------------------------------NKAKDEM-KVSD 1553
Cdd:TIGR01612 2462 IIITISQNANDVKNHFSKDLtieNELIQIQKRLediknaaheirseqitkytnaihnhieeqfkkienNSNKDEVyKINE 2541
|
250 260 270
....*....|....*....|....*....|....*....
gi 145309326 1554 LDRKVSDLENEAKKQEA---AIMDYNRDIEEIMKDIRNL 1589
Cdd:TIGR01612 2542 IDNIIEKIINYNKEPEVklhAIIDNKNEFASIIPDIKNL 2580
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1072-1258 |
3.90e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVMDLLREAQ--DVKDVDQNLMDRLQRVNNTLS---SQISRLQNIRNTIEETGNLAEQARAHVENTERLIE 1146
Cdd:COG3206 188 RKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAearAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1147 IASRELE-KAKVAAANVSVTqpestgdPNN--MTLLAEEARKLAERHKQEADDI-------VRVAKTANDTSTEAYNLLL 1216
Cdd:COG3206 268 LRAQLAElEAELAELSARYT-------PNHpdVIALRAQIAALRAQLQQEAQRIlasleaeLEALQAREASLQAQLAQLE 340
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145309326 1217 RTLAGENQTAFEIEELNRKYEQAKNISQDLEK--QAARVHEEAK 1258
Cdd:COG3206 341 ARLAELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1296-1609 |
4.17e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1296 LEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARAdaakalaeeaakkgrDTLQEANDILNNLKDFDR 1375
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDA---------------DKAQQKADFAQDNADKQR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1376 RVNDNKTAAEEALRKiPAinqTITEANEKTREAQQALGSAAADATEAKNKAHEAeriasavqKNATSTKAEaertfaevt 1455
Cdd:pfam05262 248 DEVRQKQQEAKNLPK-PA---DTSSPKEDKQVAENQKREIEKAQIEIKKNDEEA--------LKAKDHKAF--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1456 DLDNEVNNMLKQLQEAEKELKRKQDDADQDM--MMAGMASQAAQEAEiNARKAKNSVTSLLSIinDLLEQLGQLDTVDLN 1533
Cdd:pfam05262 307 DLKQESKASEKEAEDKELEAQKKREPVAEDLqkTKPQVEAQPTSLNE-DAIDSSNPVYGLKVV--DPITNLSELVLIDLK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1534 K--------LNEIEGTL--NKAKDEMKVSD---------LDRKVSDLE-----NEAKKQEAAIMDYNRDIEEIMKDIRNL 1589
Cdd:pfam05262 384 TevrlresaQQTIRRRGlyEREKDLVAIAItsgnaklqlVDIDLKNLEvikesNFEIAKNSSLYVDSRMILVAVKDDSNK 463
|
330 340
....*....|....*....|
gi 145309326 1590 EDIRKTLPSGCFNTPSIEKP 1609
Cdd:pfam05262 464 WRLAKFSPKLDEFILSENKI 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1448-1598 |
4.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1448 ERTFAEVTDLDnEVNNMLKQLQEAEKELKRKQDDADQDMMmagmasqaaQEAEINARK--AKNSVTSLLSIINDLLEQLG 1525
Cdd:PRK03918 148 EKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIK---------RTENIEELIkeKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1526 QLDTvDLNKLNEIEGTLNKAKDEmkVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPS 1598
Cdd:PRK03918 218 ELRE-ELEKLEKEVKELEELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1036-1593 |
4.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1036 RLVKDKVADHRVKLQELESLIANLGTgdemvtdqafeDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQIS 1115
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGG-----------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1116 RLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANV--SVTQPESTGDPNNMTLLAEEARKLA------ 1187
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaSLERRKSNIPARLLALRDALAEALGldeael 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1188 ----------------------------------ERHKQEADDIV------------RVAKTANDTSTEAynLLLRTLAG 1221
Cdd:COG4913 461 pfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAALRWVnrlhlrgrlvyeRVRTGLPDPERPR--LDPDSLAG 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1222 E---NQTAFE------------------IEELnRKYEQAknISQD-LEKQAARVHEeaKRAGDKAVEIYA----SVAQLS 1275
Cdd:COG4913 539 KldfKPHPFRawleaelgrrfdyvcvdsPEEL-RRHPRA--ITRAgQVKGNGTRHE--KDDRRRIRSRYVlgfdNRAKLA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1276 PLDSE--TLENEANNIKMEAENLEQLID---------QKLKDYEDLREDMRGKELEVKNLlekgktEQQtadqllarada 1344
Cdd:COG4913 614 ALEAElaELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDVASAEREIAEL------EAE----------- 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1345 akalaeeaakkgRDTLQEANDILNNLKDfdrrvndnktAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKN 1424
Cdd:COG4913 677 ------------LERLDASSDDLAALEE----------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1425 KAHEAERIASAVQknatstKAEAERTFAEVtDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINar 1504
Cdd:COG4913 735 RLEAAEDLARLEL------RALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA-- 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1505 kakNSVTSLLSiINDLLEQLGQLDTVDL-NKLNEIEGTLNKAKDEmKVSDLDRKvsdLENEAkkqeaaimdynRDIEEIM 1583
Cdd:COG4913 806 ---DLDADLES-LPEYLALLDRLEEDGLpEYEERFKELLNENSIE-FVADLLSK---LRRAI-----------REIKERI 866
|
650
....*....|.
gi 145309326 1584 KDI-RNLEDIR 1593
Cdd:COG4913 867 DPLnDSLKRIP 877
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-820 |
5.44e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 5.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 145309326 772 PCPCPGGSSCAVVPKTKEVVCTnCPTGTTGKRCELCDDGYFGDPLGRNG 820
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
342-396 |
5.75e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.96 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 342 CDCNGR---SQECYFdpelyrstgHGGHCTnCQDNTDGAHCERCRENFFRLGNNEACS 396
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
828-872 |
5.94e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 5.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 145309326 828 CQCsdNIDPNAVGNCNRLTGECLkCIYNTAGFYCDRCKDGFFGNP 872
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1361-1596 |
6.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1361 QEANDILNNLKD--FDRRVNDNKTAAEEALRkipAINQTITEANEKTREAQQALgsaaadateaknkaheaERIASavQK 1438
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALE---FLEEQLPELRKELEEAEAAL-----------------EEFRQ--KN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1439 NATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELK--RKQDDADQDMMMAGMASQA-----AQEAEINARKAKNS-- 1509
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSar 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1510 -------VTSLLSIINDLLEQLGQldtvdlnklnEIEGTLNKAKDEMKVsdLDRKVSDLENEAKKQEAAIMDYN---RDI 1579
Cdd:COG3206 286 ytpnhpdVIALRAQIAALRAQLQQ----------EAQRILASLEAELEA--LQAREASLQAQLAQLEARLAELPeleAEL 353
|
250
....*....|....*..
gi 145309326 1580 EEIMKDIRNLEDIRKTL 1596
Cdd:COG3206 354 RRLEREVEVARELYESL 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1048-1321 |
7.06e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1048 KLQELESLIANLGTGDEMVTDQafEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISRLQNIRNTIeet 1127
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQC--QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV--- 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1128 gnLAEQARAHVENTERLIeIASRELEKAKVAAANVSVTQPESTGDpnnMTLLAEearkLAERHKQEADDIVRVAKTANDT 1207
Cdd:TIGR00618 756 --LKARTEAHFNNNEEVT-AALQTGAELSHLAAEIQFFNRLREED---THLLKT----LEAEIGQEIPSDEDILNLQCET 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1208 STEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVA-QLSPLDSETleNEA 1286
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGdALIKFLHEI--TLY 903
|
250 260 270
....*....|....*....|....*....|....*
gi 145309326 1287 NNIKMEAENLEQLIDQklkdYEDLREDMRGKELEV 1321
Cdd:TIGR00618 904 ANVRLANQSEGRFHGR----YADSHVNARKYQGLA 934
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1358-1590 |
7.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1358 DTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIpainQTITEANEKTREAQQALGSAAADATEaknkaheaeriasavq 1437
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEA----DEVLEEHEERREELETLEAEIEDLRE---------------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1438 knatsTKAEAERtfaEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDmmMAGMASQAAQEAEINARKAknsvtsllSII 1517
Cdd:PRK02224 266 -----TIAETER---EREELAEEVRDLRERLEELEEERDDLLAEAGLD--DADAEAVEARREELEDRDE--------ELR 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309326 1518 NDLLEQlgQLDTVDLNklNEIEGTLNKAKD-EMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLE 1590
Cdd:PRK02224 328 DRLEEC--RVAAQAHN--EEAESLREDADDlEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1412-1576 |
8.48e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 44.22 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1412 LGSAAADATEAKNKAHEAE-RIASAVQKNatstkaeaertfaevTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAG 1490
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEeKVKELEQEN---------------LEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1491 MASQAAQEAEINARKaknsvtsllsiiNDLLEQlgQLDTVDlNKLNEiegTLNKAKD-EMKVSDLDRKVSDLENEA---- 1565
Cdd:pfam12718 67 ESEKLKTNNENLTRK------------IQLLEE--ELEESD-KRLKE---TTEKLREtDVKAEHLERKVQALEQERdewe 128
|
170
....*....|.
