|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
31-265 |
4.83e-108 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 343.41 E-value: 4.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 31 CYPATGDLLVGREanLKASSTCGLRRREPYCIVSHLQEEKKCFQCDSRRPYDpqsnpvSHRIENVITTFKPHRKkSWWQS 110
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 111 ENGKSD---VYLQLDLEAEFHFTHLIMTFKTFRPAAMLIERSADFGRSWQVYRYFANDCESIFpGISQDSLR--KVDDVI 185
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 186 CESRYSDIEPSTEGEVIFRVL--DPAIRIEDpYSPRIQNQLKITNLRLNLTKLHTLGDNLLDSRPEIKeKYYYAMYELVV 263
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 528517572 264 RG 265
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-265 |
5.22e-84 |
|
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: 275.39 E-value: 5.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 25 GCTHGSCYPATGDLLVGREanLKASSTCGLRRREPYCI-VSHLQEEKKCFQCDSRRPYDpqsnpvSHRIENVITTFKPHr 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 104 KKSWWQSENGKS---DVYLQLDLEAEFHFTHLIMTFKTFRPAAMLIERSaDFGRSWQVYRYFANDCESIFPGISQDSLRK 180
Cdd:smart00136 72 NPTWWQSEPLSNgpqNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 181 V--DDVICESRYSDIEPSTEGEVIFRVLDPAIRIED-PYSPRIQNQLKITNLRLNLTKLHTLGDNLLDSRPEIKEKYYYA 257
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 528517572 258 MYELVVRG 265
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1723-1794 |
2.80e-39 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 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. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 140.66 E-value: 2.80e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1723 AKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1221-1778 |
9.74e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1221 RAFERRFKELEDMLAQARDIVNARNA-------TAEAVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASNAL 1293
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAedakkaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1294 STLEReAKELNLNADQLnRQLDILKNSNFLGAYDSIRASYNKSRDAEHRSNRSttdtpstvsQSADTRKKTErligQKRD 1373
Cdd:PTZ00121 1227 EAVKK-AEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---------RKADELKKAE----EKKK 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1374 DFNRKNAANKRTLTDLNAKVQnlDLKKINEkvcgAPGDAQCVDSPCGGAGCRDDEGKRRcgglncngavavADTALDRSK 1453
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAE--EAKKADE----AKKKAEEAKKKADAAKKKAEEAKKA------------AEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1454 HAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAaLEKASDTKNKVDHSNNDLRDLIKQirqflMQEGADPDSIEAVA 1533
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELKKA-----AAAKKKADEAKKKA 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1534 NRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQnDVRKAEQLLLDAKKARnKAEGVKNTAESVKKALNDASRA 1613
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1614 QAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANE 1693
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1694 AKEILDG---ELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDE------AKGLLKDAQDKLQRLAELEKDYEENQKVLEG 1764
Cdd:PTZ00121 1586 AKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
570
....*....|....
gi 528517572 1765 KARQLDglEDKMKA 1778
Cdd:PTZ00121 1666 EAKKAE--EDKKKA 1677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1786 |
2.32e-17 |
|
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: 88.96 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1201 ATRTKALTDRAKELQTTGLTRaferRFKELEDMLAQARDIVNA----RNATAEAVTTLMGMIEVLRAQIGETTDTLNQQE 1276
Cdd:TIGR02168 212 AERYKELKAELRELELALLVL----RLEELREELEELQEELKEaeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1277 GDLtavqdsnYEASNALSTLEREAKELNLNADQLNRQLDILKnsnflgayDSIRASYNKSRDAEHRSNRSTTDTPSTVSQ 1356
Cdd:TIGR02168 288 KEL-------YALANEISRLEQQKQILRERLANLERQLEELE--------AQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1357 SADTRKKTERLIGQK-------------RDDFNRKNAANKRTLTDLNAKVQNLD--LKKINEKVcgapgdaQCVDSPCGG 1421
Cdd:TIGR02168 353 LESLEAELEELEAELeelesrleeleeqLETLRSKVAQLELQIASLNNEIERLEarLERLEDRR-------ERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1422 AGCRDDEGKRRCGGLNCNGAVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRA------QAALEKAS 1495
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslerlQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1496 DTKNKVDHSNNDLRDLIKQIRQFL-----------------MQ----EGADP--DSIEAVAN----RV--LELSIpASPK 1546
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELIsvdegyeaaieaalggrLQavvvENLNAakKAIAFLKQnelgRVtfLPLDS-IKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1547 QIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLD----------------------------------------- 1585
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggvitgg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1586 AKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEA 1665
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1666 LKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKL 1745
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528517572 1746 QRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQ 1786
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1466-1786 |
1.36e-16 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 82.27 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1466 VEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegadpdsieavanrvlelsipasp 1545
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE---------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 kqIRHLADEIKDRVKSLSNV-DAILEQtqndvrkaeqllldAKKARNKAEGVKNtaesVKKALNDASRAQAAAEKAIQKA 1624
Cdd:COG1340 62 --LREKRDELNEKVKELKEErDELNEK--------------LNELREELDELRK----ELAELNKAGGSIDKLRKEIERL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1625 KNDIgltqnqlaQIQSETSASERDLndaVDRLGDLERQIEALKTKR-ANNSLDAARAEetATMARDKANEAKEILdGELS 1703
Cdd:COG1340 122 EWRQ--------QTEVLSPEEEKEL---VEKIKELEKELEKAKKALeKNEKLKELRAE--LKELRKEAEEIHKKI-KELA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1704 DKyrtvqglMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKvlegKARQLDGLEDKMKAILNAI 1783
Cdd:COG1340 188 EE-------AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK----ELRELRKELKKLRKKQRAL 256
|
...
gi 528517572 1784 NRQ 1786
Cdd:COG1340 257 KRE 259
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
767-812 |
4.03e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 4.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 767 CECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGFGPSGC 812
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
766-813 |
5.05e-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: 65.07 E-value: 5.05e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 766 ACECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGF--GPSGCK 813
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
815-863 |
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: 63.91 E-value: 1.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFPNCRPCQC 863
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1258-1782 |
1.94e-12 |
|
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: 72.84 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1258 IEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASnaLSTLEREAKELNLNADQLNRQLDILK------NSNFLGAYDSIRA 1331
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQeqarnqNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1332 SYNKSRDAEHRSNRSTTDTPS------TVSQSADTRKKTERligqkrDDFNRKNA----ANKRTLTDLNAKVQNLDLKKi 1401
Cdd:pfam15921 325 TVSQLRSELREAKRMYEDKIEelekqlVLANSELTEARTER------DQFSQESGnlddQLQKLLADLHKREKELSLEK- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1402 nekvcgapgdaqcvdspcggagcrddEGKRRCGGLNCNGAVAVadtaldrsKHAEKELDKAMGVVEELFKQVADAKTKAQ 1481
Cdd:pfam15921 398 --------------------------EQNKRLWDRDTGNSITI--------DHLRRELDDRNMEVQRLEALLKAMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1482 EAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVANRVLELS---------IPASPKQIRHLA 1552
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTaslqekeraIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1553 DEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAA--AEKA-IQKAKNDIG 1629
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqVEKAqLEKEINDRR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1630 LTQNQLAQIQSETSASERDLNdavDRLGDLERQiealKTKRANNSLDAARAEETATMARDK-ANEAKEILD--GELSDKY 1706
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELE---ARVSDLELE----KVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNelNSLSEDY 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1707 RTVQGLMDNKAKTMQDAKHKaeqlrdeAKGLLKDAQDKLQRLAELEKDYEEN-----------QKVLEGKARQLDGLEDK 1775
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSdghamkvamgmQKQITAKRGQIDALQSK 749
|
570
....*....|.
gi 528517572 1776 MK----AILNA 1782
Cdd:pfam15921 750 IQfleeAMTNA 760
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
767-812 |
2.40e-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: 63.14 E-value: 2.40e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 767 CECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGFG---PSGC 812
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1139-1178 |
1.31e-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: 60.83 E-value: 1.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528517572 1139 CDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSG 1178
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
394-451 |
2.48e-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: 2.48e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 394 CDCDPDGSKnGGVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLSASDPRGC 451
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1139-1183 |
9.98e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.98e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 1139 CDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSG-TFPDC 1183
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
815-856 |
3.23e-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: 56.98 E-value: 3.23e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFP 856
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
815-856 |
3.67e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.67e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFP 856
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-905 |
3.85e-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: 56.98 E-value: 3.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 860 PCQCNGHAD---ECHQRTGACLnCRSNTAGDKCERCANGYYGNPVLGLG 905
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1138-1187 |
4.59e-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: 56.59 E-value: 4.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1138 ACDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSGTFPDCKPCH 1187
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
393-452 |
1.21e-09 |
|
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: 55.44 E-value: 1.21e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 393 ACDCDPDGSKNGgVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLsASDPRGCQ 452
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGT--------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1091-1139 |
1.31e-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: 55.44 E-value: 1.31e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 1091 CACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDPRVLCRAC 1139
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-900 |
1.73e-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: 55.05 E-value: 1.73e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517572 861 CQCNGHA---DECHQRTGACLnCRSNTAGDKCERCANGYYGNP 900
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-504 |
5.62e-09 |
|
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: 53.51 E-value: 5.62e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528517572 453 PCKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHWALSHDTSGCR 504
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1778 |
6.11e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.38 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQ-----EAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegadpdSI 1529
Cdd:NF041483 92 AERELRDARAQTQRILQEHAEHQARLQaelhtEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRA----------RT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1530 EAVANRVL-------ELSIPASPKQIRHLADEIKDRVKS-----LSNVDAILEQTQNDVRK---------------AEQL 1582
Cdd:NF041483 162 ESQARRLLdesraeaEQALAAARAEAERLAEEARQRLGSeaesaRAEAEAILRRARKDAERllnaastqaqeatdhAEQL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1583 ----LLDAKKARNKAEGVKNTAESVKKALNDASR-AQAAAEKAIQKAKNDIGltqNQLAQIQSETSASERDLNDAVDRL- 1656
Cdd:NF041483 242 rsstAAESDQARRQAAELSRAAEQRMQEAEEALReARAEAEKVVAEAKEAAA---KQLASAESANEQRTRTAKEEIARLv 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1657 GDLERQIEALKTKrANNSLDAARAE------ETATMARDKANE------------AKEILDGELSDKYRTVQGLMDNKAK 1718
Cdd:NF041483 319 GEATKEAEALKAE-AEQALADARAEaeklvaEAAEKARTVAAEdtaaqlakaartAEEVLTKASEDAKATTRAAAEEAER 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 1719 TMQDAKHKAEQLRDEAkgllKDAQDKLQRLAELE-KDYEENQKVLEGKARQLDGLEDKMKA 1778
Cdd:NF041483 398 IRREAEAEADRLRGEA----ADQAEQLKGAAKDDtKEYRAKTVELQEEARRLRGEAEQLRA 454
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
506-544 |
1.59e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 1.59e-08
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
394-451 |
1.70e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 394 CDCDPDGSKNGgVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLSasdPRGC 451
Cdd:smart00180 1 CDCDPGGSASG-TCDPDT--------GQCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1090-1132 |
1.78e-08 |
|
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: 51.97 E-value: 1.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517572 1090 PCACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDP 1132
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1445-1794 |
2.63e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1445 ADTALDRSKH-AEKELDKAMGVVEELF----KQVADAKTKAQ----EAKDRAQAALEKASDTKNKVdhsnndlRDLIKQI 1515
Cdd:NF041483 715 AEETLGSARAeADQERERAREQSEELLasarKRVEEAQAEAQrlveEADRRATELVSAAEQTAQQV-------RDSVAGL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 RQFLMQEGADPDSI-EAVANRVlelsipaspkqiRHLADEIKDRVKSlsnvDAILEQTqndvRKAEQLLLDAKKARNKAE 1594
Cdd:NF041483 788 QEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRS----DAYAERE----RASEDANRLRREAQEETE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1595 GVKNTAE-SVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDlnDAVDRLGDLERQIEAL---KTKR 1670
Cdd:NF041483 848 AAKALAErTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARE--DANRIRSDAAAQADRLigeATSE 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1671 ANNSLDAARAE------ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDK 1744
Cdd:NF041483 926 AERLTAEARAEaerlrdEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAE 1005
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1745 LQRL-----AELEKDYEENQKvlEGKARQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:NF041483 1006 AERLrtearEEADRTLDEARK--DANKRRSEAAEQADTLITEAAAEADQLTAKAQ 1058
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1034-1088 |
3.49e-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: 51.20 E-value: 3.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNLA--SGQGC 1088
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
506-544 |
5.45e-08 |
|
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: 50.82 E-value: 5.45e-08
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-499 |
5.48e-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: 50.81 E-value: 5.48e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 454 CKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHWALSHD 499
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1451-1752 |
6.83e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.91 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1451 RSKHAEK---ELDKAMGVVEELFkqvadakTKAQE-AKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLmqEGADP 1526
Cdd:NF041483 355 RTVAAEDtaaQLAKAARTAEEVL-------TKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQL--KGAAK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 DSIEAVANRVLELSIPA-----SPKQIRHLADEIKDRVKSLSNVDAIlEQTQNDVRKAEQLLldaKKARNKAEGVKNTA- 1600
Cdd:NF041483 426 DDTKEYRAKTVELQEEArrlrgEAEQLRAEAVAEGERIRGEARREAV-QQIEEAARTAEELL---TKAKADADELRSTAt 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1601 ---ESVK-KALNDASRAQAAAEKAIQKAKNDIG-LTQNQLAQIQSETSASERDlndAVDRLGDLERQIEAlktKRANNSL 1675
Cdd:NF041483 502 aesERVRtEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERA---ARELREETERAIAA---RQAEAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1676 DAAR-----------AEETATMARD-------KANEAKEILDGELSDKYRTVQglmdnkaktmQDAKHKAEQLRDEAkgl 1737
Cdd:NF041483 576 ELTRlhteaeerltaAEEALADARAeaerirrEAAEETERLRTEAAERIRTLQ----------AQAEQEAERLRTEA--- 642
|
330
....*....|....*
gi 528517572 1738 lkdAQDKLQRLAELE 1752
Cdd:NF041483 643 ---AADASAARAEGE 654
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1034-1089 |
1.68e-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: 49.27 E-value: 1.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNLAS-GQGCE 1089
Cdd:cd00055 2 CDCNGHGSLSGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1091-1132 |
1.78e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 1.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 1091 CACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDP 1132
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1748 |
2.79e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.99 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEelfKQVADAKTKAQE--AKDRAqAALEKASDTKNKV-DHSNNDLRDLIK-------QIRQflmqega 1524
Cdd:NF041483 332 AEQALADARAEAE---KLVAEAAEKARTvaAEDTA-AQLAKAARTAEEVlTKASEDAKATTRaaaeeaeRIRR------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1525 dpdSIEAVANRvlelsipaspkqIRHLADEIKDRVKSLSNVD-----AILEQTQNDVRK----AEQLLLDAKkarnkAEG 1595
Cdd:NF041483 401 ---EAEAEADR------------LRGEAADQAEQLKGAAKDDtkeyrAKTVELQEEARRlrgeAEQLRAEAV-----AEG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1596 VKNTAESVKKALNDASRAQAAAEKAIQKAKNDigltQNQLAqiQSETSASERDLNDAVDRLGDLERQI-EALKTKRANNS 1674
Cdd:NF041483 461 ERIRGEARREAVQQIEEAARTAEELLTKAKAD----ADELR--STATAESERVRTEAIERATTLRRQAeETLERTRAEAE 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528517572 1675 LDAARAEETATMARDKANEAKEILDGELSdkyRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRL 1748
Cdd:NF041483 535 RLRAEAEEQAEEVRAAAERAARELREETE---RAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERI 605
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1034-1088 |
3.37e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNlASGQGC 1088
Cdd:smart00180 1 CDCDPGGSASGTCDPD--------TGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
982-1027 |
4.09e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 4.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 982 CRCSNNIDLSDpeSCDKRTGQCLkCLYNTEGPDCSVCRSGYYGDAS 1027
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-903 |
4.40e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 4.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 861 CQCN--GHADE-CHQRTGACLnCRSNTAGDKCERCANGYYGNPVLG 903
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
981-1030 |
8.00e-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: 8.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 981 PCRCSNNIDLSDpeSCDKRTGQCLkCLYNTEGPDCSVCRSGYYGDASRRN 1030
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-494 |
1.08e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517572 454 CKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHW 494
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1441-1659 |
1.18e-06 |
|
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: 51.90 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDhsnndlrdLIKQIrqflm 1520
Cdd:smart00283 37 VAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVS--------VIDDI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1521 qegADPD-------SIEA------------VANRVlelsipaspkqiRHLAD-------EIKDRVKSL----SNVDAILE 1570
Cdd:smart00283 104 ---ADQTnllalnaAIEAarageagrgfavVADEV------------RKLAErsaesakEIESLIKEIqeetNEAVAAME 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLLLDAKKARNK-AEGVKNTAESVKKaLNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDL 1649
Cdd:smart00283 169 ESSSEVEEGVELVEETGDALEEiVDSVEEIADLVQE-IAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEEL 247
|
250
....*....|
gi 528517572 1650 NDAVDRLGDL 1659
Cdd:smart00283 248 SGLAEELDEL 257
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
506-544 |
1.81e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 1.81e-06
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
267-319 |
3.04e-06 |
|
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: 45.81 E-value: 3.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 267 CFCYGHAS---ECAPiegirddiegmVHGRCVCKHNTKGLNCEQCDDFYNDLPWRP 319
Cdd:cd00055 2 CDCNGHGSlsgQCDP-----------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1544-1657 |
1.04e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.60 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1544 SPKQIRHLADEIKDRvksLSNVDAILEQTQNDVRKAEQLLLDAK----KARNKAEGVKNTAESVKK-ALNDASRAQAAAE 1618
Cdd:NF012221 1669 SGKQLADAKQRHVDN---QQKVKDAVAKSEAGVAQGEQNQANAEqdidDAKADAEKRKDDALAKQNeAQQAESDANAAAN 1745
|
90 100 110
....*....|....*....|....*....|....*....