gi 145309326 1566 KKQEAAIMDYN 1576
Cdd:pfam12718 129 KKYEELEEKYK 139
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1280-1504 |
9.09e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1280 ETLENEANNIKMEAENLEQLIDQKLKDYEDLREDMrgKELEVKNLLEKGKTEQQTADQLlaradaakalaeeaakkgrdt 1359
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL--NKLNTAAAKIKSKIEQFQKVIK--------------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1360 LQEANDI----LNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQAlgsaAADATEAKNKAHEAERIASA 1435
Cdd:PHA02562 280 MYEKGGVcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQ----SKKLLELKNKISTNKQSLIT 355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1436 VQKNATSTKAEAERTFAEVTDLDNEvnnmLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINAR 1504
Cdd:PHA02562 356 LVDKAKKVKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDSGIKAS 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1372-1587 |
9.66e-05 |
|
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: 47.37 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1372 DFDRRVndnktaaEEALRKIPAINQTITEANEKTREAQQALGSAAADateaKNKAHEAERIASAVQKnatstkaeaertf 1451
Cdd:TIGR02169 167 EFDRKK-------EKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKRE------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1452 AEVTDLDNEVNNMLKQLQEAEKELKRKQddadqdmmmagmASQAAQEAEINARKAK-NSVTSLLSIINDLLEQLGQLDTV 1530
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLE------------EELEKLTEEISELEKRlEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1531 DLN-KLNEIEGTLNKAKDemKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIR 1587
Cdd:TIGR02169 291 RVKeKIGELEAEIASLER--SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1224-1575 |
9.83e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1224 QTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAveiyasvaqlspldsETLENEANNIKMEAENLEQLIDQ- 1302
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEL---------------EQLEEELEQARSELEQLEEELEEl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1303 ------KLKDYEDLREDMRGKELEVKNL---LEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKdf 1373
Cdd:COG4372 86 neqlqaAQAELAQAQEELESLQEEAEELqeeLEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1374 drrvndNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAE 1453
Cdd:COG4372 164 ------EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1454 VTDLDNEVNNMLKQLQEAEKELKRKQDDADQDM---------MMAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQL 1524
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIEELELAILVEkdteeeeleIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1525 GQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVS--DLENEAKKQEAAIMDY 1575
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDndVLELLSKGAEAGVADG 370
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1067-1598 |
1.07e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1067 TDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRvnntLSSQISRLQ-NIRNTIEETGNLAEQAR----AHVENT 1141
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR----LQLQADRHQeHIRARDSLIQSLATRLEldgfERGPFS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1142 ERLIE-----IASRELEKAKVAAANVSVTQPEstgdpnnmtllaeearklaERHKQEADDIVRVAKTAndtsteaynlLL 1216
Cdd:TIGR00606 389 ERQIKnfhtlVIERQEDEAKTAAQLCADLQSK-------------------ERLKQEQADEIRDEKKG----------LG 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1217 RTLagENQTafeiEELNRKYEQAKNISQDLEKQAArvheEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAENL 1296
Cdd:TIGR00606 440 RTI--ELKK----EILEKKQEELKFVIKELQQLEG----SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1297 EQLIDQKLKDyEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKG-------RDTLQEANDILNN 1369
Cdd:TIGR00606 510 KADLDRKLRK-LDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqlEDWLHSKSKEINQ 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1370 LKDFDRRVNDNKTAAEEalrkipaiNQTITEANEKTREAQQA-----LGSAAADATEAKNKAHEAERIASAVQKNATSTK 1444
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQ--------NKNHINNELESKEEQLSsyedkLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1445 AEA--------------------ERTF---AEVTDLDNEVNNMLK----QLQEAEKELKRKQDDADQDMMMAGMASQAAQ 1497
Cdd:TIGR00606 661 ATAvysqfitqltdenqsccpvcQRVFqteAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1498 EAEINARKAKNSVTSLLSII----NDLLEQLGQLDTVDLN-------------------KLNEIEGTLNKAKDEMKVSDL 1554
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIqrlkNDIEEQETLLGTIMPEeesakvcltdvtimerfqmELKDVERKIAQQAAKLQGSDL 820
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 145309326 1555 DRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPS 1598
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1043-1306 |
1.12e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1043 ADHRVKLqeLESLIaNLGTGDEMvtDQAFEDRLKEAEREVMDL---LREAQDVKDVDQNLMDRLQRVNNtlsSQISRLQN 1119
Cdd:PHA02562 149 APARRKL--VEDLL-DISVLSEM--DKLNKDKIRELNQQIQTLdmkIDHIQQQIKTYNKNIEEQRKKNG---ENIARKQN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1120 I----RNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANVS---------------------VTQPESTGdPN 1174
Cdd:PHA02562 221 KydelVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKskieqfqkvikmyekggvcptCTQQISEG-PD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1175 NMTLLAEEARKLAERHKQEADDIVRVAKTANDtsteaYNLLLRTlagenqtafeIEELNRKYEQAKNISQDLEKQAARVH 1254
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDE-----FNEQSKK----------LLELKNKISTNKQSLITLVDKAKKVK 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 1255 EEAKRAGDKAVEIYASVAQLSPlDSETLENEANNIKMEAENLeQLIDQKLKD 1306
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQD-ELDKIVKTKSELVKEKYHR-GIVTDLLKD 414
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1394-1497 |
1.21e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1394 INQTITEANEKTREAQQALGSAAADATEAKNkahEAERIASAVQKNATSTKAEAertfaeVTDLDNEVNNMLKQlqeAEK 1473
Cdd:cd06503 35 IAESLEEAEKAKEEAEELLAEYEEKLAEARA---EAQEIIEEARKEAEKIKEEI------LAEAKEEAERILEQ---AKA 102
|
90 100
....*....|....*....|....*.
gi 145309326 1474 ELKRKQDDADQDM--MMAGMASQAAQ 1497
Cdd:cd06503 103 EIEQEKEKALAELrkEVADLAVEAAE 128
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1073-1591 |
1.60e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1073 DRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNNTLSSQISR--LQNIRNTIEETGNLAEQARAHVENTERLIEIASR 1150
Cdd:PTZ00440 1254 DELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEkiLKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEA 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1151 ELEKAKVAAANVSVTQPESTGDpnnmtllaEEARKLAERH------KQEADDIVRVAKTANDTSTEAYNLLLR------- 1217
Cdd:PTZ00440 1334 KIEQAKEHKNKIYGSLEDKQID--------DEIKKIEQIKeeisnkRKEINKYLSNIKSNKEKCDLHVRNASRgkdkidf 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1218 -----TLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSET----------- 1281
Cdd:PTZ00440 1406 lnkheAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSILGKKTklekkkkeatn 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1282 ----LENEANNIKME----AENLEQLIDQK-LKDYEDLREDMRGKELEVKNLLEKGKTEQQTADqllaradaakalaeea 1352
Cdd:PTZ00440 1486 imddINGEHSIIKTKltksSEKLNQLNEQPnIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLN---------------- 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1353 akkgrdtlqeandiLNNLKDFDRRVndnKTAAEEALRKIPAINQtITEANektreaqqalgsaaaDATEAKNKAHEAERI 1432
Cdd:PTZ00440 1550 --------------ILNIKDEIETI---LNKAQDLMRDISKISK-IVENK---------------NLENLNDKEADYVKY 1596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1433 ASAVQKNATSTKAEAERTFAEVTDLDN------------EVNNMLKqLQEAEKELKRKQDDADQDM--MMAGMASQAAQE 1498
Cdd:PTZ00440 1597 LDNILKEKQLMEAEYKKLNEIYSDVDNiekelkkhkknyEIGLLEK-VIEINKNIKLYMDSTKESLnsLVNNFSSLFNNF 1675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1499 aEINARKAKNSVTSLLSIINDL----LEQLGQLDT---------VDLNKLNEI-------EGTLNKAKDEMK--VSDLDR 1556
Cdd:PTZ00440 1676 -YLNKYNINENLEKYKKKLNEIynefMESYNIIQEkmkevsnddVDYNEAKTLreeaqkeEVNLNNKEEEAKkyLNDIKK 1754
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 145309326 1557 KVS------------DLENEAKKQEAAIMDYNRDIEEIMKDIRNLED 1591
Cdd:PTZ00440 1755 QESfrfilymkekldELSKMCKQQYNIVDEGYNYIKKKIEYIKTLND 1801
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1446-1596 |
1.62e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.74 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1446 EAERTFAE---VTDLDnEVNNMLKQLQEAEKELKRKQDDADQdmmmagMASQAAQEAEiNARKAKNSVTSLLSIINDLLE 1522
Cdd:cd00176 18 EKEELLSStdyGDDLE-SVEALLKKHEALEAELAAHEERVEA------LNELGEQLIE-EGHPDAEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309326 1523 QLGQLdtvdlnkLNEIEGTLNKAKDEMKvsdLDRKVSDLEN--EAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:cd00176 90 ELREL-------AEERRQRLEEALDLQQ---FFRDADDLEQwlEEKEAALASEDLGKDLESVEELLKKHKELEEEL 155
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1102-1335 |
1.62e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.02 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1102 RLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKvaaanvsvtqpestgdpnnmTLLAE 1181
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTE--------------------ERLAE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1182 EARKLAERHKQeADDIVRVAKTANDtsteaynlllRTLAGENQtafeIEELNRKYEQAKNISQDLEKQ---AAR----VH 1254
Cdd:pfam00261 62 ALEKLEEAEKA-ADESERGRKVLEN----------RALKDEEK----MEILEAQLKEAKEIAEEADRKyeeVARklvvVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1255 EEAKRAGDKAVEIYASVAQLspldSETLENEANNIK-MEAEnleqliDQKLKDYEDLREDmrgkelEVKNLLEKGKTEQQ 1333
Cdd:pfam00261 127 GDLERAEERAELAESKIVEL----EEELKVVGNNLKsLEAS------EEKASEREDKYEE------QIRFLTEKLKEAET 190
|
..
gi 145309326 1334 TA 1335
Cdd:pfam00261 191 RA 192
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1229-1457 |
1.66e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1229 IEELNRKYEQAKNiSQDLEKQaaRVHEEAKRAGDKAVEIYASVAQLSPLDSETLEneANNIKMEAENLEQLIDQKLKdye 1308
Cdd:PRK09510 61 VEQYNRQQQQQKS-AKRAEEQ--RKKKEQQQAEELQQKQAAEQERLKQLEKERLA--AQEQKKQAEEAAKQAALKQK--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1309 dLREDMRGKELEVKNLleKGKTEQQTADQLLARADAAKALAEEAAKKGRDTlQEANdilnnlkdfdrrvndnKTAAEEAL 1388
Cdd:PRK09510 133 -QAEEAAAKAAAAAKA--KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA-AEAK----------------KKAEAEAA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1389 RKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAH-EAERIASAVQKNATSTKAEAERTFAEVTDL 1457
Cdd:PRK09510 193 AKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAaEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1366-1576 |
1.67e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.44 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1366 ILNNLKDFDRRVND--NKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERiasavQKNATST 1443
Cdd:cd22656 96 ILELIDDLADATDDeeLEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK-----ALKDLLT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1444 KAEAERTFAEVTDLDNEVNNM----LKQLQEAEKELKRKQDDADQDMmmagmasQAAQEAEINARKAKNSVTSLLSIIND 1519
Cdd:cd22656 171 DEGGAIARKEIKDLQKELEKLneeyAAKLKAKIDELKALIADDEAKL-------AAALRLIADLTAADTDLDNLLALIGP 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1520 LLEQLGQLDTVdlnkLNEIEGTLNKAKDemKVSDLDRKVSDLENEAKKQEAAIMDYN 1576
Cdd:cd22656 244 AIPALEKLQGA----WQAIATDLDSLKD--LLEDDISKIPAAILAKLELEKAIEKWN 294
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1438-1591 |
1.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1438 KNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMagmasQAAQEAEINARKAKNSVTSLLSII 1517
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1518 NDLLEQLGQLDTVdLNKLNEIEGTLNKAKDEMK-------------VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMK 1584
Cdd:COG4717 149 EELEERLEELREL-EEELEELEAELAELQEELEelleqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
....*..
gi 145309326 1585 DIRNLED 1591
Cdd:COG4717 228 ELEQLEN 234
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
341-389 |
2.20e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 2.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 341 PCDCNGR---SQECYFdpelyrstgHGGHCTnCQDNTDGAHCERCRENFFRL 389
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1131-1266 |
2.38e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1131 AEQARAHVENTERLIEIASRELEKAK------VAAANV---SVTQPESTGD---PNNMTLLAEEARKLAER-HKQEADDI 1197
Cdd:pfam05701 414 AEQAKAAASTVESRLEAVLKEIEAAKaseklaLAAIKAlqeSESSAESTNQedsPRGVTLSLEEYYELSKRaHEAEELAN 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309326 1198 VRVAKtANDTSTEAYNLLLRTLAgenqtafEIEELNRKYEQAKnisQDLEkqAArvHEEAKRA--GDKAVE 1266
Cdd:pfam05701 494 KRVAE-AVSQIEEAKESELRSLE-------KLEEVNREMEERK---EALK--IA--LEKAEKAkeGKLAAE 549
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1194-1335 |
2.89e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.67 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1194 ADDIVRVAKTANDTSTEAYNLLLRtLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDK----AVEIYA 1269
Cdd:cd22656 75 AGDIYNYAQNAGGTIDSYYAEILE-LIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKltdfENQTEK 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1270 SVAQLSPLD---SETLENEANNIkmEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTA 1335
Cdd:cd22656 154 DQTALETLEkalKDLLTDEGGAI--ARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1372-1582 |
3.47e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 44.20 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1372 DFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAAdateaknKAHEAERIASAVQKNATSTKAEAERTf 1451
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAA-------TAQSAAEAAEEGREAVEDAITAMDQI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1452 AEVTDldnEVNNMLKQLQEAEKELKRK----QDDADQDMMMAGMAS-QAAQ--EA---------EIN--ARKAKNSVTSL 1513
Cdd:smart00283 73 REVVE---EAVSAVEELEESSDEIGEIvsviDDIADQTNLLALNAAiEAARagEAgrgfavvadEVRklAERSAESAKEI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309326 1514 LSIINDLLEQLGQLDTVDLNKLNEIE---GTLNKAKDEMK-----VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEI 1582
Cdd:smart00283 150 ESLIKEIQEETNEAVAAMEESSSEVEegvELVEETGDALEeivdsVEEIADLVQEIAAATDEQAAGSEEVNAAIDEI 226
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1142-1591 |
4.31e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1142 ERLIEIASR----ELEKAKvaaanvsvtqpestgdpnNMTLLAEEARKLaERHKQEADDIVrvaktandtsteaynllLR 1217
Cdd:PRK04778 36 ERKQELENLpvndELEKVK------------------KLNLTGQSEEKF-EEWRQKWDEIV-----------------TN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1218 TLAGENQTAFEIEELNRKYE--QAKNISQDLEKQAARVHEEAKragdkavEIYASVAQLspldsetLENEANNikmeaen 1295
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKFRfrKAKHEINEIESLLDLIEEDIE-------QILEELQEL-------LESEEKN------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1296 lEQLIDQKLKDYEDLREDMRGK---------ELEVKnlLEKGKTEQQTADQLLARadaakalaeeaakkGrDTLqEANDI 1366
Cdd:PRK04778 139 -REEVEQLKDLYRELRKSLLANrfsfgpaldELEKQ--LENLEEEFSQFVELTES--------------G-DYV-EAREI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1367 LNNLKDfdrrvndnKTAA-EEALRKIPAInqtITEANEKTREAQQALGSAAADATEAKNKAheaeriasavqknatsTKA 1445
Cdd:PRK04778 200 LDQLEE--------ELAAlEQIMEEIPEL---LKELQTELPDQLQELKAGYRELVEEGYHL----------------DHL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1446 EAERTFAEVTDLDNEVNNMLKQLQ--EAEKELKRKQDDADQ--DMMmagmasqaaqEAEInarKAKNSVTSLLSIINDLL 1521
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERIDQlyDIL----------EREV---KARKYVEKNSDTLPDFL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1522 EQLGQ--------LDTVDLN----------------KLNEIEGTLNKAKDEMKvsdlDRKV--SDLENEAKKQEAAIMDY 1575
Cdd:PRK04778 320 EHAKEqnkelkeeIDRVKQSytlneselesvrqlekQLESLEKQYDEITERIA----EQEIaySELQEELEEILKQLEEI 395
|
490
....*....|....*.
gi 145309326 1576 NRDIEEIMKDIRNLED 1591
Cdd:PRK04778 396 EKEQEKLSEMLQGLRK 411
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
286-327 |
4.40e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 4.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 145309326 286 CKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRP 327
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
687-999 |
5.29e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 44.19 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 687 VESCTCPVGYGGQFCEMCLSG-YRRETPNLGPYS---PCVLCACNGHSETCDPETGVCNCRDNTAGPHCEKCSDGYY--G 760
Cdd:pfam03302 25 TENCKACSNDKREVCEECNSNnYLTPTSQCIDDCakiGNYYYTTNANNKKICKECTVANCKTCEDQGQCQACNDGFYksG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 761 DSTAGTSSDCQPCPCPGGSSCAVVPK----------TKEVVCTNCPTGTTGKRCELCDDGYFGdplgrngpVRLCRLCQC 830
Cdd:pfam03302 105 DACSPCHESCKTCSGGTASDCTECLTgkalrygndgTKGTCGEGCTTGTGAGACKTCGLTIDG--------TSYCSECAT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 831 SDNIDPNAV--GNCNRLTGECLKCiyNTAGFYCDRCKDGFF-------------GNPL--APNPADKCKACNCNLYGTMK 893
Cdd:pfam03302 177 ETEYPQNGVctSTAARATATCKAS--SVANGMCSSCANGYFrmnggcyettkfpGKSVceEANSGGTCQKEAPGYKLNNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 894 QQSSCNPVTGQCEclphvTGQDCGACDPGFynLQSGQGCERCDchalgSTNGQCDIRTGQCEC------QPGITGQHCER 967
Cdd:pfam03302 255 DLVTCSPGCKTCT-----SNTVCTTCMDGY--VKTSDSCTKCD-----SSCETCTGATTTCKTcatgyyKSGTGCVSCTS 322
|
330 340 350
....*....|....*....|....*....|....*
gi 145309326 968 CEVNHFGFGPEGCKPCDCHPEGSLSLQC---KDDG 999
Cdd:pfam03302 323 SESDNGITGVKGCLNCAPPSNNKGSVLCyliKDSG 357
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1452-1597 |
5.35e-04 |
|
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: 43.37 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1452 AEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQdmmmagmasQAAQEAEINAR--KAKNS--VTSLLSIINDLLEQLGQL 1527
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEE---------VEARIKKYEEQlgNVRNNkeYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1528 DTVDLNKLNEIEgTLNKAKDEMKvSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIrnlEDIRKTLP 1597
Cdd:COG1579 109 EDEILELMERIE-ELEEELAELE-AELAELEAELEEKKAELDEELAELEAELEELEAER---EELAAKIP 173