gi 528517572 1619 KAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLG 1657
Cdd:NF012221 1746 DAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNRQG 1784
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
331-383 |
2.48e-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: 43.11 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 331 CNCNGH---SNQCHFDmavylatgnisGGVCDnCLHNTMGSNCESCKPFYYQDPTR 383
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
331-382 |
3.32e-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: 42.73 E-value: 3.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 331 CNCNGH---SNQCHFdmavylatgniSGGVCDnCLHNTMGSNCESCKPFYYQDPT 382
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1571-1748 |
7.11e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 45.01 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLlldakkarnkaegVKNTAESVKKALNDASRAQAAaeKAIQKAKNDIgltQNQLAQIQSetSASErdln 1650
Cdd:cd13769 2 QLSELIQKAQEA-------------INNLAQQVQKQLGLQNPEEVV--NTLKEQSDNF---ANNLQEVSS--SLKE---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1651 DAVDRLGDLERQIEALKTKRANNSLDAARAEETatmaRDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKhkaEQL 1730
Cdd:cd13769 58 EAKKKQGEVEEAWNEFKTKLSETVPELRKSLPV----EEKAQELQAKLQSGLQTLVTESQKLAKAISENSQKAQ---EEL 130
|
170
....*....|....*...
gi 528517572 1731 RDEAKGLLKDAQDKLQRL 1748
Cdd:cd13769 131 QKATKQAYDIAVEAAQNL 148
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
982-1025 |
9.54e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 528517572 982 CRCsnNIDLSDPESCDKRTGQCLkCLYNTEGPDCSVCRSGYYGD 1025
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1680-1794 |
7.42e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AEETATMARDKA------NEAKEILDgELSDKYRTVQ---GLMDNKAKTMQDAKHK-AEQLRDEAKGLLKDAQDKLQRLA 1749
Cdd:smart00787 150 DENLEGLKEDYKllmkelELLNSIKP-KLRDRKDALEeelRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 528517572 1750 ELEKDYEENQKVLEGKArqldgleDKMKAILNAINRQIQIYNTCQ 1794
Cdd:smart00787 229 ELEEELQELESKIEDLT-------NKKSELNTEIAEAEKKLEQCR 266
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
290-322 |
1.34e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|...
gi 528517572 290 VHGRCVCKHNTKGLNCEQCDDFYNDLPWRPAEG 322
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
331-384 |
1.61e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 331 CNCNG---HSNQCHFDmavylatgnisGGVCDnCLHNTMGSNCESCKPFYYQDPTRD 384
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
910-980 |
1.66e-03 |
|
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: 38.10 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 910 PCPCPEGPNSGrhfaASCYQDNrsqqVVCNCNQGYTGtvkrsagavlnrPRCDECAPGYFGDPSKPGGqCQ 980
Cdd:cd00055 1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTG------------RRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
290-317 |
4.09e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 4.09e-03
10 20
....*....|....*....|....*...
gi 528517572 290 VHGRCVCKHNTKGLNCEQCDDFYNDLPW 317
Cdd:smart00180 16 DTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
911-979 |
4.82e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 4.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 911 CPCPEGPNSGrhfaASCYQdnrsQQVVCNCNQGYTGtvkrsagavlnrPRCDECAPGYFGDPSKPGGQC 979
Cdd:pfam00053 1 CDCNPHGSLS----DTCDP----ETGQCLCKPGVTG------------RHCDRCKPGYYGLPSDPPQGC 49
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1709-1788 |
7.55e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.05 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1709 VQGLMDNkaktMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVL-----EGKARQLDGLEDKMKAILNAI 1783
Cdd:COG2825 31 VQRILQE----SPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLseeerQKKERELQKKQQELQRKQQEA 106
|
....*
gi 528517572 1784 NRQIQ 1788
Cdd:COG2825 107 QQDLQ 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
31-265 |
4.83e-108 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 343.41 E-value: 4.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 31 CYPATGDLLVGREanLKASSTCGLRRREPYCIVSHLQEEKKCFQCDSRRPYDpqsnpvSHRIENVITTFKPHRKkSWWQS 110
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 111 ENGKSD---VYLQLDLEAEFHFTHLIMTFKTFRPAAMLIERSADFGRSWQVYRYFANDCESIFpGISQDSLR--KVDDVI 185
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 186 CESRYSDIEPSTEGEVIFRVL--DPAIRIEDpYSPRIQNQLKITNLRLNLTKLHTLGDNLLDSRPEIKeKYYYAMYELVV 263
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 528517572 264 RG 265
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-265 |
5.22e-84 |
|
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: 275.39 E-value: 5.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 25 GCTHGSCYPATGDLLVGREanLKASSTCGLRRREPYCI-VSHLQEEKKCFQCDSRRPYDpqsnpvSHRIENVITTFKPHr 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 104 KKSWWQSENGKS---DVYLQLDLEAEFHFTHLIMTFKTFRPAAMLIERSaDFGRSWQVYRYFANDCESIFPGISQDSLRK 180
Cdd:smart00136 72 NPTWWQSEPLSNgpqNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 181 V--DDVICESRYSDIEPSTEGEVIFRVLDPAIRIED-PYSPRIQNQLKITNLRLNLTKLHTLGDNLLDSRPEIKEKYYYA 257
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 528517572 258 MYELVVRG 265
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1723-1794 |
2.80e-39 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 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. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 140.66 E-value: 2.80e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1723 AKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1722-1793 |
7.47e-24 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 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. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 96.39 E-value: 7.47e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1722 DAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTC 1793
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1725-1793 |
1.04e-20 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components 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. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 87.33 E-value: 1.04e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1725 HKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTC 1793
Cdd:cd22295 2 DRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1221-1778 |
9.74e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1221 RAFERRFKELEDMLAQARDIVNARNA-------TAEAVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASNAL 1293
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAedakkaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1294 STLEReAKELNLNADQLnRQLDILKNSNFLGAYDSIRASYNKSRDAEHRSNRSttdtpstvsQSADTRKKTErligQKRD 1373
Cdd:PTZ00121 1227 EAVKK-AEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---------RKADELKKAE----EKKK 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1374 DFNRKNAANKRTLTDLNAKVQnlDLKKINEkvcgAPGDAQCVDSPCGGAGCRDDEGKRRcgglncngavavADTALDRSK 1453
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAE--EAKKADE----AKKKAEEAKKKADAAKKKAEEAKKA------------AEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1454 HAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAaLEKASDTKNKVDHSNNDLRDLIKQirqflMQEGADPDSIEAVA 1533
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELKKA-----AAAKKKADEAKKKA 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1534 NRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQnDVRKAEQLLLDAKKARnKAEGVKNTAESVKKALNDASRA 1613
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1614 QAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANE 1693
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1694 AKEILDG---ELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDE------AKGLLKDAQDKLQRLAELEKDYEENQKVLEG 1764
Cdd:PTZ00121 1586 AKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
570
....*....|....
gi 528517572 1765 KARQLDglEDKMKA 1778
Cdd:PTZ00121 1666 EAKKAE--EDKKKA 1677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1786 |
2.32e-17 |
|
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: 88.96 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1201 ATRTKALTDRAKELQTTGLTRaferRFKELEDMLAQARDIVNA----RNATAEAVTTLMGMIEVLRAQIGETTDTLNQQE 1276
Cdd:TIGR02168 212 AERYKELKAELRELELALLVL----RLEELREELEELQEELKEaeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1277 GDLtavqdsnYEASNALSTLEREAKELNLNADQLNRQLDILKnsnflgayDSIRASYNKSRDAEHRSNRSTTDTPSTVSQ 1356
Cdd:TIGR02168 288 KEL-------YALANEISRLEQQKQILRERLANLERQLEELE--------AQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1357 SADTRKKTERLIGQK-------------RDDFNRKNAANKRTLTDLNAKVQNLD--LKKINEKVcgapgdaQCVDSPCGG 1421
Cdd:TIGR02168 353 LESLEAELEELEAELeelesrleeleeqLETLRSKVAQLELQIASLNNEIERLEarLERLEDRR-------ERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1422 AGCRDDEGKRRCGGLNCNGAVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRA------QAALEKAS 1495
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslerlQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1496 DTKNKVDHSNNDLRDLIKQIRQFL-----------------MQ----EGADP--DSIEAVAN----RV--LELSIpASPK 1546
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELIsvdegyeaaieaalggrLQavvvENLNAakKAIAFLKQnelgRVtfLPLDS-IKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1547 QIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLD----------------------------------------- 1585
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggvitgg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1586 AKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEA 1665
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1666 LKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKL 1745
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528517572 1746 QRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQ 1786
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1466-1786 |
1.36e-16 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 82.27 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1466 VEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegadpdsieavanrvlelsipasp 1545
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE---------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 kqIRHLADEIKDRVKSLSNV-DAILEQtqndvrkaeqllldAKKARNKAEGVKNtaesVKKALNDASRAQAAAEKAIQKA 1624
Cdd:COG1340 62 --LREKRDELNEKVKELKEErDELNEK--------------LNELREELDELRK----ELAELNKAGGSIDKLRKEIERL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1625 KNDIgltqnqlaQIQSETSASERDLndaVDRLGDLERQIEALKTKR-ANNSLDAARAEetATMARDKANEAKEILdGELS 1703
Cdd:COG1340 122 EWRQ--------QTEVLSPEEEKEL---VEKIKELEKELEKAKKALeKNEKLKELRAE--LKELRKEAEEIHKKI-KELA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1704 DKyrtvqglMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKvlegKARQLDGLEDKMKAILNAI 1783
Cdd:COG1340 188 EE-------AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK----ELRELRKELKKLRKKQRAL 256
|
...
gi 528517572 1784 NRQ 1786
Cdd:COG1340 257 KRE 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1198-1785 |
3.00e-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: 82.03 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1198 QDLATRTKALTDRAKELQT--TGLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQQ 1275
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1276 EGDLTAVQDSNYEASNALSTLEREAKELNLnaDQLNRQLDILKnsnflGAYDSIRASYNKSRDAEHRSNRSTTDTPSTVS 1355
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQ-----EELERLEEALEELREELEEAEQALDAAERELA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1356 QSADTRKKTERLIGQKRDDFN--RKNAANKRTLTDLNAKVQNL-----DLKKINEKVCGAPGDAQCVDS----------- 1417
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEgvKALLKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVVVENlnaakkaiafl 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1418 -----------PCGGAGCRDDEGKRRCGGLNCNGAVAVA---------------------------DTALDRSKH----- 1454
Cdd:TIGR02168 566 kqnelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAkdlvkfdpklrkalsyllggvlvvddlDNALELAKKlrpgy 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 ----AEKELDKAMGVV------------------EELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDhsnnDLRDLI 1512
Cdd:TIGR02168 646 rivtLDGDLVRPGGVItggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELE----QLRKEL 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1513 KQIRQFLMQEGADPDSIEAVANRVLElsipaspkQIRHLADEIKDRVKSLSNVDAILEQTQN----DVRKAEQLLLDAKK 1588
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEE--------RIAQLSKELTELEAEIEELEERLEEAEEelaeAEAEIEELEAQIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1589 ARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKT 1668
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1669 KRanNSLDAARAEETATMARdkANEAKEILDGELSDKYRTVQGLMDNkaktMQDAKHKAEQLRDEAKGLLKDAQDKLQRL 1748
Cdd:TIGR02168 874 EL--EALLNERASLEEALAL--LRSELEELSEELRELESKRSELRRE----LEELREKLAQLELRLEGLEVRIDNLQERL 945
|
650 660 670
....*....|....*....|....*....|....*...
gi 528517572 1749 AELEKDYEENQKVLE-GKARQLDGLEDKMKAILNAINR 1785
Cdd:TIGR02168 946 SEEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1575-1788 |
6.73e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1575 DVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKN-------DIGLTQNQLAQIQSETSASER 1647
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1648 DLNDAVDRLGDLER--------------QIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLM 1713
Cdd:COG1196 303 DIARLEERRRELEErleeleeelaeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEEL 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1714 DNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1724-1793 |
8.49e-15 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It 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. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 70.72 E-value: 8.49e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1724 KHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTC 1793
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
767-812 |
4.03e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 4.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 767 CECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGFGPSGC 812
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1203-1788 |
4.89e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1203 RTKALtdRAKELQTTGLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAV 1282
Cdd:COG1196 209 AEKAE--RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1283 QDSNYEASNALSTLERE-------AKELNLNADQLNRQLDILKNSnfLGAYDSIRASYNKSRDAEHRSNRSTTDTPSTVS 1355
Cdd:COG1196 287 QAEEYELLAELARLEQDiarleerRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1356 QSADTRKKTERLIGQKRDDFNRKNAANKRTLTDLNAKVQNLDLKKINEKVcgapgdaqcvdspcggagcRDDEGKRRcgg 1435
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------------------RLERLEEE--- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1436 lncngavavADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQI 1515
Cdd:COG1196 423 ---------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 RQFLMQEGADPDSIEAVANRVLelsIPASPKQIRHLADEIKDRVK--------SLSNVDAILEQTQNDVRKAEQLLLDAK 1587
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGVEAAyeaaleaaLAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1588 KAR------NKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDigLTQNQLAQIQSETSASERDLNDAVDRLGDLER 1661
Cdd:COG1196 571 AGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYY--VLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1662 QIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDA 1741
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 528517572 1742 QDKLQRLAELEKDYEENQKVLEGKARQLDGLED--KMKAILNAINRQIQ 1788
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDleELERELERLEREIE 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1221-1788 |
1.30e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1221 RAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQQEgDLTAVQDSNYEASNAlstleREA 1300
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEA-----KKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1301 KELNLNADQLNRQLDILKNSnflgAYDSIRASYNKSRDAEHRSNRSTTdtpSTVSQSADTRKKTERligQKRDDFNRKNA 1380
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEA---AEEKAEAAEKKKEEA---KKKADAAKKKA 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1381 ANKRTLTDLNAKVQnlDLKKINEKVCGAPGDAQCVDSPCGGAG--CRDDEGKRRcgglncngavAVADTALDRSKHAEKE 1458
Cdd:PTZ00121 1388 EEKKKADEAKKKAE--EDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKK----------AEEAKKADEAKKKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1459 LDKAmgvvEELFKQvADAKTKAQEAKDRAQAAlEKASDTKNKVDHSNNDLRDLIKQIRQflmQEGADPDSIEAVANRVLE 1538
Cdd:PTZ00121 1456 AKKA----EEAKKK-AEEAKKADEAKKKAEEA-KKADEAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1539 LSIPASPKQirhlADEIKDrvkslsnvdAILEQTQNDVRKAEQLlldaKKA--RNKAEGVKNTAESVKKALNDASRAQAA 1616
Cdd:PTZ00121 1527 AKKAEEAKK----ADEAKK---------AEEKKKADELKKAEEL----KKAeeKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1617 AEKAIQKAKNDIG---------LTQNQLAQIQSETSASERDLNDAVDRLGDLE----RQIEALKTKRANNSLdaaRAEET 1683
Cdd:PTZ00121 1590 EEARIEEVMKLYEeekkmkaeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKKAEEENKI---KAAEE 1666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1684 ATMARDKANEAKEILDGELSDKYRTVQGLMDNKA--------KTMQDAKHKAEQLRDE-------AKGLLKDAQDKLQRL 1748
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkaeelkKKEAEEKKKAEELKKAeeenkikAEEAKKEAEEDKKKA 1746
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 528517572 1749 AELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1455-1788 |
2.79e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQEAKDR---AQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQ-----EGADP 1526
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerlEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 DSIEAVANRV--------LELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGvkn 1598
Cdd:TIGR02168 776 ELAEAEAEIEeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE--- 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1599 TAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRAnnslDAA 1678
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA----QLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1679 RAEETATMardKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGL-------LKDAQDKLQRLAEL 1751
Cdd:TIGR02168 929 LRLEGLEV---RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFL 1005
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 528517572 1752 EKDYEEnqkVLEGKARQLDGLED-------KMKAILNAINRQIQ 1788
Cdd:TIGR02168 1006 TAQKED---LTEAKETLEEAIEEidreareRFKDTFDQVNENFQ 1046
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
766-813 |
5.05e-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: 65.07 E-value: 5.05e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 766 ACECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGF--GPSGCK 813
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1368-1781 |
8.93e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1368 IGQKRDDFNRKNAANKRTLTDlnakvQNLDLKKINEKVCGAPGDAQCVDSpcggagcRDDEGKRRCGGLNcnGAVAVADT 1447
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEE-------RAEELREEAAELE--SELEEARE 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1448 ALDRSKHAEKELDKAMgvvEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIR--QFLMQEGAD 1525
Cdd:PRK02224 378 AVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaEALLEAGKC 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1526 P------------DSIEAVANRVLELSipASPKQIRHLADEIK---DRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKA- 1589
Cdd:PRK02224 455 PecgqpvegsphvETIEEDRERVEELE--AELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETi 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1590 ---RNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERdLNDAVDRLGDLERQIEAL 1666
Cdd:PRK02224 533 eekRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERL 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1667 KTKRannsldAARAEetatmardKANEAKEILDgELSDKYRTVQGLMDnkaktmQDAKHKAEQLRDEAKGLLKDAQDKLQ 1746
Cdd:PRK02224 612 REKR------EALAE--------LNDERRERLA-EKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLD 670
|
410 420 430
....*....|....*....|....*....|....*
gi 528517572 1747 RLAELEKDYEENQKVLEGKARQLDGLEDKMKAILN 1781
Cdd:PRK02224 671 ELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
815-863 |
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: 63.91 E-value: 1.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFPNCRPCQC 863
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1441-1785 |
1.79e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDR-SKHAEK--ELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDtknkVDHSNNDLRDlikqirq 1517
Cdd:PRK02224 232 ARETRDEADEVlEEHEERreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE----LEEERDDLLA------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1518 flmQEGADPDSIEAVANRVLELSipaspKQIRHLADEIKDRVKSLSnvdAILEQTQNDVRKAEQLLLDAKKARNKAEGVK 1597
Cdd:PRK02224 301 ---EAGLDDADAEAVEARREELE-----DRDEELRDRLEECRVAAQ---AHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1598 NTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANN---- 1673
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAeall 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1674 -----------------------------SLDAARAEETATMAR-----DKANEAKEILDG--ELSDKYRTVQGLMDNKA 1717
Cdd:PRK02224 450 eagkcpecgqpvegsphvetieedrerveELEAELEDLEEEVEEveerlERAEDLVEAEDRieRLEERREDLEELIAERR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1718 KTMQDAKHKAEQLRDEAKGLLKDAQDK--------------LQRLAELEKDYEENQKVLEgkarQLDGLEDKMKAILNAI 1783
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeaeeaREEVAELNSKLAELKERIE----SLERIRTLLAAIADAE 605
|
..
gi 528517572 1784 NR 1785
Cdd:PRK02224 606 DE 607
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1258-1782 |
1.94e-12 |
|
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: 72.84 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1258 IEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASnaLSTLEREAKELNLNADQLNRQLDILK------NSNFLGAYDSIRA 1331
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIIQeqarnqNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1332 SYNKSRDAEHRSNRSTTDTPS------TVSQSADTRKKTERligqkrDDFNRKNA----ANKRTLTDLNAKVQNLDLKKi 1401
Cdd:pfam15921 325 TVSQLRSELREAKRMYEDKIEelekqlVLANSELTEARTER------DQFSQESGnlddQLQKLLADLHKREKELSLEK- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1402 nekvcgapgdaqcvdspcggagcrddEGKRRCGGLNCNGAVAVadtaldrsKHAEKELDKAMGVVEELFKQVADAKTKAQ 1481
Cdd:pfam15921 398 --------------------------EQNKRLWDRDTGNSITI--------DHLRRELDDRNMEVQRLEALLKAMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1482 EAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVANRVLELS---------IPASPKQIRHLA 1552
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTaslqekeraIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1553 DEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAA--AEKA-IQKAKNDIG 1629
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqVEKAqLEKEINDRR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1630 LTQNQLAQIQSETSASERDLNdavDRLGDLERQiealKTKRANNSLDAARAEETATMARDK-ANEAKEILD--GELSDKY 1706
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELE---ARVSDLELE----KVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNelNSLSEDY 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1707 RTVQGLMDNKAKTMQDAKHKaeqlrdeAKGLLKDAQDKLQRLAELEKDYEEN-----------QKVLEGKARQLDGLEDK 1775
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSdghamkvamgmQKQITAKRGQIDALQSK 749
|
570
....*....|.
gi 528517572 1776 MK----AILNA 1782
Cdd:pfam15921 750 IQfleeAMTNA 760
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
767-812 |
2.40e-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: 63.14 E-value: 2.40e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 767 CECDPQGSLSSECDVRGGQCRCRPNISGRRCEKCAPGAYGFG---PSGC 812
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1610-1788 |
4.73e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 ASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEEtatmard 1689
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1690 KANEAKEILDGELSDKYRT-------------------------VQGLMDNKAKTMQD---AKHKAEQLRDEAKGLLKDA 1741
Cdd:COG3883 80 EIEERREELGERARALYRSggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEElkaDKAELEAKKAELEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528517572 1742 QDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1455-1652 |
4.94e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQirqfLMQEGADPDSIEAVAN 1534
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA----LYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 rvlelsipaspkqIRHLADEIkDRVKSLSNV----DAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNda 1610
Cdd:COG3883 111 -------------SESFSDFL-DRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528517572 1611 sRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDA 1652
Cdd:COG3883 175 -AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-1779 |
4.96e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 DRSKHAEKELDKAMGVVEELFKQvadaKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSI 1529
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1530 EAVANRVLELSipaspKQIRHLADE----------IKDRVKSLSNVDAILEQTQNDVRkaeqllLDAKKARNKAEGVKNT 1599
Cdd:PRK02224 282 RDLRERLEELE-----EERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECR------VAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1600 AESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRanNSLDAAR 1679
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER--DELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AEETATM--ARDKANEAKEILD-GELSDKYRTVQGlmDNKAKTMQDAKHKAEQLRDEakglLKDAQDKlqrLAELEKDYE 1756
Cdd:PRK02224 429 AELEATLrtARERVEEAEALLEaGKCPECGQPVEG--SPHVETIEEDRERVEELEAE----LEDLEEE---VEEVEERLE 499
|
330 340
....*....|....*....|...