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1195-1589 |
5.64e-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: 45.04 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1195 DDIVRVAKTANDTSTEAYNLLlrTLAGENQTAFE-IEELNrkyeQAKNISQDLEKQAARVHEEAKRAGDKAVEI------ 1267
Cdd:TIGR01612 1960 DTLLDIFKKSQDLHKKEQDTL--NIIFENQQLYEkIQASN----ELKDTLSDLKYKKEKILNDVKLLLHKFDELnklscd 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1268 ---YASVAQLSPLDSetLENEANNIKMEAENL---------EQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTA 1335
Cdd:TIGR01612 2034 sqnYDTILELSKQDK--IKEKIDNYEKEKEKFgidfdvkamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSK 2111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1336 DQLLARADAAKALAEEAakkgRDTLQEANDILNNLKDFDRR--VNDNKTAAEEALRKIPAINQTITEANEKTREAQQALG 1413
Cdd:TIGR01612 2112 KKLKELTEAFNTEIKII----EDKIIEKNDLIDKLIEMRKEclLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIE 2187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1414 saaaDATEAKNKAHEAERIasavQKNATSTKAEAERTFAEVTdldNEVNNMLKQLQEAEKELKR---------KQDDAD- 1483
Cdd:TIGR01612 2188 ----DISDSLNDDIDALQI----KYNLNQTKKHMISILADAT---KDHNNLIEKEKEATKIINNltelftidfNNADADi 2256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1484 ---QDMMMAGMASQAAQEAE--------INARKAKNsvtslLSIIN----DLLEQLG---QLD----TVDLNKLNEIE-- 1539
Cdd:TIGR01612 2257 lhnNKIQIIYFNSELHKSIEsikklykkINAFKLLN-----ISHINekyfDISKEFDniiQLQkhklTENLNDLKEIDqy 2331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1540 -------------GTLNKAKDEMK-----VSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNL 1589
Cdd:TIGR01612 2332 isdkkniflhalnENTNFNFNALKeiyddIINRENKADEIENINNKENENIMQYIDTITKLTEKIQDI 2399
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1130-1599 |
5.65e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1130 LAEQARAHVENTERLIEIASRE-LEKAKVAAANVSVTQPEstgdpnnmtLLAEEARKLAERHKQEADDIVRVAKTANDTS 1208
Cdd:COG3064 31 AEQKAKEEAEEERLAELEAKRQaEEEAREAKAEAEQRAAE---------LAAEAAKKLAEAEKAAAEAEKKAAAEKAKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1209 TEAynlllrtlagENQTAFEieelnRKYEQAKNisQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANN 1288
Cdd:COG3064 102 KEA----------EAAAAAE-----KAAAAAEK--EKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1289 IKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLE-KGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDIL 1367
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAAlAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1368 NNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEkTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEA 1447
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV-VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1448 ERTFAEVTDLDNEVNNMLKQLQEAE-KELKRKQDDADQDMMMAGMASQAAQEAE------INARKAKNSVTSLLSIINDL 1520
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAaAAAAGAGALATGALGDALAAEAAGALLLgkladvEEAAGAGILAAAGGGGLLGL 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1521 LEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPSG 1599
Cdd:COG3064 404 RLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADLLL 482
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1043-1327 |
6.39e-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: 44.12 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1043 ADHRVKLQELESLIANLGtgDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDR-----------LQRVNNTLS 1111
Cdd:pfam07888 125 AAHEARIRELEEDIKTLT--QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslskeFQELRNSLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1112 SQISRLQNIRNTIEE-TGNLAEQARAHVENTERLIEIAS-RELekakvaaANVSVTQPESTGDpNNMTLLAEEARKLAER 1189
Cdd:pfam07888 203 QRDTQVLQLQDTITTlTQKLTTAHRKEAENEALLEELRSlQER-------LNASERKVEGLGE-ELSSMAAQRDRTQAEL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1190 HK---QEADDIVRVAKTandtsteayNLLLR----TLAGENQTAFEIEELNRkyEQAKNISQDLEKQAARVHEE----AK 1258
Cdd:pfam07888 275 HQarlQAAQLTLQLADA---------SLALRegraRWAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEErmerEK 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1259 RAGDKAVEIYASVAQLSPLDSETLENEAnNIKMEAENLEQLIDQKlkdyEDLREDMRgkELEVKnlLEK 1327
Cdd:pfam07888 344 LEVELGREKDCNRVQLSESRRELQELKA-SLRVAQKEKEQLQAEK----QELLEYIR--QLEQR--LET 403
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1458 |
6.61e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1038 VKDKVADHRVKLQELESLIANLgtgdemvtdQAFEDRLKEAEREV---MDLLrEAQDVKDVDQNLM--DRLQRVNNTLSS 1112
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSL---------NQRIRALRENLDELsrnMEML-NGQSVCPVCGTTLgeEKSNHIINHYNE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1113 QISRLQ-NIRNTIEETGNLAEQARAHVENTERLieiASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEearklAERHK 1191
Cdd:PRK01156 477 KKSRLEeKIREIEIEVKDIDEKIVDLKKRKEYL---ESEEINKSINEYNKIESARADLEDIKIKINELKD-----KHDKY 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1192 QEADDIVRVAKTAN-DTSTEAYNLLLRTLagenqTAFEIEELNRKYEQAKNISQDLEKqaaRVHEeakragdkaVEI-YA 1269
Cdd:PRK01156 549 EEIKNRYKSLKLEDlDSKRTSWLNALAVI-----SLIDIETNRSRSNEIKKQLNDLES---RLQE---------IEIgFP 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1270 SVAQLSPLDSETLENEANNI---KMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEkgkteqqtadqllaradaak 1346
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-------------------- 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1347 alaeeaakkgrdTLQEANDILNNLKDFDRRVNDNKT------AAEEALR-KIPAINQTITEANeKTREAQQALGSAAADA 1419
Cdd:PRK01156 672 ------------ITSRINDIEDNLKKSRKALDDAKAnrarleSTIEILRtRINELSDRINDIN-ETLESMKKIKKAIGDL 738
|
410 420 430
....*....|....*....|....*....|....*....
gi 145309326 1420 TEAKNkAHEAERIASAVQKNATSTKAEAERTFAEVTDLD 1458
Cdd:PRK01156 739 KRLRE-AFDKSGVPAMIRKSASQAMTSLTRKYLFEFNLD 776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1089-1303 |
6.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1089 AQDVKDVDQNLMDRLQRVNNTLSSQISRLQNirnTIEETGNLAEQARAHVENTERLIEIASRELEKAKvaaanvsvtqpe 1168
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAE------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1169 stgdpnnmtllaeeaRKLAERHKQEADDIVRVAKTANDTST-----EAYNL--------LLRTLAGENQTAfeIEELNRK 1235
Cdd:COG3883 79 ---------------AEIEERREELGERARALYRSGGSVSYldvllGSESFsdfldrlsALSKIADADADL--LEELKAD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309326 1236 YEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQK 1303
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1160-1438 |
6.80e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 43.43 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1160 ANVSVTQPESTGDPNN-MTLLAEEARKLAERhkqeADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQ 1238
Cdd:smart00283 10 AAGAEEQAEELEELAErMEELSASIEEVAAN----ADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1239 AKNISQDLEKQAARVHE--------------EAKRAGDkAVEIYASVAQlspldsetlE--NEANNIKMEAENLEQLIDQ 1302
Cdd:smart00283 86 LEESSDEIGEIVSVIDDiadqtnllalnaaiEAARAGE-AGRGFAVVAD---------EvrKLAERSAESAKEIESLIKE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1303 KLKDYEDLREDMRgkelEVKNLLEKGKTeqqtadqllaradaakalaeeaakKGRDTLQEANDILNNLKDFDRRVNDNKT 1382
Cdd:smart00283 156 IQEETNEAVAAME----ESSSEVEEGVE------------------------LVEETGDALEEIVDSVEEIADLVQEIAA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145309326 1383 AAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAknkAHEAERIASAVQK 1438
Cdd:smart00283 208 ATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEEL---SGLAEELDELVER 260
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1063-1309 |
7.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1063 DEMVTDQAFEDRLKEAEREVMDLLREAQDVKDvdqnlmdRLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTE 1142
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK-------KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1143 RLIEIASRELEKAKVAAANVSVTqpestgdpnnmtllAEEARKLAERHKQEADDIvrvaKTANDTSTEaynlllrtlagE 1222
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKE--------------AEEAKKAEELKKKEAEEK----KKAEELKKA-----------E 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1223 NQTAFEIEELNRKYEQAKNISQDLEKQaarvHEEAKRAGDKAVEIYASVAQLSPLDSETLENEannIKMEAENLEQLIDQ 1302
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDK 1798
|
....*..