gi 528517572 1757 ENQKVLEgKARQLDGLEDKMKAI 1779
Cdd:PRK02224 500 RAEDLVE-AEDRIERLEERREDL 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1598-1788 |
5.53e-12 |
|
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: 69.79 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1598 NTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRA--NNSL 1675
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1676 DAAR---AEETATMAR-DKANEAKEILDGE-LSDKYRT---VQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQR 1747
Cdd:COG4942 100 EAQKeelAELLRALYRlGRQPPLALLLSPEdFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 528517572 1748 LAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1725-1793 |
7.08e-12 |
|
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: 62.37 E-value: 7.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1725 HKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTC 1793
Cdd:cd22301 2 ERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1467-1792 |
8.02e-12 |
|
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: 70.87 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1467 EELFKQVADAKTKAQEAKDRAQAALEKASDTKNKvdhsnndLRDLIKQIRQFLMQEGADPDSIEAVANRVLELS--IPAS 1544
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1545 PKQIRHLADEIKDRVKSLSNVDAILEQTQND-----VRKAEQLLLDAKKARNKAEGVkntAESVKKALNDASRAQAAAEK 1619
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEAR---LREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1620 AIQKAKNDIGLTQNQ--------------LAQIQSETSASERDLNDAVDRLGDLERQIEALKT-----KRANNSLDAA-- 1678
Cdd:TIGR02169 834 EIQELQEQRIDLKEQiksiekeienlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAqlrelERKIEELEAQie 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1679 ----RAEETATMARDKANEAKEILDGELSDK--------YRTVQGLMDNKAKTMQ---DAKHKAEQLRDEAKGLLKDAQD 1743
Cdd:TIGR02169 914 kkrkRLSELKAKLEALEEELSEIEDPKGEDEeipeeelsLEDVQAELQRVEEEIRalePVNMLAIQEYEEVLKRLDELKE 993
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1744 KLQRLAELEKDYEENQKVLEGKARQLdgledKMKAiLNAINRQIQ-IYNT 1792
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV-----FMEA-FEAINENFNeIFAE 1037
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1139-1178 |
1.31e-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: 60.83 E-value: 1.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528517572 1139 CDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSG 1178
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1196-1788 |
1.53e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1196 IVQDLATRTKALTDR------AKELQTTGLTRAFERRFKELEDMLAQArdIVNARNAtAEAVTTLMGMIEVLRAQIGETT 1269
Cdd:pfam12128 384 IKEQNNRDIAGIKDKlakireARDRQLAVAEDDLQALESELREQLEAG--KLEFNEE-EYRLKSRLGELKLRLNQATATP 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1270 DTLNQQEGDLTAVQ--DSNYEASNA-LSTLEREAKELNLNADQLNRQLDILknsnflgaydSIRASYNKSRDAEHR---S 1343
Cdd:pfam12128 461 ELLLQLENFDERIEraREEQEAANAeVERLQSELRQARKRRDQASEALRQA----------SRRLEERQSALDELElqlF 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1344 NRSTTDTPSTVSQSADTRKKTERLIGQK---RDDF----NRKNAANKRTLTDLNakvqnLDLKKINekvcgAPGDAQcvd 1416
Cdd:pfam12128 531 PQAGTLLHFLRKEAPDWEQSIGKVISPEllhRTDLdpevWDGSVGGELNLYGVK-----LDLKRID-----VPEWAA--- 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1417 spcggagcRDDEGKRRcgglncngaVAVADTALDRSKHAEKELDKAMGvveelfkQVADAKTKAQEAKDRAQAALEKASD 1496
Cdd:pfam12128 598 --------SEEELRER---------LDKAEEALQSAREKQAAAEEQLV-------QANGELEKASREETFARTALKNARL 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1497 tknkvdhsnnDLRDLIKQIRQflmqegadpdsiEAVA-NRVLELSIPASPKQIRHLADEIKDRVKSLSnvdAILEQTQND 1575
Cdd:pfam12128 654 ----------DLRRLFDEKQS------------EKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQ---AWLEEQKEQ 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1576 VRKAEQLLLDAKKArnkAEGVKNTAESVKKALNDASRAQAAAE-KAIQKakndigltqnqlaqiQSETSASERDLNDavD 1654
Cdd:pfam12128 709 KREARTEKQAYWQV---VEGALDAQLALLKAAIAARRSGAKAElKALET---------------WYKRDLASLGVDP--D 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1655 RLGDLERQIEALKTKRANnsldAARAEETATMARDKANEA----KEILDGELSDKYRTVQGLMDNKAKTMQDAK------ 1724
Cdd:pfam12128 769 VIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQETwlqrRPRLATQLSNIERAISELQQQLARLIADTKlrrakl 844
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1725 ----HKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEG--KARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:pfam12128 845 emerKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIgeRLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1507-1769 |
2.08e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1507 DLRDL--------IKQIRQFLMQEGADP-DSIEAVANRVLE-LSIPA-----------SPKQIRHLADEIKDRV----KS 1561
Cdd:COG4913 144 DLEDFeefahgfdIRALKARLKKQGVEFfDSFSAYLARLRRrLGIGSekalrllhktqSFKPIGDLDDFVREYMleepDT 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1562 LSNVDAILEQTQnDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQA--------AAEKAIQKAKNDIGLTQN 1633
Cdd:COG4913 224 FEAADALVEHFD-DLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEELRA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1634 QLAQIQSETSASERDLNDAVDRLGDLERQ--------IEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSDk 1705
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE- 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1706 YRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRL-AELEkDYEENQKVLEGKARQL 1769
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeAEIA-SLERRKSNIPARLLAL 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1250-1787 |
2.27e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1250 AVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASNALSTLEREAKELNLNADQL--NRQLDILKNsnfLGayd 1327
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEK---IG--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1328 SIRASYNKSRDAEHRSNRSttdtpstVSQSADTRKKTERLIGQKR---DDFNRKNAANKRTLTDLNAKVQNLDlKKINEK 1404
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELK-EELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1405 VcgapGDAQCVDspcggagcrddegkrrcgglncngavAVADTALDRSKHAEKELDKAMGVVEEL---FKQVADAKTKAQ 1481
Cdd:TIGR02169 370 R----AELEEVD--------------------------KEFAETRDELKDYREKLEKLKREINELkreLDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1482 EAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAvanrvlelSIPASPKQIRHLADEIKDRVKS 1561
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ--------ELYDLKEEYDRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1562 LSNVDA---ILEQTQNDVRKAEQLLldakKARNKaeGVKNT-AE--SVK----KALNDAS--RAQAA-------AEKAIQ 1622
Cdd:TIGR02169 492 LAEAEAqarASEERVRGGRAVEEVL----KASIQ--GVHGTvAQlgSVGeryaTAIEVAAgnRLNNVvveddavAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1623 --KAKNdIG----LTQNQLAQIQSETSASERD--LNDAVDrLGDLERQIE-----ALKTKRANNSLDAARA--------- 1680
Cdd:TIGR02169 566 llKRRK-AGratfLPLNKMRDERRDLSILSEDgvIGFAVD-LVEFDPKYEpafkyVFGDTLVVEDIEAARRlmgkyrmvt 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1681 ------EETATM--------------ARDKA-----NEAKEILDGELS---DKYRTVQGLMDNKAKTMQDAKHKAEQLRD 1732
Cdd:TIGR02169 644 legelfEKSGAMtggsraprggilfsRSEPAelqrlRERLEGLKRELSslqSELRRIENRLDELSQELSDASRKIGEIEK 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 1733 EAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLE---DKMKAILNAINRQI 1787
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariEELEEDLHKLEEAL 781
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
394-451 |
2.48e-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: 2.48e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 394 CDCDPDGSKnGGVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLSASDPRGC 451
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1546-1781 |
2.85e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLldaKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAK 1625
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEEL---EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1626 NDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTK-----RANNSLDAARAEETATMARDKANEAKEILDG 1700
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElaaleQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1701 ELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAIL 1780
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
.
gi 528517572 1781 N 1781
Cdd:COG4372 282 A 282
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1522-1763 |
3.00e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 68.50 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1522 EGADPDSIEAVANRVLELSIpaspkqIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKkARNKAEGVKNTAE 1601
Cdd:COG3206 143 TSPDPELAAAVANALAEAYL------EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-QKNGLVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1602 SVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERD--LNDAVDRLGDLERQIEALKTKRANNSLDAAR 1679
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AeetatmaRDKANEAKEILDGELSDKYRTVQglmdNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQ 1759
Cdd:COG3206 296 L-------RAQIAALRAQLQQEAQRILASLE----AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364
|
....
gi 528517572 1760 KVLE 1763
Cdd:COG3206 365 ELYE 368
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1139-1183 |
9.98e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.98e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 1139 CDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSG-TFPDC 1183
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1205-1748 |
1.12e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1205 KALTDRAKELQT-TG-LTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETtdtlnQQEGDLTAV 1282
Cdd:COG4717 49 ERLEKEADELFKpQGrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1283 QDSNYEASNALSTLEREAKELNLNADQLNRQLDILKNsnFLGAYDSIRASY-NKSRDAEHRSNRSTTDTPSTVSQSADTR 1361
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRE--LEEELEELEAELaELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1362 KKTERLIGQKRDDFNRKNAANKRTLTDLNAKVQNLDLKKINEKVcgapgdaqcvdspcggagcrddegKRRCGGLNCNGA 1441
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL------------------------KEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1442 VAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKnkvdhsnnDLRDliKQIRQFLmq 1521
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE--------ELEE--EELEELL-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1522 egadpdsieavanRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQ-TQNDVRKAEQLLLDAKKARNKAE-----G 1595
Cdd:COG4717 326 -------------AALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEElraalE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1596 VKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQ--NQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTkraNN 1673
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLEE---DG 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1674 SLDAARAEEtaTMARDKANeakeildgELSDKYRTVQGLmdnkAKTMQDAKHKAEQLRdeAKGLLKDAQDKLQRL 1748
Cdd:COG4717 470 ELAELLQEL--EELKAELR--------ELAEEWAALKLA----LELLEEAREEYREER--LPPVLERASEYFSRL 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1585-1778 |
1.18e-10 |
|
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: 65.56 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1585 DAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIE 1664
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1665 ALKTKRAN------------------NSLDAARAEETATMARDKANEAKEILDG------ELSDKYRTVQGLMDNKAKT- 1719
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEElradlaELAALRAELEAERAELEALl 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1720 --MQDAKHKAEQLRDEAKGLLKDAQDKL----QRLAELEKDYEENQKVLEGKARQLDGLEDKMKA 1778
Cdd:COG4942 181 aeLEEERAALEALKAERQKLLARLEKELaelaAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1730-1794 |
1.36e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 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. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 58.61 E-value: 1.36e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1730 LRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:cd22303 7 IKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
815-856 |
3.23e-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: 56.98 E-value: 3.23e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFP 856
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1449-1785 |
3.64e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1449 LDRSKHAEKELDKAMGVVEElFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDH--SNNDLRDLIKQIRQFLMQEGADP 1526
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 DSIEAVANRVLEL--SIPASPKQIRHLADEIKDRVKSLSNVD-AILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESV 1603
Cdd:COG4717 149 EELEERLEELRELeeELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1604 KKALNDASRAQAAAEKaIQKAKNDI---GLTQNQLAQIQSETSASERDLNDAVDRLG--------------DLERQIEAL 1666
Cdd:COG4717 229 LEQLENELEAAALEER-LKEARLLLliaAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllarekaSLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1667 KTKRANNSLDAARAEETATmARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHkaEQLRDEAKGLLKDAQ---- 1742
Cdd:COG4717 308 QALPALEELEEEELEELLA-ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGvede 384
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 528517572 1743 DKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINR 1785
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
815-856 |
3.67e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.67e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 815 CECSLEGSQSRFCDLYSGQCPCRPGAYGQRCDGCQAGHWGFP 856
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1555-1790 |
3.74e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.77 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1555 IKDRVKSLSNVDAILEQTQNDVRKAEQLLldaKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQ 1634
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1635 LAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRAN-NSLDAARAEETATMARDKANEAKEILDGELSDKYRTVQGLM 1713
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAElQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1714 DNKAKTMQDAKHKAEQLR--DEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIY 1790
Cdd:COG4372 183 QALDELLKEANRNAEKEEelAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-905 |
3.85e-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: 56.98 E-value: 3.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 860 PCQCNGHAD---ECHQRTGACLnCRSNTAGDKCERCANGYYGNPVLGLG 905
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1138-1187 |
4.59e-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: 56.59 E-value: 4.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1138 ACDCDPRGIESSQCNRMTGHCVCQQGVSGVRCDQCARGFSGTFPDCKPCH 1187
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1192-1790 |
4.87e-10 |
|
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: 64.66 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1192 DWDRIVQDLATRTKALTDRAKELqttgltrafERRFKELEDMLAQARDIVNARNATaeaVTTLMGMIEVLRAQIGETTDT 1271
Cdd:TIGR04523 58 NLDKNLNKDEEKINNSNNKIKIL---------EQQIKDLNDKLKKNKDKINKLNSD---LSKINSEIKNDKEQKNKLEVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1272 LNQQEGDLTAVQDSNYEASNALSTLEREAKELNLNADQLNRQ-------LDILKN--SNFLGAYDSIRASYNKSR----- 1337
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQkeeleneLNLLEKekLNIQKNIDKIKNKLLKLElllsn 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1338 -DAEHRSNRSTTdtpSTVSQSADTRKKTERLIGQKRDDFNRKNAANKRTLTDLNakvqnlDLKKINEKVcgapgdaqcvd 1416
Cdd:TIGR04523 206 lKKKIQKNKSLE---SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN------QLKDEQNKI----------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1417 spcggagcrddegkrrcgglncngavavadtaLDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAAL----- 1491
Cdd:TIGR04523 266 --------------------------------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkelk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1492 -------EKASDTKNKVDHSN---NDLRDLIKQIRQFLMQEGADpdsieavaNRVLELSIPASPKQIRHLADEIKDRVKS 1561
Cdd:TIGR04523 314 selknqeKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESE--------NSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1562 LSNvdaiLEQTQNDVrkaEQLLLDAKK-ARNKAEGVKNtAESVKKALndasraqaaaEKAIQKAKNDIGLTQNQLAQIQS 1640
Cdd:TIGR04523 386 IKN----LESQINDL---ESKIQNQEKlNQQKDEQIKK-LQQEKELL----------EKEIERLKETIIKNNSEIKDLTN 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1641 ETSASERDLNDAVDRLGDLERQIEALKT--KRANNSLDAARAE-ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKA 1717
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKElKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1718 KTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKD--------YEENQKVLEGKARQLDGLEDKMKAILNAINRQIQI 1789
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDeknkeieeLKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
.
gi 528517572 1790 Y 1790
Cdd:TIGR04523 608 K 608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1573-1786 |
7.56e-10 |
|
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: 62.86 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1573 QNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQaaaEKAIQKAKNDIGLTQNQLAQIqsetsasERDLNDA 1652
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAAL-------EAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1653 VDRLGDLERQIEALKTKRAN------------------NSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMD 1714
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1715 NKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQ 1786
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1610-1790 |
7.76e-10 |
|
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: 62.86 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 ASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARD 1689
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1690 KANEAKEILDGELSDKYRT-----VQGLMDNK-----AKTMQDAKHKAEQLRDEAKGL---LKDAQDKLQRLAELEKDYE 1756
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgrqppLALLLSPEdfldaVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELE 177
|
170 180 190
....*....|....*....|....*....|....
gi 528517572 1757 ENQKVLEGKARQLDGLEDKMKAILNAINRQIQIY 1790
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1448-1779 |
8.95e-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: 63.93 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1448 ALDRSKHAEKELDKAMGVVEELFKQVaDAKTKAQEAKDRAQAALEKASDTKNKVdHSNNdLRDLIKQIRQFLmqegADPD 1527
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYEGYE-LLKE-KEALERQKEAIE----RQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1528 SIEavanrvlelsipaspKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKaeqllldakKARNKAEGVKNTAESVKKAL 1607
Cdd:TIGR02169 248 SLE---------------EELEKLTEEISELEKRLEEIEQLLEELNKKIKD---------LGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1608 NDASRAQAAAEKAIQKAkndigltQNQLAQIQSETSASERDLNDavdrlgdLERQIEALKTKRAN--NSLDAARAE---- 1681
Cdd:TIGR02169 304 ASLERSIAEKERELEDA-------EERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKltEEYAELKEEledl 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1682 --------ETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLlkdaqdkLQRLAELEK 1753
Cdd:TIGR02169 370 raeleevdKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGI-------EAKINELEE 441
|
330 340
....*....|....*....|....*.
gi 528517572 1754 DYEENQKVLEGKARQLDGLEDKMKAI 1779
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
393-452 |
1.21e-09 |
|
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: 55.44 E-value: 1.21e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 393 ACDCDPDGSKNGgVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLsASDPRGCQ 452
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGT--------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1441-1652 |
1.29e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.15 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSK----HAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIR 1516
Cdd:COG3883 10 TPAFADPQIQAKQkelsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1517 QFL--MQE-GADPDSIEAV---------ANRVLELSIPASpkQIRHLADEIKDRVKSLSNVDAILEQTQNDvrkAEQLLL 1584
Cdd:COG3883 90 ERAraLYRsGGSVSYLDVLlgsesfsdfLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAE---LEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 1585 DAKKARNKAEGVKNTAEsvkKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDA 1652
Cdd:COG3883 165 ELEAAKAELEAQQAEQE---ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1091-1139 |
1.31e-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: 55.44 E-value: 1.31e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517572 1091 CACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDPRVLCRAC 1139
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1518-1760 |
1.52e-09 |
|
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: 62.09 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1518 FLMQEGADPDSIEAVANRVLELSipaspKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEgvk 1597
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQ-----QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1598 ntaesvkKALNDASRAQAAAEKAIQKAKNDIGlTQNQLAQIQSETSA-----SERDLNDAVDRLGDLERQIEALKTKRAN 1672
Cdd:COG4942 83 -------AELAELEKEIAELRAELEAQKEELA-ELLRALYRLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1673 NSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELE 1752
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*...
gi 528517572 1753 KDYEENQK 1760
Cdd:COG4942 234 AEAAAAAE 241
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1449-1757 |
1.54e-09 |
|
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: 62.74 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1449 LDRSKHAEKELDKamgVVEElfkqVADAKTKAQEAKDRAQAALEKASDTKNKVDhsnnDLR-DLIK------QIRQFL-- 1519
Cdd:pfam05701 34 VERRKLVELELEK---VQEE----IPEYKKQSEAAEAAKAQVLEELESTKRLIE----ELKlNLERaqteeaQAKQDSel 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1520 -------MQEG-ADPDSIEAVANrvLELSipaspkQIRH---LAD--EIKDRVKSLSNV-DAILEQTQNDVRKAEQLLLD 1585
Cdd:pfam05701 103 aklrveeMEQGiADEASVAAKAQ--LEVA------KARHaaaVAElkSVKEELESLRKEyASLVSERDIAIKRAEEAVSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1586 AKKARNKAEGVknTAE--SVKKALNDASRAQAAAEKaiQKakndIGLTqnqLAQIQsETSASERDLNDAVDRLGDLERQI 1663
Cdd:pfam05701 175 SKEIEKTVEEL--TIEliATKESLESAHAAHLEAEE--HR----IGAA---LAREQ-DKLNWEKELKQAEEELQRLNQQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1664 EA---LKTKRANNS--LDAARAEETATMARDKANEAKEilDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKgLL 1738
Cdd:pfam05701 243 LSakdLKSKLETASalLLDLKAELAAYMESKLKEEADG--EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVN-CL 319
|
330
....*....|....*....
gi 528517572 1739 KDAQDKLQrlAELEKDYEE 1757
Cdd:pfam05701 320 RVAAASLR--SELEKEKAE 336
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-900 |
1.73e-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: 55.05 E-value: 1.73e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517572 861 CQCNGHA---DECHQRTGACLnCRSNTAGDKCERCANGYYGNP 900
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1553-1768 |
1.73e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1553 DEIKDRVKSLSNVDAILEQTQNDVRKAEQlllDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGlTQ 1632
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG-ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1633 NQLAQIQSETSA------SERDLNDAVDRLGDLERQIEAlktkrANNSLDAARAeetatmARDKANEAKEILDGELSDky 1706
Cdd:COG3883 92 ARALYRSGGSVSyldvllGSESFSDFLDRLSALSKIADA-----DADLLEELKA------DKAELEAKKAELEAKLAE-- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1707 rtvqglMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQ 1768
Cdd:COG3883 159 ------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1643-1791 |
2.62e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.07 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1643 SASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQD 1722
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1723 AKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYN 1791
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1267-1680 |
2.69e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1267 ETTDTLNQQEGDLTAVQDSNYEASNALSTLEREAKE----LNLNADQLNRQLDILKNSnflgaYDSIRASYNKSRDAEhr 1342
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKaeryKELKAELRELELALLVLR-----LEELREELEELQEEL-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1343 sNRSTTDTPSTVSQSADTRKKTERLIGQKRDDFNRKNAANKRtLTDLNAKVQNLDLKK--INEKvcgapgDAQCVDSPCG 1420
Cdd:TIGR02168 249 -KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRLEQQKqiLRER------LANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1421 GAGCRDDEGKRRcgglncngavavaDTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQaALEKASDTknk 1500
Cdd:TIGR02168 321 LEAQLEELESKL-------------DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLET--- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1501 vdhsnndLRDLIKQIRQflmqegadpdSIEAVANRVLELS--IPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRK 1578
Cdd:TIGR02168 384 -------LRSKVAQLEL----------QIASLNNEIERLEarLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1579 AEQLLLDAKKARnkaegVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSA------SERDLNDA 1652
Cdd:TIGR02168 447 EELEELQEELER-----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallkNQSGLSGI 521
|
410 420 430
....*....|....*....|....*....|....*....
gi 528517572 1653 VDRLGDL-------ERQIEALKTKRANN----SLDAARA 1680
Cdd:TIGR02168 522 LGVLSELisvdegyEAAIEAALGGRLQAvvveNLNAAKK 560
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1210-1782 |
2.78e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.55 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1210 RAKELQTTGLTRAFERRFKELEDMLAQARDIVNarnataEAVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAVQDSNYEa 1289
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1290 snalsTLEREAKELNLNADQLNRQLDILKNsnFLGAYDSIRASYNKSRDAehRSNRSTTDTPSTVSQSADTRKKTERLIG 1369
Cdd:pfam12128 341 -----TAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSK--IKEQNNRDIAGIKDKLAKIREARDRQLA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1370 QKRDDFNRKNAANKRTLtdlnaKVQNLDLKKINEKVCGAPGDAQcvdspcggagcrddegkrrcggLNCNGAVAVADTAL 1449
Cdd:pfam12128 412 VAEDDLQALESELREQL-----EAGKLEFNEEEYRLKSRLGELK----------------------LRLNQATATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 D------RSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEG 1523
Cdd:pfam12128 465 QlenfdeRIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEA 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1524 AD-PDSIEAVANRVLelsipaspkqirhladeikdrvksLSNVDaiLEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAes 1602
Cdd:pfam12128 545 PDwEQSIGKVISPEL------------------------LHRTD--LDPEVWDGSVGGELNLYGVKLDLKRIDVPEWA-- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1603 vkkALNDASRAQ-AAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAV-------DRLGDLERQIEALKTKranns 1674
Cdd:pfam12128 597 ---ASEEELRERlDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalknarLDLRRLFDEKQSEKDK----- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1675 LDAARAEEtatmaRDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQrlAELEKD 1754
Cdd:pfam12128 669 KNKALAER-----KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLK--AAIAAR 741
|
570 580
....*....|....*....|....*...
gi 528517572 1755 YeenqkvlEGKARQLDGLEDKMKAILNA 1782
Cdd:pfam12128 742 R-------SGAKAELKALETWYKRDLAS 762
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1259-1750 |
2.85e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1259 EVLRAQIGETTDTLNQQEGDLTAVQDSNYEASNALSTLEREAKELNlNADQLNRQLDILKNsnflgaydsiRASYNKSRD 1338
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKK----------KADELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1339 AEHRSNRSTTDTPSTVSQSADTRKKTERligQKRDDFNRKNAANKRTLTDLNAKVQNldlKKINEKVCGAPGDAQCVDSp 1418
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEE---AKKADEAKKKAEEAKKAEEAKKKAEE---AKKADEAKKKAEEAKKADE- 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1419 cggAGCRDDEGKRRCGGLNcngAVAVADTALDRSKHAEK-----ELDKAmgvvEElfKQVADAKTKAQEAK--DRAQAAL 1491
Cdd:PTZ00121 1488 ---AKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEakkadEAKKA----EE--AKKADEAKKAEEKKkaDELKKAE 1555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1492 E-KASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVANRVLELSIPASPK-----QIRHLADEIKDRVKSLSNV 1565
Cdd:PTZ00121 1556 ElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeEAKIKAEELKKAEEEKKKV 1635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1566 DAILEQTQNDVRKAEQL-------LLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNdigltQNQLAQI 1638
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKK 1710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1639 QSETSASERDLNDAVDrlgdlERQIEALKTKRANNSlDAARAEEtatmARDKANEAKEILDGELSDKYRTVQGLMDNKAK 1718
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEE-----ENKIKAEEAKKEAEE-DKKKAEE----AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
490 500 510
....*....|....*....|....*....|..
gi 528517572 1719 TMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAE 1750
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-504 |
5.62e-09 |
|
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: 53.51 E-value: 5.62e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528517572 453 PCKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHWALSHDTSGCR 504
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1778 |
6.11e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.38 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQ-----EAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegadpdSI 1529
Cdd:NF041483 92 AERELRDARAQTQRILQEHAEHQARLQaelhtEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRA----------RT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1530 EAVANRVL-------ELSIPASPKQIRHLADEIKDRVKS-----LSNVDAILEQTQNDVRK---------------AEQL 1582
Cdd:NF041483 162 ESQARRLLdesraeaEQALAAARAEAERLAEEARQRLGSeaesaRAEAEAILRRARKDAERllnaastqaqeatdhAEQL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1583 ----LLDAKKARNKAEGVKNTAESVKKALNDASR-AQAAAEKAIQKAKNDIGltqNQLAQIQSETSASERDLNDAVDRL- 1656
Cdd:NF041483 242 rsstAAESDQARRQAAELSRAAEQRMQEAEEALReARAEAEKVVAEAKEAAA---KQLASAESANEQRTRTAKEEIARLv 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1657 GDLERQIEALKTKrANNSLDAARAE------ETATMARDKANE------------AKEILDGELSDKYRTVQGLMDNKAK 1718
Cdd:NF041483 319 GEATKEAEALKAE-AEQALADARAEaeklvaEAAEKARTVAAEdtaaqlakaartAEEVLTKASEDAKATTRAAAEEAER 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 1719 TMQDAKHKAEQLRDEAkgllKDAQDKLQRLAELE-KDYEENQKVLEGKARQLDGLEDKMKA 1778
Cdd:NF041483 398 IRREAEAEADRLRGEA----ADQAEQLKGAAKDDtKEYRAKTVELQEEARRLRGEAEQLRA 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1554-1775 |
8.14e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1554 EIKDRVKSLsnvdaileQTQndVRKAEQ---------------LLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAE 1618
Cdd:TIGR02168 197 ELERQLKSL--------ERQ--AEKAERykelkaelrelelalLVLRLEELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1619 KAIQKAKNDIGLTQNQLAQIQSEtsaserdLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEAKEIL 1698
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1699 DgELSDKYRTVQGLMDNKAKTMQdakhKAEQLRDEAKGLLKDAQDKLQRL----AELEKDYEENQKVLEGKARQLDGLED 1774
Cdd:TIGR02168 340 A-ELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLrskvAQLELQIASLNNEIERLEARLERLED 414
|
.
gi 528517572 1775 K 1775
Cdd:TIGR02168 415 R 415
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
506-544 |
1.59e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 1.59e-08
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
394-451 |
1.70e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 394 CDCDPDGSKNGgVCDGHDdpslgmiaGQCRCKDNVEGSRCDKCKPGFFGLSasdPRGC 451
Cdd:smart00180 1 CDCDPGGSASG-TCDPDT--------GQCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1090-1132 |
1.78e-08 |
|
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: 51.97 E-value: 1.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517572 1090 PCACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDP 1132
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1445-1794 |
2.63e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1445 ADTALDRSKH-AEKELDKAMGVVEELF----KQVADAKTKAQ----EAKDRAQAALEKASDTKNKVdhsnndlRDLIKQI 1515
Cdd:NF041483 715 AEETLGSARAeADQERERAREQSEELLasarKRVEEAQAEAQrlveEADRRATELVSAAEQTAQQV-------RDSVAGL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 RQFLMQEGADPDSI-EAVANRVlelsipaspkqiRHLADEIKDRVKSlsnvDAILEQTqndvRKAEQLLLDAKKARNKAE 1594
Cdd:NF041483 788 QEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRS----DAYAERE----RASEDANRLRREAQEETE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1595 GVKNTAE-SVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDlnDAVDRLGDLERQIEAL---KTKR 1670
Cdd:NF041483 848 AAKALAErTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARE--DANRIRSDAAAQADRLigeATSE 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1671 ANNSLDAARAE------ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDK 1744
Cdd:NF041483 926 AERLTAEARAEaerlrdEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAE 1005
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1745 LQRL-----AELEKDYEENQKvlEGKARQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:NF041483 1006 AERLrtearEEADRTLDEARK--DANKRRSEAAEQADTLITEAAAEADQLTAKAQ 1058
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1205-1761 |
3.39e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1205 KALTDRAKELQTTGLTRAFERRFKELEDmlaqaRDIVNARNATAEAVTtlmgmievLRAQIGETTDTLNQQEGDLTAVQD 1284
Cdd:PRK01156 260 TAESDLSMELEKNNYYKELEERHMKIIN-----DPVYKNRNYINDYFK--------YKNDIENKKQILSNIDAEINKYHA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1285 SNYEASNaLSTLEREAKELNLNADQLNRQLDILK--NSNFLGAYDSIRaSYNKSRDAEHRSNRSTTDTPSTVSQSADTrk 1362
Cdd:PRK01156 327 IIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEgyEMDYNSYLKSIE-SLKKKIEEYSKNIERMSAFISEILKIQEI-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1363 kTERLIGQKRDDFNRKnaankrtLTDLNAKVQNLDLKKinekvcgapgdaqcvdspcGGAGCRDDEGKRRCGGLNCNGAV 1442
Cdd:PRK01156 403 -DPDAIKKELNEINVK-------LQDISSKVSSLNQRI-------------------RALRENLDELSRNMEMLNGQSVC 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1443 AVADTAL--DRSKHAEKEL-DKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFL 1519
Cdd:PRK01156 456 PVCGTTLgeEKSNHIINHYnEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIK 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1520 mqegadpDSIEAVANRVLElsipaspkqirhlADEIKDRVKSLSNVDaiLEQtqndvRKAEQLLLDAKKARNKAEGVKNT 1599
Cdd:PRK01156 536 -------IKINELKDKHDK-------------YEEIKNRYKSLKLED--LDS-----KRTSWLNALAVISLIDIETNRSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1600 AESVKKALNDASRAQAAAEKAIQKAKNdigLTQNQLAQIQSETsaseRDLNDAVDRLGDLERQIEALKTKRANNSLDAAR 1679
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKS---YIDKSIREIENEA----NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AEEtatMARDKANEAKEILDGElsDKYRTVQGLMDnkaktmqDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQ 1759
Cdd:PRK01156 662 IDS---IIPDLKEITSRINDIE--DNLKKSRKALD-------DAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
..