gi 145309326 1303 KLKDYED 1309
Cdd:PTZ00121 1799 KIKDIFD 1805
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
1126-1507 |
8.08e-04 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 43.95 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1126 ETGNLAEQARAHVENTERLIEIASRELEKAkvaaanvsvtqpestgdpnnMTLLAEEARKLAERHKQEADDIVRVAKTAN 1205
Cdd:COG2770 266 EIGELARAFNRMADSLRESIEEAEEEEELA--------------------EAELARLLEALLELLLALLLLLLALLLLAA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1206 DTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENE 1285
Cdd:COG2770 326 AALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1286 ANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEAND 1365
Cdd:COG2770 406 ELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1366 ILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKA 1445
Cdd:COG2770 486 ALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAA 565
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309326 1446 EAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAK 1507
Cdd:COG2770 566 LLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGA 627
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1398-1450 |
8.79e-04 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 39.28 E-value: 8.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1398 ITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERT 1450
Cdd:pfam11839 3 VEELQSKADQAEQDAAAAQSAADSAKAKADEAAARANAAEAAAEEAQQAAEEA 55
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1361-1586 |
9.14e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1361 QEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIasavqkna 1440
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1441 tstkaeaeRTFAEVTDLDNEvnNMLKQLQEAEKELKRKQDDADQDMMMAG----MASQAAQEAEINARKAKNSVTSLLSI 1516
Cdd:pfam00261 80 --------RKVLENRALKDE--EKMEILEAQLKEAKEIAEEADRKYEEVArklvVVEGDLERAEERAELAESKIVELEEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1517 INDLLEQLGQL--------DTVDLNKlNEIEGTLNKAKD-EMKVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDI 1586
Cdd:pfam00261 150 LKVVGNNLKSLeaseekasEREDKYE-EQIRFLTEKLKEaETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1462-1596 |
9.80e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1462 NNMLKQLQEAEKELKRKQDDADQDMmmagmASQAAQ--------EAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDlN 1533
Cdd:cd22656 90 DSYYAEILELIDDLADATDDEELEE-----AKKTIKallddllkEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLE-K 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1534 KLNEIEGTLNKAKDEMKVSDLDRKVsdleneAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:cd22656 164 ALKDLLTDEGGAIARKEIKDLQKEL------EKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1053-1476 |
1.09e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1053 ESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLmDRLQRVNNTLSSQISRLQN--IRNTIEETGNL 1130
Cdd:COG5185 209 ESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL-EKLVEQNTDLRLEKLGENAesSKRLNENANNL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1131 AEQarahVENTERLIeiasRELEKAKVAAAnvsvtqpeSTGDPNNMTLLAEEARKLAERhKQEADdivrvakTANDTSTE 1210
Cdd:COG5185 288 IKQ----FENTKEKI----AEYTKSIDIKK--------ATESLEEQLAAAEAEQELEES-KRETE-------TGIQNLTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1211 AYNLLLRTLAgENQTA--------FEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIyasvaqlspldsetL 1282
Cdd:COG5185 344 EIEQGQESLT-ENLEAikeeieniVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEI--------------L 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1283 ENEANNIKMEAENLEQL---IDQKLKDYEdlredmrgkelEVKNLLEKGKTEQQTADQLLARADAAKalaeeaakkgrdt 1359
Cdd:COG5185 409 ATLEDTLKAADRQIEELqrqIEQATSSNE-----------EVSKLLNELISELNKVMREADEESQSR------------- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1360 LQEANDILN-----NLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTR----EAQQALGSAAADATEAKNKAHEAE 1430
Cdd:COG5185 465 LEEAYDEINrsvrsKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRskldQVAESLKDFMRARGYAHILALENL 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 145309326 1431 RIASAVQKNATST---KAEAERTFaeVTDLDNEVNNMLKQLQEAEKELK 1476
Cdd:COG5185 545 IPASELIQASNAKtdgQAANLRTA--VIDELTQYLSTIESQQAREDPIP 591
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1147-1537 |
1.09e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.47 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1147 IASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQTA 1226
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1227 FEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAENLEQLIDQKLKD 1306
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1307 YEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKkgrdtLQEANDILNNLKDFDRRVNDNKTAAEE 1386
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRP-----LRELLEVLERIAEGDLTVRIDVDSKDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1387 --ALRKipAINQTIteanEKTREAQQALGSAAADATEAknkAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNM 1464
Cdd:COG0840 237 igQLAD--AFNRMI----ENLRELVGQVRESAEQVASA---SEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEV 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309326 1465 LKQLQEaekelkrkqddadqdmmmagmASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVdLNKLNE 1537
Cdd:COG0840 308 AENAQQ---------------------AAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAET-IEELGE 358
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1067-1568 |
1.16e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1067 TDQAFEDRLKEAEREV--MDLLR----------EAQDvkdvdQNLMDR---LQRVNNTLSSQISRLQNIRNTIEETGNLA 1131
Cdd:pfam10174 114 TEENFRRLQSEHERQAkeLFLLRktleemelriETQK-----QTLGARdesIKKLLEMLQSKGLPKKSGEEDWERTRRIA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1132 EqARAHVENTERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTLLAEEARKLA--ERHKQEADDIVRVAKTANDTST 1209
Cdd:pfam10174 189 E-AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISslERNIRDLEDEVQMLKTNGLLHT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1210 EAYNLLLRTL-AGENQTAF---EIE----ELNRKYEQAKNISQDLE---------KQAARVHEEAKRAGDKAveiyasva 1272
Cdd:pfam10174 268 EDREEEIKQMeVYKSHSKFmknKIDqlkqELSKKESELLALQTKLEtltnqnsdcKQHIEVLKESLTAKEQR-------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1273 qlspldSETLENEANNIKMEAENLEQLIDQKLKDYEDLRE----------DMRgKELEVK----NLLEKgKTEqqtadql 1338
Cdd:pfam10174 340 ------AAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEekstlageirDLK-DMLDVKerkiNVLQK-KIE------- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1339 laradaakalaeeaakkgrdTLQEandilnNLKDFDRRVNDNK-----------------TAAEEALrkipAINQTITEA 1401
Cdd:pfam10174 405 --------------------NLQE------QLRDKDKQLAGLKervkslqtdssntdtalTTLEEAL----SEKERIIER 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1402 --NEKTREAQQALgsaaaDATEAKNKA-HEAERIASAVQKNATSTKAEAERTFAEVTDLDN---EVNNMLKQLqeaEKEL 1475
Cdd:pfam10174 455 lkEQREREDRERL-----EELESLKKEnKDLKEKVSALQPELTEKESSLIDLKEHASSLASsglKKDSKLKSL---EIAV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1476 KRKQDDAdqdmmmAGMASQ--AAQEAEINARkAKNSVTSLLSiindLLEQLGQLDTVDLNKLN-EIEGTLNKAKD-EMKV 1551
Cdd:pfam10174 527 EQKKEEC------SKLENQlkKAHNAEEAVR-TNPEINDRIR----LLEQEVARYKEESGKAQaEVERLLGILREvENEK 595
|
570
....*....|....*..
gi 145309326 1552 SDLDRKVSDLENEAKKQ 1568
Cdd:pfam10174 596 NDKDKKIAELESLTLRQ 612
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
1394-1484 |
1.26e-03 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 40.85 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1394 INQTITEANEKTREAQQALGSAAADATEAKNKAHE----AERIASAVQKNA-TSTKAEAERTFAEV-TDLDNEVNNMLKQ 1467
Cdd:TIGR01144 31 IADGLASAERAKKEAALAQKKAQVILKEAKDEAQEiienANKRGSEILEEAkAEAREEREKIKAQArAEIEAEKEQAREE 110
|
90 100
....*....|....*....|....*.
gi 145309326 1468 LQE---------AEKELKRKQDDADQ 1484
Cdd:TIGR01144 111 LRKqvadlsvlgAEKIIERNIDKQAQ 136
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1357-1527 |
1.48e-03 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 42.27 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1357 RDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTRE------------------AQQ----ALGS 1414
Cdd:smart00283 35 EEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEleessdeigeivsviddiADQtnllALNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1415 A--AADATEA------------------KNKAHEAERIASAVQKNATSTKAEAERTFAEV-----------------TDL 1457
Cdd:smart00283 115 AieAARAGEAgrgfavvadevrklaersAESAKEIESLIKEIQEETNEAVAAMEESSSEVeegvelveetgdaleeiVDS 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1458 DNEVNNMLKQLQEAEKELKRKQDDADQdmMMAGMAsQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQL 1527
Cdd:smart00283 195 VEEIADLVQEIAAATDEQAAGSEEVNA--AIDEIA-QVTQETAAMSEEISAAAEELSGLAEELDELVERF 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1214-1496 |
1.56e-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: 42.83 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1214 LLLRTLAGENQTAFEIEELNRKYEQaknISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSpldseTLENEANNIKMEA 1293
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQ---LQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1294 ENLEQLIDQKLKDYEDLREDMRGKELEVKNLLekgKTEQQTADQLlaradaakalaeeaakkgrdtlqEANDILN--NLK 1371
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELL---RALYRLGRQP-----------------------PLALLLSpeDFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1372 DFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKaheaeriasavQKNATSTKAEAERTF 1451
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-----------RAALEALKAERQKLL 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 145309326 1452 AEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAA 1496
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1067-1608 |
1.68e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1067 TDQAFEDRLKEAEREVMDLLR----EAQDVK-DVDQNLmdrlqrvnNTLSSQISRLQNIRNTIEETGNLAEQARAHVENT 1141
Cdd:PTZ00440 415 TLKAAEDVLKENSQKIADYALysnlEIIEIKkKYDEKI--------NELKKSINQLKTLISIMKSFYDLIISEKDSMDSK 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1142 ERLIEIASRELEKAKVAAANVSVTQPESTGDPNNMTllaeearklaerhkqeadDIVRVAKTANDTSTEaYNLLLRTLAG 1221
Cdd:PTZ00440 487 EKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFK------------------NIEDYYITIEGLKNE-IEGLIELIKY 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1222 ENQtafEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGD---KAVEIYASVAQLSPLDSETLEN-------------- 1284
Cdd:PTZ00440 548 YLQ---SIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDiisLNDEIDNIIQQIEELINEALFNkekfinekndlqek 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1285 -EANNIKMEAENLEQLIDQK---LKDYEDLREDMRGKElEVKNLLEKGKTEQQtadqllaradaakalaeeaakkgRDTL 1360
Cdd:PTZ00440 625 vKYILNKFYKGDLQELLDELshfLDDHKYLYHEAKSKE-DLQTLLNTSKNEYE-----------------------KLEF 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1361 QEANDILNNLKDFDRRVNDNKTAAEEALRK-IPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKN 1439
Cdd:PTZ00440 681 MKSDNIDNIIKNLKKELQNLLSLKENIIKKqLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNE 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1440 ATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRkqddadqdmmmagmasqaaqeaEINA-RKAKNSVTSLLSIIN 1518
Cdd:PTZ00440 761 FILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISN----------------------DINIlKENKKNNQDLLNSYN 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1519 DLLEQLGQLDTVDLNKLNEIegtLNKAKDEmkvsDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIRKTLPS 1598
Cdd:PTZ00440 819 ILIQKLEAHTEKNDEELKQL---LQKFPTE----DENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAINR 891
|
570
....*....|
gi 145309326 1599 GCFNTPSIEK 1608
Cdd:PTZ00440 892 SNSNKQLVEH 901
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
286-328 |
1.79e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 145309326 286 CKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPW 328
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1123-1255 |
1.80e-03 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 41.45 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1123 TIEETGNLAEQARAHVENTERLIEIASRELEKAkVAAANVSVTQPESTG------------------------DPNNMTL 1178
Cdd:cd11386 6 SIEEVAASADQVAETSQQAAELAEKGREAAEDA-INQMNQIDESVDEAVsaveeleessaeigeiveviddiaEQTNLLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1179 L-------------------AEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLRT---------LAGENQTAFE-- 1228
Cdd:cd11386 85 LnaaieaarageagrgfavvADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETseeveegveLVEETGRAFEei 164
|
170 180 190
....*....|....*....|....*....|
gi 145309326 1229 ---IEELNrkyEQAKNISQDLEKQAARVHE 1255
Cdd:cd11386 165 vasVEEVA---DGIQEISAATQEQSASTQE 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1038-1346 |
1.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1038 VKDKVADHRVKLQELESLIAN----LGTGD-----EMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRVNN 1108
Cdd:PRK02224 424 LREREAELEATLRTARERVEEaealLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1109 --TLSSQISRLQNIRNTIEEtgnLAEQARAHVENTERLIEiasrELEKAKVAAANVSVTQPEStgdpnnmtllAEEARKL 1186
Cdd:PRK02224 504 lvEAEDRIERLEERREDLEE---LIAERRETIEEKRERAE----ELRERAAELEAEAEEKREA----------AAEAEEE 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1187 AERHKQEADDIVRvAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAknisQDLEKQAaRVHEEAKRAGDKAVE 1266
Cdd:PRK02224 567 AEEAREEVAELNS-KLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL----AELNDER-RERLAEKRERKRELE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1267 iyasvaqlSPLDSETLEnEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAK 1346
Cdd:PRK02224 641 --------AEFDEARIE-EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| t_SNARE |
smart00397 |
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
1072-1155 |
1.87e-03 |
|
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".
Pssm-ID: 197699 [Multi-domain] Cd Length: 66 Bit Score: 38.33 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1072 EDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQrvnntlsSQISRLQNIRNtieetgnlaeqaraHVENTERLIEIASRE 1151
Cdd:smart00397 4 LAREEERDEELEQLEKSIQELKQIFLDMGTELE-------EQGEQLDRIED--------------NVDDADVNLKKANKR 62
|
....
gi 145309326 1152 LEKA 1155
Cdd:smart00397 63 LKKA 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1228-1535 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1228 EIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANNIKMEAenLEQLIDQKLKDY 1307
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA--LEEQLEELEAEL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1308 EDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEA 1387
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1388 LRKI-PAINQTITEANEKTREAQQALGSAAADATE--------AKNKAHEAE-RIASAVQKNAT------STKAEAERtf 1451
Cdd:COG4913 782 LNRAeEELERAMRAFNREWPAETADLDADLESLPEylalldrlEEDGLPEYEeRFKELLNENSIefvadlLSKLRRAI-- 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1452 AEVTDLDNEVNNMLKQLQ-EAEKELK---RKQDDAD----QDMMMAgmASQAAQEAEINARKAKNSVtsLLSIINDLLEQ 1523
Cdd:COG4913 860 REIKERIDPLNDSLKRIPfGPGRYLRleaRPRPDPEvrefRQELRA--VTSGASLFDEELSEARFAA--LKRLIERLRSE 935
|
330
....*....|..
gi 145309326 1524 LGQLDTVDLNKL 1535
Cdd:COG4913 936 EEESDRRWRARV 947
|
|
| V_AnPalA_UmRIM20_like |
cd09236 |
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ... |
1180-1336 |
2.06e-03 |
|
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.
Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 42.34 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1180 AEEAR--KLAERHKQEADDIVRVAKTANDTSTEAYNLLLrTLAGENQTA---FEIEELNRkyEQAKNISQDLEKQAARVH 1254
Cdd:cd09236 64 AEEIRqeDGLERIRASLDDVARLAASDRAILEEAMDILD-DEASEDESLrrkFGTDRWTR--PDSHEANPKLYTQAAEYE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1255 EEAKRAG--DKAV-----EIYASVAQL---------------SPLDSETLENEANNIKMEAENLEQLIDQKLKDYEDLRE 1312
Cdd:cd09236 141 GYLKQAGasDELVrrkldEWEDLIQILtgderdlenfvpssrRPSIPPELERHVRALRVSLEELDRLESRRRRKVERART 220
|
170 180 190
....*....|....*....|....*....|.
gi 145309326 1313 -----DMRGKELEVKNLLEKGK--TEQQTAD 1336
Cdd:cd09236 221 karadDIRPEILREAARLEREYpaTEVAPAH 251
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
1359-1468 |
2.16e-03 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 40.04 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1359 TLQE-ANDILNNLKDFdrrvndNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEaeRIASAVQ 1437
Cdd:pfam07464 24 TIKEnTENLVDQLKQV------QKSLQEELKKASGEAEEALKELNTKIVETADKLSEANPEVVQKANELQE--KFQSGVQ 95
|
90 100 110
....*....|....*....|....*....|.
gi 145309326 1438 KNATSTKAEAERTFAEVTDLDNEVNNMLKQL 1468
Cdd:pfam07464 96 SLVTESQKLAKSISENSQGATEKLQKATKQA 126
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1452 |
2.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1191 KQEADDIVRVAKTANDTSTEAYNLLLRTLAGENQTAFEIEELNRKYEQAKnisQDLEKQAARVHEEAKRAGDKAVEIYAS 1270
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1271 VAQLSPLD----SETLE--------------------NEANNIKMEAENLEQLIDQKLKDYEDLREDMRGKelevKNLLE 1326
Cdd:COG3883 99 GGSVSYLDvllgSESFSdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1327 KGKTEQQTAdqllaradaakalaeeaakkgrdtLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTR 1406
Cdd:COG3883 175 AQQAEQEAL------------------------LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 145309326 1407 EAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFA 1452
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1418-1603 |
2.42e-03 |
|
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: 41.45 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1418 DATEAKNKAHEAERiaSAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRkqddaDQDMMMAGMAS--QA 1495
Cdd:COG1579 20 DRLEHRLKELPAEL--AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----YEEQLGNVRNNkeYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1496 AQEAEINARKAKNSVTSllsiiNDLLEQLGQLDTVDlNKLNEIEGTLNKAKDEmkvsdLDRKVSDLENEAKKQEAAIMDY 1575
Cdd:COG1579 93 ALQKEIESLKRRISDLE-----DEILELMERIEELE-EELAELEAELAELEAE-----LEEKKAELDEELAELEAELEEL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 145309326 1576 NRDIEEIMKDI-RNL----EDIRKTLP------------SGCFNT 1603
Cdd:COG1579 162 EAEREELAAKIpPELlalyERIRKRKNglavvpveggacGGCFME 206
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1234-1593 |
2.42e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1234 RKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEiYAsvaqlspldsetlENEANNIKMEAENLEQLID----QKLKDYED 1309
Cdd:COG3064 19 EQAEAEKRAAAEAEQKAKEEAEEERLAELEAKR-QA-------------EEEAREAKAEAEQRAAELAaeaaKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1310 LREDMRgKELEVKNLLEKGKTEQQTADQllaradaakalaeeaakkgRDTLQEANdilnnlkdfdRRVNDNKTAAEEALR 1389
Cdd:COG3064 85 AAAEAE-KKAAAEKAKAAKEAEAAAAAE-------------------KAAAAAEK----------EKAEEAKRKAEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1390 KipainqtitEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQ 1469
Cdd:COG3064 135 R---------KAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1470 EAEKELKRKQDDADQdmmMAGMASQAAQEAEINARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEM 1549
Cdd:COG3064 206 AAAAAAADAALLALA---VAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVA 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 145309326 1550 KVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLEDIR 1593
Cdd:COG3064 283 AALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGA 326
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1377-1571 |
2.69e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1377 VNDNKTAAEEaLRkipaiNQTITEA----NEKTREAQQALGSAAAdateaknkahEAERIASAVQKNATStKAEAERTfa 1452
Cdd:NF041483 147 VNENVAWAEQ-LR-----ARTESQArrllDESRAEAEQALAAARA----------EAERLAEEARQRLGS-EAESARA-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1453 evtdldnevnnmlkqlqEAEKELKRKQDDADQdmmMAGMASQAAQEAEINARKAKNSVTSLlsiINDLLEQLGQLDTVDL 1532
Cdd:NF041483 208 -----------------EAEAILRRARKDAER---LLNAASTQAQEATDHAEQLRSSTAAE---SDQARRQAAELSRAAE 264
|
170 180 190
....*....|....*....|....*....|....*....