gi 528517572 1760 KV 1761
Cdd:PRK01156 730 KI 731
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1034-1088 |
3.49e-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: 51.20 E-value: 3.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNLA--SGQGC 1088
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1202-1668 |
4.36e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1202 TRTKALTDRAKElQTTGLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLmgmIEVLRAQIGETTDTLNQQEgdlTA 1281
Cdd:PRK02224 264 RETIAETERERE-ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR---REELEDRDEELRDRLEECR---VA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1282 VQDSNYEASNAL---STLEREAKELNLNADQLNRQLDilknsnflgaydSIRASYNKSR------DAEHRSNRST-TDTP 1351
Cdd:PRK02224 337 AQAHNEEAESLRedaDDLEERAEELREEAAELESELE------------EAREAVEDRReeieelEEEIEELRERfGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1352 STVSQSADTRKkterLIGQKRDDFNRKnaankrtLTDLNAKVQNLDlKKINEK----------VCGAPGDaqcvDSP--C 1419
Cdd:PRK02224 405 VDLGNAEDFLE----ELREERDELRER-------EAELEATLRTAR-ERVEEAealleagkcpECGQPVE----GSPhvE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1420 GGAGCRDDEGKRRCGGLNCNGAVAVADTALDRSK---HAEKEL---------------DKAMGV------VEELFKQVAD 1475
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlvEAEDRIerleerredleeliaERRETIeekrerAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1476 AKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDlIKQIRQFLMQEGADPDSIEAVANRVLELSipASPKQIRHLADEI 1555
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLR--EKREALAELNDER 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1556 KDRVKSLSNVDAILEQTQNDVRKAEqllldakkARNKaegvKNTAESVKKALNDASRAQAAAEKAIQKAkndIGLTQNQL 1635
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDEARIEE--------ARED----KERAEEYLEQVEEKLDELREERDDLQAE---IGAVENEL 690
|
490 500 510
....*....|....*....|....*....|....
gi 528517572 1636 AQIqsETSASERD-LNDAVDRLGDLERQIEALKT 1668
Cdd:PRK02224 691 EEL--EELRERREaLENRVEALEALYDEAEELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1546-1785 |
4.58e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSLSNVD-------AILEQTQNDVRKAEQLLldaKKARNKAEGVKNTAESVKKalndasraqaaae 1618
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEelikekeKELEEVLREINEISSEL---PELREELEKLEKEVKELEE------------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1619 kaiqkakndiglTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKtkrannsldaARAEETatmaRDKANEAKEIl 1698
Cdd:PRK03918 236 ------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----------KEIEEL----EEKVKELKEL- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1699 dGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGL---LKDAQDKLQRLAELEKDYEENQK---VLEGKARQLdgl 1772
Cdd:PRK03918 289 -KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeerIKELEEKEERLEELKKKLKELEKrleELEERHELY--- 364
|
250
....*....|...
gi 528517572 1773 eDKMKAILNAINR 1785
Cdd:PRK03918 365 -EEAKAKKEELER 376
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
506-544 |
5.45e-08 |
|
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: 50.82 E-value: 5.45e-08
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-499 |
5.48e-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: 50.81 E-value: 5.48e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 454 CKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHWALSHD 499
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1577-1788 |
5.50e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 57.74 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1577 RKAEQLL---LDAKKARNKAEgvkntAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSA-SERDLNDA 1652
Cdd:COG3064 8 KAAEAAAqerLEQAEAEKRAA-----AEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAeAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1653 VDRLGDLERQIEALKTKRannsldAARAEETATMARDKANEAKEILDgelsdkyrtvqglmDNKAKTMQDAKHKAEQLRD 1732
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKA------AKEAEAAAAAEKAAAAAEKEKAE--------------EAKRKAEEEAKRKAEEERK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1733 EAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG3064 143 AAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1633-1788 |
5.71e-08 |
|
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: 55.70 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1633 NQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgelsdkyrTVQgl 1712
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NVR-- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1713 mdnKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG1579 87 ---NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1548-1788 |
6.14e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1548 IRH-LADEIKDRVKSLSNvdailEQTQNDVRKAEQLLlDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKN 1626
Cdd:COG4717 43 IRAmLLERLEKEADELFK-----PQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1627 DIGL--TQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRAnnslDAARAEETATMARDKANEAKEILDGElsd 1704
Cdd:COG4717 117 ELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLA--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1705 kyrtvqglmdnKAKTMQDAKHKAEQLRdeakgllkdaqdklQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAilNAIN 1784
Cdd:COG4717 190 -----------TEEELQDLAEELEELQ--------------QRLAELEEELEEAQEELEELEEELEQLENELEA--AALE 242
|
....
gi 528517572 1785 RQIQ 1788
Cdd:COG4717 243 ERLK 246
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1451-1752 |
6.83e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.91 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1451 RSKHAEK---ELDKAMGVVEELFkqvadakTKAQE-AKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLmqEGADP 1526
Cdd:NF041483 355 RTVAAEDtaaQLAKAARTAEEVL-------TKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQL--KGAAK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 DSIEAVANRVLELSIPA-----SPKQIRHLADEIKDRVKSLSNVDAIlEQTQNDVRKAEQLLldaKKARNKAEGVKNTA- 1600
Cdd:NF041483 426 DDTKEYRAKTVELQEEArrlrgEAEQLRAEAVAEGERIRGEARREAV-QQIEEAARTAEELL---TKAKADADELRSTAt 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1601 ---ESVK-KALNDASRAQAAAEKAIQKAKNDIG-LTQNQLAQIQSETSASERDlndAVDRLGDLERQIEAlktKRANNSL 1675
Cdd:NF041483 502 aesERVRtEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERA---ARELREETERAIAA---RQAEAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1676 DAAR-----------AEETATMARD-------KANEAKEILDGELSDKYRTVQglmdnkaktmQDAKHKAEQLRDEAkgl 1737
Cdd:NF041483 576 ELTRlhteaeerltaAEEALADARAeaerirrEAAEETERLRTEAAERIRTLQ----------AQAEQEAERLRTEA--- 642
|
330
....*....|....*
gi 528517572 1738 lkdAQDKLQRLAELE 1752
Cdd:NF041483 643 ---AADASAARAEGE 654
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1450-1787 |
7.53e-08 |
|
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: 57.49 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 DRSKHAEK---ELDKAMGVVE----ELFKQVAD-----AKTKAQEAK--DRAQAALEKASDTKNKVDHSNNDLRDLIKQI 1515
Cdd:pfam01576 194 ERLKKEEKgrqELEKAKRKLEgestDLQEQIAElqaqiAELRAQLAKkeEELQAALARLEEETAQKNNALKKIRELEAQI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 RQflMQEgaDPDSIEAVANRvlelsipaSPKQIRHLADEikdrvksLSNVDAILEQT------QNDVR-KAEQLLLDAKK 1588
Cdd:pfam01576 274 SE--LQE--DLESERAARNK--------AEKQRRDLGEE-------LEALKTELEDTldttaaQQELRsKREQEVTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1589 A---------------RNK--------------AEGVKNTAESVKKALnDASRAQAAAE-KAIQKAKNDI----GLTQNQ 1634
Cdd:pfam01576 335 AleeetrsheaqlqemRQKhtqaleelteqleqAKRNKANLEKAKQAL-ESENAELQAElRTLQQAKQDSehkrKKLEGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1635 LAQIQSETSASERDLNDAVDRLGDLERQIEAL---------KTKRANNSLDAA----------RAEET------ATMAR- 1688
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVssllneaegKNIKLSKDVSSLesqlqdtqelLQEETrqklnlSTRLRq 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1689 --DKANEAKEILDGELSDKyRTV--------QGLMDNKAKTMQDAKhKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEEN 1758
Cdd:pfam01576 494 leDERNSLQEQLEEEEEAK-RNVerqlstlqAQLSDMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
410 420
....*....|....*....|....*....
gi 528517572 1759 QKvleGKARQLDGLEDKMKAILNaiNRQI 1787
Cdd:pfam01576 572 EK---TKNRLQQELDDLLVDLDH--QRQL 595
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1458-1773 |
8.21e-08 |
|
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: 57.67 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1458 ELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEgadpDSIEAVANRVL 1537
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT----QQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1538 ELSIPASPKQirHLADEIKDRVKSLSNVDAILEQTQ---NDVRKAEQLLLDAK---KARNKAEGVKNTAESVKKALNDAS 1611
Cdd:TIGR00618 250 EAQEEQLKKQ--QLLKQLRARIEELRAQEAVLEETQeriNRARKAAPLAAHIKavtQIEQQAQRIHTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1612 RAQAAAEKAIQKAKNDIGLTQNQLAQ-----IQSETSASERDLNDA----VDRLGDLERQIEAL--KTKRANNSLDAARA 1680
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTLHSQeihirDAHEVATSIREISCQqhtlTQHIHTLQQQKTTLtqKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1681 EETATMARDKANEAKEI----LDGE--LSDKYRTVQGLMdnKAKTMQDAKHKAEQLRdEAKGLLKDAQDKLQRLAELEKD 1754
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGqlahAKKQqeLQQRYAELCAAA--ITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQTKEQIHLQ 484
|
330
....*....|....*....
gi 528517572 1755 YEENQKVLEGKARQLDGLE 1773
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEP 503
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1455-1787 |
9.05e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEElfkqvadaktkAQEAKDRAQAALEKASDtknKVDHSNNDLRDLikqirqflmQEGADPDSIEAV-- 1532
Cdd:COG3096 359 LTERLEEQEEVVEE-----------AAEQLAEAEARLEAAEE---EVDSLKSQLADY---------QQALDVQQTRAIqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1533 --ANRVLElsipaSPKQIRHLAD-EIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVkntAESVKKALND 1609
Cdd:COG3096 416 qqAVQALE-----KARALCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKA---YELVCKIAGE 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 ASRAQA--AAEKAIQKAKNDIGLTQnQLAQIQSETSASERDLNdavdRLGDLERQIEALkTKRANNSLDAARAEEtatma 1687
Cdd:COG3096 488 VERSQAwqTARELLRRYRSQQALAQ-RLQQLRAQLAELEQRLR----QQQNAERLLEEF-CQRIGQQLDAAEELE----- 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1688 rDKANEAKEILDgELSDKYRT-VQGLMDNKAkTMQDAKHKAEQLRDEAKGLLKdAQDKLQRLAELEKDYEEN-------- 1758
Cdd:COG3096 557 -ELLAELEAQLE-ELEEQAAEaVEQRSELRQ-QLEQLRARIKELAARAPAWLA-AQDALERLREQSGEALADsqevtaam 632
|
330 340
....*....|....*....|....*....
gi 528517572 1759 QKVLEgKARQLDGLEDKMKAILNAINRQI 1787
Cdd:COG3096 633 QQLLE-REREATVERDELAARKQALESQI 660
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1571-1778 |
1.11e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLA-QIQSETSASERDL 1649
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeAKAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1650 NDavdrlgDLERQIEALKTKRAnnsldAARAEETATMARDKA-NEAKEILDGElsdkyrtvqglmdNKAKTmQDAKHKAE 1728
Cdd:TIGR02794 145 KE------EAAKQAEEEAKAKA-----AAEAKKKAEEAKKKAeAEAKAKAEAE-------------AKAKA-EEAKAKAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1729 QLRDEAKgllKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKA 1778
Cdd:TIGR02794 200 AAKAKAA---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1195-1794 |
1.31e-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: 56.98 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1195 RIVQDLATRTKALTDRAKELQTTGLTRAFERRFKELEdmlAQARDIVNARNATAEAVTtlmgmiEVLRAQIGETtDTLNQ 1274
Cdd:TIGR00606 183 RYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA---CEIRDQITSKEAQLESSR------EIVKSYENEL-DPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1275 QEGDLTAVQDSNYEASNALSTLEREAKELnlnaDQLNRQLDILKNSNFLGAYDSIRASYNKsrdaEHRSNRSTTDTPSTV 1354
Cdd:TIGR00606 253 RLKEIEHNLSKIMKLDNEIKALKSRKKQM----EKDNSELELKMEKVFQGTDEQLNDLYHN----HQRTVREKERELVDC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1355 SQSADTRKKTERLIGQKRDDFnrknaANKRTLTDLNAKVQNLDLKKinekvcgapgdaqcvdspcggagcRDDEGKRRCG 1434
Cdd:TIGR00606 325 QRELEKLNKERRLLNQEKTEL-----LVEQGRLQLQADRHQEHIRA------------------------RDSLIQSLAT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1435 GLNCNGavavadtaLDRSKHAEKELDKAMGVVEElfKQVADAKTKAQEAKD------RAQAALEKASDTKN--------- 1499
Cdd:TIGR00606 376 RLELDG--------FERGPFSERQIKNFHTLVIE--RQEDEAKTAAQLCADlqskerLKQEQADEIRDEKKglgrtielk 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1500 --KVDHSNNDLRDLIKQIRQFlmqEGADPDSIE---AVANRVLELS-------IPASPKQIRHLADEIKDRVKSLSNVDA 1567
Cdd:TIGR00606 446 keILEKKQEELKFVIKELQQL---EGSSDRILEldqELRKAERELSkaeknslTETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1568 ILEQTQNDVRKAEQLLLDAKKARNKAEGVKNtaesVKKALNDASRAQAA-------AEKAIQKAKNDIGLTQNQLAQIQS 1640
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK----IKSRHSDELTSLLGyfpnkkqLEDWLHSKSKEINQTRDRLAKLNK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1641 ETSASERDLN---------------------------DAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANE 1693
Cdd:TIGR00606 599 ELASLEQNKNhinneleskeeqlssyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1694 AKEILD---------GELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLA-ELEKDYEENQKVLE 1763
Cdd:TIGR00606 679 CCPVCQrvfqteaelQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEkEIPELRNKLQKVNR 758
|
650 660 670
....*....|....*....|....*....|.