gi 145309326 1533 NKLNEIEGTLNKAKDEMkvsdlDRKVSDLENEAKKQEAA 1571
Cdd:NF041483 265 QRMQEAEEALREARAEA-----EKVVAEAKEAAAKQLAS 298
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1385-1484 |
2.98e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1385 EEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNK-AHEAERIASAVQKnATSTKAEAERTFAEVTDLDNEVNN 1463
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyERELVLHAEDIKA-LQALREELNELKAEIAELKAEAES 82
|
90 100 110
....*....|....*....|....*....|....*
gi 145309326 1464 MLKQLQEAEK--------------ELKRKQDDADQ 1484
Cdd:pfam07926 83 AKAELEESEEsweeqkkelekelsELEKRIEDLNE 117
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1046-1596 |
3.21e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1046 RVKL----QELEslianlgtgdEMVTDqaFEDRLKEAEREVMDLLRE----AQDVKDVDQNLMD------RLQRVNNTLS 1111
Cdd:pfam01576 63 RARLaarkQELE----------EILHE--LESRLEEEEERSQQLQNEkkkmQQHIQDLEEQLDEeeaarqKLQLEKVTTE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1112 SQISRLQNIRNTIEETGNLAEQARAHVEntERLIEIASR---ELEKAKvaaanvsvtqpestgdpnNMTLLaeearklae 1188
Cdd:pfam01576 131 AKIKKLEEDILLLEDQNSKLSKERKLLE--ERISEFTSNlaeEEEKAK------------------SLSKL--------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1189 RHKQEAddivrvaktandtsteaynlllrtlagenqTAFEIEELNRKYEQAKnisQDLEKQAARVHEEAKRAGDKAVEIY 1268
Cdd:pfam01576 182 KNKHEA------------------------------MISDLEERLKKEEKGR---QELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1269 ASVAQLspldsetlenEANNIKMEAE------NLEQLIDQKLKDYEDLREdMRGKELEVKNLLEKGKTEQQTADQLLara 1342
Cdd:pfam01576 229 AQIAEL----------RAQLAKKEEElqaalaRLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQR--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1343 daakalaeeaakkgRDTLQEANDILNNLKDfdrrvNDNKTAAEEALR-----KIPAINQTItEANEKTREAQ-QALGSAA 1416
Cdd:pfam01576 295 --------------RDLGEELEALKTELED-----TLDTTAAQQELRskreqEVTELKKAL-EEETRSHEAQlQEMRQKH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1417 ADATEAKNKAHE-AERIASAVQKNATSTKAEaertfaevtdlDNEVNNMLKQLQEAEKELKRKQDDADqdmmmagmasqa 1495
Cdd:pfam01576 355 TQALEELTEQLEqAKRNKANLEKAKQALESE-----------NAELQAELRTLQQAKQDSEHKRKKLE------------ 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1496 AQEAEINARKAKNSVTSllsiiNDLLEQLGQLDtvdlNKLNEIEGTLNKAkdEMKVSDLDRKVSDLENEAKKQEAAIMDY 1575
Cdd:pfam01576 412 GQLQELQARLSESERQR-----AELAEKLSKLQ----SELESVSSLLNEA--EGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
570 580
....*....|....*....|.
gi 145309326 1576 NRDIEEIMKDIRNLEDIRKTL 1596
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSL 501
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1228-1335 |
3.39e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1228 EIEELNRKYEQAKNISQDLEKQAARVHEE----AKRAGDKAVEIYASVAQLSPlDSETLENEANNIKMEAEnLEQLIDQK 1303
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEksklEKALKDLQKEQGAKKDVKSN-LKEISDLEEKMAALKSD-LEKTLNAS 211
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 145309326 1304 LKDYEDLRED---MRGKELEVKNLLEKGKTE-----QQTA 1335
Cdd:pfam15294 212 TALQKSLEEDlasTKHELLKVQEQLEMAEKElekkfQQTA 251
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1046-1527 |
3.77e-03 |
|
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: 42.04 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1046 RVKLQELESLIANLgTGDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMDRLQRV-------NNTLSSQISRLQ 1118
Cdd:pfam05557 1 RAELIESKARLSQL-QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLekreaeaEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1119 NIRNTIEETGNLAEQARAHVENTERLI-----EIAS--RELEKAKVAaanVSVTQPEstgdpnNMTLlaEEARKLAERHK 1191
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVIsclknELSElrRQIQRAELE---LQSTNSE------LEEL--QERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1192 QEADDIVrvaktandtstEAYNLLLRTLAGENQTAFEIEELNRKYEQ----AKNISQ------DLEKQAARVHEEAKRAg 1261
Cdd:pfam05557 149 SEAEQLR-----------QNLEKQQSSLAEAEQRIKELEFEIQSQEQdseiVKNSKSelaripELEKELERLREHNKHL- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1262 dkaveiyasvaqlspldSETLENeaNNI-KMEAENLEqlidQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTAdqlla 1340
Cdd:pfam05557 217 -----------------NENIEN--KLLlKEEVEDLK----RKLEREEKYREEAATLELEKEKLEQELQSWVKLA----- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1341 radaakalaeeaakkgrdtlQEANDILNNLKDFDRRV----NDNKTAAEEalrkIPAINQTITEANEKTREAQQALGSAA 1416
Cdd:pfam05557 269 --------------------QDTGLNLRSPEDLSRRIeqlqQREIVLKEE----NSSLTSSARQLEKARRELEQELAQYL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1417 ADATEAKNKAHEAERIASAVQK-NATSTKaeaERTF--AEVTDLDNEVNN------MLKQLQEAEKELKRKQDDA----- 1482
Cdd:pfam05557 325 KKIEDLNKKLKRHKALVRRLQRrVLLLTK---ERDGyrAILESYDKELTMsnyspqLLERIEEAEDMTQKMQAHNeemea 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 145309326 1483 --DQDMMMAGMASQAAQ--EAEINARKAKNS----------VTSLLSIINDLLEQLGQL 1527
Cdd:pfam05557 402 qlSVAEEELGGYKQQAQtlERELQALRQQESladpsyskeeVDSLRRKLETLELERQRL 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1365-1608 |
3.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1365 DILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALgsaaADATEAKNKAHEAERIASAVQKNatstK 1444
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGS----K 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1445 AEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQE-AEINARKAKnsvtsLLSIINDLLEQ 1523
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElREIEKRLSR-----LEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1524 LGQLDTvDLNKLNEIEGtlnkakdemKVSDLDRKVSDLENEAKKqeaaimdynrdIEEIMKDIRNLEDIRKTLpsGCFNT 1603
Cdd:PRK03918 330 IKELEE-KEERLEELKK---------KLKELEKRLEELEERHEL-----------YEEAKAKKEELERLKKRL--TGLTP 386
|
....*
gi 145309326 1604 PSIEK 1608
Cdd:PRK03918 387 EKLEK 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1116-1316 |
3.90e-03 |
|
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: 40.68 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1116 RLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAKVAAANvsvtqpestgdpnnmtlLAEEARKLAERHKQEAD 1195
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-----------------LEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1196 DIVRV-AKTANDTSTEAYNLLLRtlagenqtafEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL 1274
Cdd:COG1579 74 RIKKYeEQLGNVRNNKEYEALQK----------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145309326 1275 SP-LDSET--LENEANNIKMEAENLEQLIDQKLKD-YEDLREDMRG 1316
Cdd:COG1579 144 KAeLDEELaeLEAELEELEAEREELAAKIPPELLAlYERIRKRKNG 189
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1364-1484 |
3.91e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.93 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1364 NDILNNLKDFDRRVNDN----KTAAEEalrkipaINQTITEANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKN 1439
Cdd:COG0840 245 NRMIENLRELVGQVRESaeqvASASEE-------LAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAEL 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 145309326 1440 ATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQ 1484
Cdd:COG0840 318 AEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQE 362
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1266-1572 |
4.03e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1266 EIYASVAQLSPLDSETLENEANnikmeAENLEQLIDQKLKDYE---DLREDMRGKELEVKNLLEKGKTEQQTADQLLARA 1342
Cdd:COG5278 87 EIDELLAELRSLTADNPEQQAR-----LDELEALIDQWLAELEqviALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1343 DAAKALAEEAAKKGRDTLQEANDILNNLKDFDRRVNDNKTAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEA 1422
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1423 KNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEIN 1502
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1503 ARKAKNSVTSLLSIINDLLEQLGQLDTVDLNKLNEIEGTLNKAKDEMKVSDLDRKVSDLENEAKKQEAAI 1572
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1429-1574 |
4.37e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1429 AERIASAVQK----------NATSTKAEAERTFAEVTDLDNEVNNMLK-------QLQEAEKELKRKQDDADQDmmmagm 1491
Cdd:COG0497 221 AEKLREALQEalealsggegGALDLLGQALRALERLAEYDPSLAELAErlesaliELEEAASELRRYLDSLEFD------ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1492 aSQAAQEAE-----IN--ARKAKNSVTSLLSIINDLLEQLGQLDTVDlNKLNEIEGTLNKAKDEM-----KVSDLDRKVs 1559
Cdd:COG0497 295 -PERLEEVEerlalLRrlARKYGVTVEELLAYAEELRAELAELENSD-ERLEELEAELAEAEAELleaaeKLSAARKKA- 371
|
170
....*....|....*
gi 145309326 1560 dleneAKKQEAAIMD 1574
Cdd:COG0497 372 -----AKKLEKAVTA 381
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1380-1507 |
4.45e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.40 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1380 NKTAAE-EALRKIPAINQTITEANEKTREAQQAlgsAAADATEAKNKAHEAERIASAVQKNATSTKAEAERTFAEVtdld 1458
Cdd:COG2268 220 NREAEEaELEQEREIETARIAEAEAELAKKKAE---ERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREI---- 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145309326 1459 nevnnmlkQLQEAEKELKRKQDDADQDMMMAGMASQAAQEAEINARKAK 1507
Cdd:COG2268 293 --------ELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1466-1573 |
4.46e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.20 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1466 KQLQEAEKeLKRKQDDAD----------QDMMMagmaSQAAQE-AEINARKAKNSVTSLLSIINDLLEQLGQLdTVDLNK 1534
Cdd:pfam10473 4 KQLHVLEK-LKESERKADslkdkvenleRELEM----SEENQElAILEAENSKAEVETLKAEIEEMAQNLRDL-ELDLVT 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 145309326 1535 LNEIEGTLNKAKDEM--KVSDLDRKVSDLENEAKKQEAAIM 1573
Cdd:pfam10473 78 LRSEKENLTKELQKKqeRVSELESLNSSLENLLEEKEQEKV 118
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1286-1327 |
5.17e-03 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 37.34 E-value: 5.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145309326 1286 ANNIKMEAENLEQLIDQKLKDYEDL----------REDmrgKELEVKNLLEK 1327
Cdd:cd22301 4 LKNIKKEAENLAKEIEDKMKRIEDLekriqdlnkrKED---KANQLARLEKQ 52
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
342-388 |
5.66e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.14 E-value: 5.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 145309326 342 CDCNGR---SQECYFDpelyrstghGGHCTnCQDNTDGAHCERCRENFFR 388
Cdd:smart00180 1 CDCDPGgsaSGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1361-1469 |
6.29e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1361 QEANDILNNLKDFDRRVNDNK-------TAAEEALRKIPAINQTITEANEKTREAQQALGSAAADATEAKNKAHEAeriA 1433
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQadlaaaqTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLAT---A 323
|
90 100 110
....*....|....*....|....*....|....*.
gi 145309326 1434 SAVQKNATSTKAEAErtfAEVTDLDNEVNNMLKQLQ 1469
Cdd:TIGR04320 324 QAALANAEARLAKAK---EALANLNADLAKKQAALD 356
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1097-1596 |
7.40e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1097 QNLMD---RLQRVNNTLSSQISRLQNIRNTIEETGNLAEQARAHVENTERLIEIASRELEKAK-VAAANVSVTQPESTGD 1172
Cdd:PTZ00440 522 KNIEDyyiTIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKdIISLNDEIDNIIQQIE 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1173 PnnmtlLAEEARKLAERHKQEADDIVRVAKTANDTSTEAYNLLLrtlagENQTAFEIEELNRKYEQAKNIsQDLEKqaar 1252
Cdd:PTZ00440 602 E-----LINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQEL-----LDELSHFLDDHKYLYHEAKSK-EDLQT---- 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1253 VHEEAKRAGDKAVEI-YASVAQLSP-LDSET---LENEANNIKMEAENLEQLI----DQKLKDYEDLREDMRGKELEvKN 1323
Cdd:PTZ00440 667 LLNTSKNEYEKLEFMkSDNIDNIIKnLKKELqnlLSLKENIIKKQLNNIEQDIsnslNQYTIKYNDLKSSIEEYKEE-EE 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1324 LLEKGKteqqtadqllaradaakalaeeaakkgRDTLQEANDILNNLKDFDRRVNDNKTAAEEALR-------KIPAINQ 1396
Cdd:PTZ00440 746 KLEVYK---------------------------HQIINRKNEFILHLYENDKDLPDGKNTYEEFLQykdtilnKENKISN 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1397 TITEANEKTREAQQALGSAAaDATEaKNKAHEAERIASAVQ-------KNATSTKAEAERTFAEVTDLdneVNNMLKQLQ 1469
Cdd:PTZ00440 799 DINILKENKKNNQDLLNSYN-ILIQ-KLEAHTEKNDEELKQllqkfptEDENLNLKELEKEFNENNQI---VDNIIKDIE 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1470 EAEKELkrkqdDADQDMMMAGMASQAAQEaeiNARKAKNSVTSLLSIINDLLEQLGQLDTVD-------LNKLNEIEGTL 1542
Cdd:PTZ00440 874 NMNKNI-----NIIKTLNIAINRSNSNKQ---LVEHLLNNKIDLKNKLEQHMKIINTDNIIQkneklnlLNNLNKEKEKI 945
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 145309326 1543 NKAKDEMKVSDLDRKVSDLENEAKKQEAAIMDYNR-DIEEIMKDIRNLEDIRKTL 1596
Cdd:PTZ00440 946 EKQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGtHLEKLDKEKDEWEHFKSEI 1000
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1049-1254 |
7.40e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1049 LQELESLIANLGTGDEMVTDQAFEDRLKEAEREVMDLLREAQDVKDVDQNLMD-----------RLQRVNntlssqiSRL 1117
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEeghpdaeeiqeRLEELN-------QRW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1118 QNIRNTIEETGN-LAEQARAHVENTE-RLIEIASRELEKAkvaaanvsVTQPESTGDPnnmtllaEEARKLAERHKQEAD 1195
Cdd:cd00176 89 EELRELAEERRQrLEEALDLQQFFRDaDDLEQWLEEKEAA--------LASEDLGKDL-------ESVEELLKKHKELEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1196 DIVRVAKTANDTSTEAYNLL-LRTLAGENQTAFEIEELNRKYEQAKNISQDLEKQAARVH 1254
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELLeEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1292-1596 |
8.71e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.94 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1292 EAENLEQLI------DQKL----KDYEDLREDMRGKELEVKNLLEKGKTEQQTADQllaradaakalaeeaakkGRDTLQ 1361
Cdd:pfam09728 2 AARELMQLLnkldspEEKLaalcKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQ------------------LQSELS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1362 EAN---DILNNL-KDFDRRvndNKTAAEEALRKIpainqtiTEANEKTREAQQALGSAAADaTEAKNKAHEAERIASAVQ 1437
Cdd:pfam09728 64 KAIlakSKLEKLcRELQKQ---NKKLKEESKKLA-------KEEEEKRKELSEKFQSTLKD-IQDKMEEKSEKNNKLREE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1438 KNATSTKAeaeRTFAEVTDL-DNEVNNMLKQlqeaeKELKRKQDDADqdMMMAGMASQA-AQEAEIN-ARKAKNSVTSLL 1514
Cdd:pfam09728 133 NEELREKL---KSLIEQYELrELHFEKLLKT-----KELEVQLAEAK--LQQATEEEEKkAQEKEVAkARELKAQVQTLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1515 SIINDLLEQL-------GQL-DTvdLNKLNEIEGTLNKAKDEMkvsdlDRKVSDLENEA----KKQEA---AIMD----- 1574
Cdd:pfam09728 203 ETEKELREQLnlyvekfEEFqDT--LNKSNEVFTTFKKEMEKM-----SKKIKKLEKENltwkRKWEKsnkALLEmaeer 275
|
330 340
....*....|....*....|....
gi 145309326 1575 --YNRDIEEIMKDIRNLEDIRKTL 1596
Cdd:pfam09728 276 qkLKEELEKLQKKLEKLENLCRAL 299
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1234-1475 |
9.48e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1234 RKYEQAKNISQDLEKQAARVHEEAK------RAGDKAVEIYasvaqlspldsETLENEannikmeaenLEQLIDQKLKDY 1307
Cdd:pfam15619 11 HKIKELQNELAELQSKLEELRKENRllkrlqKRQEKALGKY-----------EGTESE----------LPQLIARHNEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1308 EDLREDMRGKELEVKNLLEKGK-TEQQtadqllaradaakalaeeaakkgrdtLQEANDILNNLKDfdrrVNDNKTAAE- 1385
Cdd:pfam15619 70 RVLRERLRRLQEKERDLERKLKeKEAE--------------------------LLRLRDQLKRLEK----LSEDKNLAEr 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1386 -EALRKIPAINQTITEANEKTREAQQALgsaaadatEAKNKAHeAERIASAVQKnatsTKAeaerTFAEVTDLDNEVNNM 1464
Cdd:pfam15619 120 eELQKKLEQLEAKLEDKDEKIQDLERKL--------ELENKSF-RRQLAAEKKK----HKE----AQEEVKILQEEIERL 182
|
250
....*....|.
gi 145309326 1465 LKQLQEAEKEL 1475
Cdd:pfam15619 183 QQKLKEKEREL 193
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1131-1440 |
9.89e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1131 AEQARAHVE-NTERLI-EIASRElEKAKVAAANVSVTQPEStgdpnnmtlLAEEARKLAERHKQEADDIVRVAKTANDTS 1208
Cdd:PRK05035 448 AEEAKARFEaRQARLErEKAARE-ARHKKAAEARAAKDKDA---------VAAALARVKAKKAAATQPIVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1209 TEAYNLLLRTLAGENQTAfeieelnrkyeQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLSPLDSETLENEANN 1288
Cdd:PRK05035 518 AVIAAREARKAQARARQA-----------EKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1289 IKMEAENLEQLIDQKLKDYEDLREDMRGKELEVKNLLEKGKTEQQTADQLLARADaakalaeeaakkgrdtlqeandiln 1368
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPV------------------------- 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309326 1369 nlkdfdrrvnDNKTAAEEAlrkipAInqtiteANEKTREAQQALGSAAADATEAKNKAHEAERIASAVQKNA 1440
Cdd:PRK05035 642 ----------DPRKAAVAA-----AI------ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1444-1590 |
9.91e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1444 KAEAERTFAE-------VTDLDNEVNNMLKQLQ-EAEK-----ELKRKQDDADQDMMMAGMASQAAQEAEINARKAKNSv 1510
Cdd:COG1196 174 KEEAERKLEAteenlerLEDILGELERQLEPLErQAEKaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309326 1511 TSLLSIINDLLEQLGQLDTVDLnKLNEIEGTLNKAKDEmkVSDLDRKVSDLENEAKKQEAAIMDYNRDIEEIMKDIRNLE 1590
Cdd:COG1196 253 AELEELEAELAELEAELEELRL-ELEELELELEEAQAE--EYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
|
| |