gi 528517572 1764 GKARQLDGLEdKMKAILNAINRQIQIYNTCQ 1794
Cdd:TIGR00606 759 DIQRLKNDIE-EQETLLGTIMPEEESAKVCL 788
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1594-1785 |
1.38e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1594 EGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIgltqnqlAQIQSETSASERDLNDAVDRLGDLERQIEALKTKR--- 1670
Cdd:PRK02224 226 EEQREQARETRDEADEVLEEHEERREELETLEAEI-------EDLRETIAETEREREELAEEVRDLRERLEELEEERddl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1671 -ANNSLDAArAEETATMARDKANEAKEILDGELSDKyRTVQGLMDNKAKTMQ----DAKHKAEQLRDEAKGLLKDAQ--- 1742
Cdd:PRK02224 299 lAEAGLDDA-DAEAVEARREELEDRDEELRDRLEEC-RVAAQAHNEEAESLRedadDLEERAEELREEAAELESELEear 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528517572 1743 ----DKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINR 1785
Cdd:PRK02224 377 eaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1194-1757 |
1.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1194 DRIVQDLATRTKALTDRAKELQTTGLTRAFERrfKELEDMLAQARDIVNA----RNATAEAVTTLMGMIEVLRAQIGETT 1269
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASA--EEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1270 DTLNQQEGdltavQDSNYEAsNALSTLEREAKELNLNADQLNrqldilknsnFLGAYDSIRASYNKSRDA-EH--RSNRS 1346
Cdd:COG4913 426 AEIASLER-----RKSNIPA-RLLALRDALAEALGLDEAELP----------FVGELIEVRPEEERWRGAiERvlGGFAL 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1347 T----TDTPSTVSQSADTRKKTERLIGQK----RDDFNRKnAANKRTLTDLnakvqnLDLKK------INEKVcGAPGDA 1412
Cdd:COG4913 490 TllvpPEHYAAALRWVNRLHLRGRLVYERvrtgLPDPERP-RLDPDSLAGK------LDFKPhpfrawLEAEL-GRRFDY 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1413 QCVDSPcggagcRDDEGKRRcgglncngavAVADTALDRSKHAEKELDKAMGVVEELF------KQVADAKTKAQEAKDR 1486
Cdd:COG4913 562 VCVDSP------EELRRHPR----------AITRAGQVKGNGTRHEKDDRRRIRSRYVlgfdnrAKLAALEAELAELEEE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1487 AQAALEKASDTKNKVDhSNNDLRDLIKQIRQFLMQEgadpdsieavanrvleLSIPASPKQIRHLADEIKDrvkslsnvd 1566
Cdd:COG4913 626 LAEAEERLEALEAELD-ALQERREALQRLAEYSWDE----------------IDVASAEREIAELEAELER--------- 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1567 aiLEQTQNDVRKAEQLLLDAKKARNkaegvkntaesvkkalndasraqaAAEKAIQKAKNDIGLTQNQLAQIQSETSASE 1646
Cdd:COG4913 680 --LDASSDDLAALEEQLEELEAELE------------------------ELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1647 RDLNDAVDRLGDLERQiealktkrannSLDAARAEEtatMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKhk 1726
Cdd:COG4913 734 DRLEAAEDLARLELRA-----------LLEERFAAA---LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN-- 797
|
570 580 590
....*....|....*....|....*....|....*...
gi 528517572 1727 aEQLRDEAKGL---LKDAQDKLQRLAELEKD----YEE 1757
Cdd:COG4913 798 -REWPAETADLdadLESLPEYLALLDRLEEDglpeYEE 834
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1188-1789 |
1.42e-07 |
|
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: 56.90 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1188 QCFGDWDRIVQDLATRtkaLTDRAKELQTTGLTRAFERRFKELEDMLAQ--ARDIVNARNATAEAvttlmGMIEVLRAQI 1265
Cdd:TIGR00618 304 QIEQQAQRIHTELQSK---MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhSQEIHIRDAHEVAT-----SIREISCQQH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1266 GETTDTLNQQEgDLTAVQDSNYEASNALSTLERE-AKELNLNADQLNRQLDIlknsnflgaydsirASYNKSRDAEHRSN 1344
Cdd:TIGR00618 376 TLTQHIHTLQQ-QKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQL--------------AHAKKQQELQQRYA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1345 RSTTDTPSTVSQSADTRKKTERLIGQKRDDFNRKnAANKRTLTDLNAKVQNLDLKKINEK------VCGAPG--DAQCVD 1416
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ-LQTKEQIHLQETRKKAVVLARLLELqeepcpLCGSCIhpNPARQD 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1417 SPCGGAGCRddegkRRCGGLNcngavavadtaldRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKasd 1496
Cdd:TIGR00618 520 IDNPGPLTR-----RMQRGEQ-------------TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC--- 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1497 tKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVANRVLELSIPASPKQirHLADEIKDRVKSLSNVDAILEQ----- 1571
Cdd:TIGR00618 579 -DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ--DVRLHLQQCSQELALKLTALHAlqltl 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1572 TQNDVR------------KAEQLLLDAKKARNKAEGVKNTAESVKKAlNDASRAQAAAEKAIQKAKNDIgltQNQLAQIQ 1639
Cdd:TIGR00618 656 TQERVRehalsirvlpkeLLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDREFNEI---ENASSSLG 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1640 SETSASERDLNDAvdrLGDLERQieaLKTKRANNSLDAARAEETATMArdkaneakEILDGELSDKYRTVQGLMDNKAKT 1719
Cdd:TIGR00618 732 SDLAAREDALNQS---LKELMHQ---ARTVLKARTEAHFNNNEEVTAA--------LQTGAELSHLAAEIQFFNRLREED 797
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528517572 1720 MQDAKHKAEQLRDEAK--GLLKDAQDKL--QRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQI 1789
Cdd:TIGR00618 798 THLLKTLEAEIGQEIPsdEDILNLQCETlvQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1455-1791 |
1.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.68 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAalekasdTKNKVDHSNNDLRDLIKQIRQflmqegadpdsieavAN 1534
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQ-------LEEELEQARSELEQLEEELEE---------------LN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 RVLElsipASPKQIRHLADEIKDRVKSLSNVDAILEQTQNdvrkaEQLLLDAKKARNKAEgvkntaesvkkalndasraq 1614
Cdd:COG4372 87 EQLQ----AAQAELAQAQEELESLQEEAEELQEELEELQK-----ERQDLEQQRKQLEAQ-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 aaaekaIQKAKNDIGLTQNQLAQIQSEtsaserdLNDAVDRLGDLERQIEALKTKRANNSLDAAR--AEETATMARDKAN 1692
Cdd:COG4372 138 ------IAELQSEIAEREEELKELEEQ-------LESLQEELAALEQELQALSEAEAEQALDELLkeANRNAEKEEELAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1693 EAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGL 1772
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
330
....*....|....*....
gi 528517572 1773 EDKMKAILNAINRQIQIYN 1791
Cdd:COG4372 285 LEALEEAALELKLLALLLN 303
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1034-1089 |
1.68e-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: 49.27 E-value: 1.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNLAS-GQGCE 1089
Cdd:cd00055 2 CDCNGHGSLSGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1091-1132 |
1.78e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 1.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517572 1091 CACDPNNAYTSACNEFTGQCQCRVGFGGKTCTDCQENHWGDP 1132
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1578-1770 |
2.46e-07 |
|
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: 53.78 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1578 KAEQLL----LDAKKARNKAEgvkntAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIqsetsasERDLNDAV 1653
Cdd:COG1579 5 DLRALLdlqeLDSELDRLEHR-----LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-------ELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1654 DRLGDLERQIEALKTkraNNSLDAARAEEtATMARDKANEAKEILDgelsdkyrtvqgLMDnKAKTMQDAKHKAEQLRDE 1733
Cdd:COG1579 73 ARIKKYEEQLGNVRN---NKEYEALQKEI-ESLKRRISDLEDEILE------------LME-RIEELEEELAELEAELAE 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 528517572 1734 AKGLLKDAQDKLQ-RLAELEKDYEENQKVLEGKARQLD 1770
Cdd:COG1579 136 LEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1748 |
2.79e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.99 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEelfKQVADAKTKAQE--AKDRAqAALEKASDTKNKV-DHSNNDLRDLIK-------QIRQflmqega 1524
Cdd:NF041483 332 AEQALADARAEAE---KLVAEAAEKARTvaAEDTA-AQLAKAARTAEEVlTKASEDAKATTRaaaeeaeRIRR------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1525 dpdSIEAVANRvlelsipaspkqIRHLADEIKDRVKSLSNVD-----AILEQTQNDVRK----AEQLLLDAKkarnkAEG 1595
Cdd:NF041483 401 ---EAEAEADR------------LRGEAADQAEQLKGAAKDDtkeyrAKTVELQEEARRlrgeAEQLRAEAV-----AEG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1596 VKNTAESVKKALNDASRAQAAAEKAIQKAKNDigltQNQLAqiQSETSASERDLNDAVDRLGDLERQI-EALKTKRANNS 1674
Cdd:NF041483 461 ERIRGEARREAVQQIEEAARTAEELLTKAKAD----ADELR--STATAESERVRTEAIERATTLRRQAeETLERTRAEAE 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528517572 1675 LDAARAEETATMARDKANEAKEILDGELSdkyRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRL 1748
Cdd:NF041483 535 RLRAEAEEQAEEVRAAAERAARELREETE---RAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERI 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1221-1779 |
2.81e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1221 RAFERRFKELEDMLAQARDIVNA-RNATAEavttlmgMIEVLRaQIGETTDTLNQQEGDLTAVQdSNY----EASNALST 1295
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELiKEKEKE-------LEEVLR-EINEISSELPELREELEKLE-KEVkeleELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1296 LEREAKELNLNADQLNRQLDILKnsnflgayDSIRASYNKSRDAEHRSNRSTTDTPStvsqsadtrKKTERLIGQKRDDF 1375
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELE--------ERIEELKKEIEELEEKVKELKELKEK---------AEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1376 NRKNAANKRTLTDLNAKVQNLD--LKKINEKVcgapgdaqcvdSPCGGAGCRDDEGKRRcgglncngavavadtaLDRSK 1453
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEerIKELEEKE-----------ERLEELKKKLKELEKR----------------LEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1454 HAEKELDKAMGVVEELFKQvadAKTKAQEAKDRAQAALEKASDTKNKVDhsnNDLRDLIKQIRQfLMQEGAD-PDSIEA- 1531
Cdd:PRK03918 359 ERHELYEEAKAKKEELERL---KKRLTGLTPEKLEKELEELEKAKEEIE---EEISKITARIGE-LKKEIKElKKAIEEl 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1532 --------VANRvlELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAK---KARNKAEGVKNTA 1600
Cdd:PRK03918 432 kkakgkcpVCGR--ELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliKLKELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1601 ESVKKaLNdasraqaaAEKAIQKAKnDIGLTQNQLAQIQSETSASERDLNdavdRLGDLERQIEALKTKrannsLDAARA 1680
Cdd:PRK03918 510 EKLKK-YN--------LEELEKKAE-EYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKK-----LDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1681 E--ETATMARDKANEAKEILDGELS------DKYRTVQGL---MDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLA 1749
Cdd:PRK03918 571 ElaELLKELEELGFESVEELEERLKelepfyNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528517572 1750 ELEKDY--EENQKV----------LEGKARQLDGLEDKMKAI 1779
Cdd:PRK03918 651 ELEKKYseEEYEELreeylelsreLAGLRAELEELEKRREEI 692
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1546-1781 |
3.01e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.53 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKdrvkslsnvdaILEQT--QNDVR-KAEQLLLDA-----KKARNKAEGVKNT---AESVKKALNDASRAQ 1614
Cdd:pfam07111 73 QELRRLEEEVR-----------LLRETslQQKMRlEAQAMELDAlavaeKAGQAEAEGLRAAlagAEMVRKNLEEGSQRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 AaaeKAIQKakndigLTQNQLAqiqSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEA 1694
Cdd:pfam07111 142 L---EEIQR------LHQEQLS---SLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1695 KEILDGELS-----DKYRTVQGLMD--------NKAKTMQDAKHKAEQlRDEAKGLLKDAQDKLQRLAELEKDYEENqkv 1761
Cdd:pfam07111 210 QEELEAQVTlveslRKYVGEQVPPEvhsqtwelERQELLDTMQHLQED-RADLQATVELLQVRVQSLTHMLALQEEE--- 285
|
250 260
....*....|....*....|....
gi 528517572 1762 LEGKARQLDGLE----DKMKAILN 1781
Cdd:pfam07111 286 LTRKIQPSDSLEpefpKKCRSLLN 309
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1451-1782 |
3.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1451 RSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmQEGADPDSIE 1530
Cdd:COG4913 268 RERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG---NGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1531 avanrvlelsipaspKQIRHLADEIKDRVKSLSNVDAILEQ-TQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALND 1609
Cdd:COG4913 345 ---------------REIERLERELEERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 ASRAQAAAEKAIQKAKNDI-GLTQNQ----------LAQIQSETSASERDL----------------------------- 1649
Cdd:COG4913 410 AEAALRDLRRELRELEAEIaSLERRKsniparllalRDALAEALGLDEAELpfvgelievrpeeerwrgaiervlggfal 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1650 ------------NDAVDRLgDLERQIEALKTKRANNSLDAARAEEtATMARD---KANEAKEILDGELSDKYR------- 1707
Cdd:COG4913 490 tllvppehyaaaLRWVNRL-HLRGRLVYERVRTGLPDPERPRLDP-DSLAGKldfKPHPFRAWLEAELGRRFDyvcvdsp 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1708 ----------TVQGLM-----------------------DNKAK---------TMQDAKHKAEQLRDEAKGLLKDAQDKL 1745
Cdd:COG4913 568 eelrrhpraiTRAGQVkgngtrhekddrrrirsryvlgfDNRAKlaaleaelaELEEELAEAEERLEALEAELDALQERR 647
|
410 420 430
....*....|....*....|....*....|....*..
gi 528517572 1746 QRLAELEkDYEENQKVLEGKARQLDGLEDKMKAILNA 1782
Cdd:COG4913 648 EALQRLA-EYSWDEIDVASAEREIAELEAELERLDAS 683
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1034-1088 |
3.37e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1034 CTCNFLGTERSQCLSRddcvcqraTGQCQCLPNVIGQTCDHCAPNSWNlASGQGC 1088
Cdd:smart00180 1 CDCDPGGSASGTCDPD--------TGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
982-1027 |
4.09e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 4.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 982 CRCSNNIDLSDpeSCDKRTGQCLkCLYNTEGPDCSVCRSGYYGDAS 1027
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-903 |
4.40e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 4.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517572 861 CQCN--GHADE-CHQRTGACLnCRSNTAGDKCERCANGYYGNPVLG 903
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1456-1782 |
6.12e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1456 EKELDKAMGVVEELFKQVADAK----TKAQEAKdRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegADPDSIEA 1531
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKktetGKAEEAR-KAEEAKKKAEDARKAEEARKAEDARKAEEARK------AEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1532 VANRVLElsipASPKQIRHLADEIKdrvKSLSNVDAILEQTQNDVRKAEqlllDAKKAR--NKAEGVKNtAESVKKAlND 1609
Cdd:PTZ00121 1156 IARKAED----ARKAEEARKAEDAK---KAEAARKAEEVRKAEELRKAE----DARKAEaaRKAEEERK-AEEARKA-ED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 ASRAQAAaeKAIQKAKNDigltqNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEET--ATMA 1687
Cdd:PTZ00121 1223 AKKAEAV--KKAEEAKKD-----AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkADEA 1295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1688 RD-----KANEAKEilDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVL 1762
Cdd:PTZ00121 1296 KKaeekkKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
330 340
....*....|....*....|
gi 528517572 1763 EGKARQLDGLEDKMKAILNA 1782
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA 1393
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
981-1030 |
8.00e-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: 8.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 528517572 981 PCRCSNNIDLSDpeSCDKRTGQCLkCLYNTEGPDCSVCRSGYYGDASRRN 1030
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1443-1675 |
8.42e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.29 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1443 AVADTALDrSKHAEKELdkamgvveelfKQVADAKTKAQ-EAKDRAQAALEKASDTKNKVDHSN------NDLRDLIKQI 1515
Cdd:PRK10929 17 AYAATAPD-EKQITQEL-----------EQAKAAKTPAQaEIVEALQSALNWLEERKGSLERAKqyqqviDNFPKLSAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 RQFLMQEGADPDSIEA-------------VANRVLELS-------------------IPASPKQIRHLADEIKDRVKSLS 1563
Cdd:PRK10929 85 RQQLNNERDEPRSVPPnmstdaleqeilqVSSQLLEKSrqaqqeqdrareisdslsqLPQQQTEARRQLNEIERRLQTLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1564 NVDAILEQTQNDVRKAEQLLLDAK---------KARNKAEGVKNTAESVKKALNDA------------SRAQAAAEKAIQ 1622
Cdd:PRK10929 165 TPNTPLAQAQLTALQAESAALKALvdelelaqlSANNRQELARLRSELAKKRSQQLdaylqalrnqlnSQRQREAERALE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1623 K----AKNDIGLTQNQLAQIQSETSASeRDLNDAVDRLGDL---ERQI--EALKTKRANNSL 1675
Cdd:PRK10929 245 StellAEQSGDLPKSIVAQFKINRELS-QALNQQAQRMDLIasqQRQAasQTLQVRQALNTL 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1450-1763 |
9.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 DRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKvdHSNNDLRDLIKQIRQFLMQEGA----- 1524
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLLLLIAAAllall 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1525 -DPDSIEAVANRVLELSI---------PASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARnkAE 1594
Cdd:COG4717 263 gLGGSLLSLILTIAGVLFlvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE--LL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1595 GVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQnqlAQIQSETSASER-----DLNDAVDRLGDLERQIEALktk 1669
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE---AGVEDEEELRAAleqaeEYQELKEELEELEEQLEEL--- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1670 raNNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQglmdnkaKTMQDAKHKAEQLRDEAK--GLLKDAQDKLQR 1747
Cdd:COG4717 415 --LGELEELLEALDEEELEEELEELEEELE-ELEEELEELR-------EELAELEAELEQLEEDGElaELLQELEELKAE 484
|
330
....*....|....*.
gi 528517572 1748 LAELEKDYEENQKVLE 1763
Cdd:COG4717 485 LRELAEEWAALKLALE 500
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1190-1794 |
9.11e-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: 54.28 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1190 FGDWDRIVQDLATRT---KALTDRAKELQTTGLTRAFER---RFKELEDMLAQARDIVNARNATAEAVTtlmgmiEVLRA 1263
Cdd:TIGR00606 417 LQSKERLKQEQADEIrdeKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRILELDQELRKAER------ELSKA 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1264 QIGETTDTLNQQEGDLtavQDSNYEASNALSTLEREAKELNLNADQLNRQLDILKNSnfLGAYDSIRAsyNKSRDAEHRS 1343
Cdd:TIGR00606 491 EKNSLTETLKKEVKSL---QNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK--MDKDEQIRK--IKSRHSDELT 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1344 NRSTtDTPSTvSQSADTRKKTERLIGQKRDDfnrknaankrtLTDLNAKVQNLDLKK---INEKVCGAPGDAQCVDSPCG 1420
Cdd:TIGR00606 564 SLLG-YFPNK-KQLEDWLHSKSKEINQTRDR-----------LAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1421 GAGCRDDEG-----KRRCGGLNCNGAVAVADTALdRSKHAEKELDKAMG---VVEELFKqvadAKTKAQEAKDRAQAALE 1492
Cdd:TIGR00606 631 VCGSQDEESdlerlKEEIEKSSKQRAMLAGATAV-YSQFITQLTDENQSccpVCQRVFQ----TEAELQEFISDLQSKLR 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1493 KASDtknKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEavanrVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQT 1572
Cdd:TIGR00606 706 LAPD---KLKSTESELKKKEKRRDEMLGLAPGRQSIID-----LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1573 QNDVRKAEQLLLDAKKARNKAEGVKntaESVKKALNDASRAQAA-AEKAIQKAKNDIGLTQNQLAQIQSETSASERDLND 1651
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQMELK---DVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1652 AVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEAKEiLDGELSDKYRTVQGLmdnkAKTMQDAKHKAEQLR 1731
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS-LIREIKDAKEQDSPL----ETFLEKDQQEKEELI 929
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1732 DEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARqlDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ--DGKDDYLKQKETELNTVNAQLEECE 990
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1505-1774 |
9.19e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1505 NNDLRDLIKQIRQFLmqeGADPDSIEAVANRVLE---LSIPAS--PKQI---RhlaDEIKDRVKSLSNVD---------- 1566
Cdd:COG2268 100 NSDPEDIANAAERFL---GRDPEEIEELAEEKLEgalRAVAAQmtVEELnedR---EKFAEKVQEVAGTDlakngleles 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1567 -AI--LEQTQN--D---VRKAEQLLLDAKKARNKAEgvKNTAESVKKALNDASRAQAAAEKAIQKAKndIGLTQNQLAQI 1638
Cdd:COG2268 174 vAItdLEDENNylDalgRRKIAEIIRDARIAEAEAE--RETEIAIAQANREAEEAELEQEREIETAR--IAEAEAELAKK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1639 QSETSASERDLNDAVDRLGDLERQIEALKTKRAnnsLDAARAEETATMARDKANEAKEILDGELS-----DKYRTVQglm 1713
Cdd:COG2268 250 KAEERREAETARAEAEAAYEIAEANAEREVQRQ---LEIAEREREIELQEKEAEREEAELEADVRkpaeaEKQAAEA--- 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1714 dnKAKtmQDAKHKAEQLRDEAKGLLK--DAQDKLQRLAELEKDYEENQKVLEGKARQLDGLED 1774
Cdd:COG2268 324 --EAE--AEAEAIRAKGLAEAEGKRAlaEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1455-1782 |
9.95e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 53.70 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQeakdraqaaLEKASDTKNKVDHSNNDLRDLIKQIrqflmqegadPDSIEAVAN 1534
Cdd:pfam06160 147 AIDELEKQLAEIEEEFSQFEELTESGD---------YLEAREVLEKLEEETDALEELMEDI----------PPLYEELKT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 RVlelsipasPKQIrhlaDEIKDRVKSLS---------NVDAILEQTQNDVRKAEQLL--LDAKKARNKAEGVKNTAESV 1603
Cdd:pfam06160 208 EL--------PDQL----EELKEGYREMEeegyalehlNVDKEIQQLEEQLEENLALLenLELDEAEEALEEIEERIDQL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1604 KKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSET---SASERDLNDAVDRLGDLERQIEALKTKraNNSLDAARA 1680
Cdd:pfam06160 276 YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELervQQSYTLNENELERVRGLEKQLEELEKR--YDEIVERLE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1681 EETA--TMARDKANEAKEILDgELSDKyrtvQGLMDNKAKTM----QDAKHKAEQLRD---EAK---------GL----- 1737
Cdd:pfam06160 354 EKEVaySELQEELEEILEQLE-EIEEE----QEEFKESLQSLrkdeLEAREKLDEFKLelrEIKrlveksnlpGLpesyl 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 528517572 1738 --LKDAQDKLQRLA-ELEK---DYEE-NQKVLEGKArQLDGLEDKMKAILNA 1782
Cdd:pfam06160 429 dyFFDVSDEIEDLAdELNEvplNMDEvNRLLDEAQD-DVDTLYEKTEELIDN 479
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1554-1678 |
1.03e-06 |
|
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: 52.81 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1554 EIKDRVKSLSNVDAILEQTQNDVRKAeqllldakkarnkaegvkntaesvKKALNDASRAQAAAEKAIQKAKNDIGLTQN 1633
Cdd:TIGR04320 248 PIPNPPNSLAALQAKLATAQADLAAA------------------------QTALNTAQAALTSAQTAYAAAQAALATAQK 303
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 528517572 1634 QLAQIQ-SETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAA 1678
Cdd:TIGR04320 304 ELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLA 349
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-494 |
1.08e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517572 454 CKCDPRGTVSGssQCDPVSGDCFCKRLVTGHSCNQCLPEHW 494
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1641-1788 |
1.14e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1641 ETSASERDLNDavdRLGDLERQIEALKTKR--ANNSLDAARAE------ETATMaRDKANEAKEILDgELSDKYRTVQGL 1712
Cdd:COG1340 5 ELSSSLEELEE---KIEELREEIEELKEKRdeLNEELKELAEKrdelnaQVKEL-REEAQELREKRD-ELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1713 MDNKAKTMQDAKHKAEQLRDEAKGL------LKDAQDKLQRL---------------------AELEKDYEENQKVLEGK 1765
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLewrqqtevlspeeekelvekiKELEKELEKAKKALEKN 159
|
170 180
....*....|....*....|....*.
gi 528517572 1766 aRQLDGLEDKMKAI---LNAINRQIQ 1788
Cdd:COG1340 160 -EKLKELRAELKELrkeAEEIHKKIK 184
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1450-1784 |
1.15e-06 |
|
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: 53.90 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 DRSKHAEKELDKAMGVVE---ELFKQVadaktkaqeaKDRAQAALEKASDT--KNKVDHSNNDLRDLIKQIR----QFLM 1520
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEknkELFEQY----------KKDVTELLNKYSALaiKNKFAKTKKDSEIIIKEIKdahkKFIL 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1521 QEGADPDSIEAVANrvlelsipaspKQIRhLADEIKDRVKslSNVDAIleQTQNDVRKAEQLLLDAKKARNKAEGVKNTA 1600
Cdd:TIGR01612 1563 EAEKSEQKIKEIKK-----------EKFR-IEDDAAKNDK--SNKAAI--DIQLSLENFENKFLKISDIKKKINDCLKET 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1601 ESVKKALNDASRAQAAAE---------------KAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVD--RLGDLERQI 1663
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTElkengdnlnslqeflESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKnyEIGIIEKIK 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1664 EALKTKRanNSLDAARAEETATMARD----KANEAKEILDGELSDKYRTVQG-----------LMDNKAKTMQdakhKAE 1728
Cdd:TIGR01612 1707 EIAIANK--EEIESIKELIEPTIENLissfNTNDLEGIDPNEKLEEYNTEIGdiyeefielynIIAGCLETVS----KEP 1780
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1729 QLRDEAKGLLKDAQDKLQRLAELEKDYeeNQKVLEGKARQLDGLEDKMKAILNAIN 1784
Cdd:TIGR01612 1781 ITYDEIKNTRINAQNEFLKIIEIEKKS--KSYLDDIEAKEFDRIINHFKKKLDHVN 1834
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1441-1659 |
1.18e-06 |
|
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: 51.90 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDhsnndlrdLIKQIrqflm 1520
Cdd:smart00283 37 VAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVS--------VIDDI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1521 qegADPD-------SIEA------------VANRVlelsipaspkqiRHLAD-------EIKDRVKSL----SNVDAILE 1570
Cdd:smart00283 104 ---ADQTnllalnaAIEAarageagrgfavVADEV------------RKLAErsaesakEIESLIKEIqeetNEAVAAME 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLLLDAKKARNK-AEGVKNTAESVKKaLNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDL 1649
Cdd:smart00283 169 ESSSEVEEGVELVEETGDALEEiVDSVEEIADLVQE-IAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEEL 247
|
250
....*....|
gi 528517572 1650 NDAVDRLGDL 1659
Cdd:smart00283 248 SGLAEELDEL 257
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1446-1628 |
1.34e-06 |
|
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: 51.46 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1446 DTALDRSKHAEKELDKamgvveelfkQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDL---RDLIKQIRQFLMQe 1522
Cdd:COG1579 16 DSELDRLEHRLKELPA----------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeevEARIKKYEEQLGN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1523 GADPDSIEAVAnrvlelsipaspKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEgvkntaES 1602
Cdd:COG1579 85 VRNNKEYEALQ------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AE 146
|
170 180
....*....|....*....|....*.
gi 528517572 1603 VKKALNDASRAQAAAEKAIQKAKNDI 1628
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAKI 172
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1454-1774 |
1.42e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1454 HAEKeLDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDlikqirqflMQEGADPDSIEAV- 1532
Cdd:PRK04863 346 QQEK-IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD---------YQQALDVQQTRAIq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1533 ---ANRVLElsipaSPKQIRHLADeikdrvKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKN----TAESVKK 1605
Cdd:PRK04863 416 yqqAVQALE-----RAKQLCGLPD------LTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqAYQLVRK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1606 ALNDASRAQA--AAEKAIQKAKNDIGLTQnQLAQIQSETSASERDLNDAvdrlGDLERQIEALKtKRANNSLDAA----R 1679
Cdd:PRK04863 485 IAGEVSRSEAwdVARELLRRLREQRHLAE-QLQQLRMRLSELEQRLRQQ----QRAERLLAEFC-KRLGKNLDDEdeleQ 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AEETATMARDKANEAKEILDGELSDKYRTVQGL------MDNKAKTMQDAKHKAEQLRDEAKGLLKDAQD---KLQRLAE 1750
Cdd:PRK04863 559 LQEELEARLESLSESVSEARERRMALRQQLEQLqariqrLAARAPAWLAAQDALARLREQSGEEFEDSQDvteYMQQLLE 638
|
330 340 350
....*....|....*....|....*....|....
gi 528517572 1751 LEK-------DYEENQKVLEGKARQL---DGLED 1774
Cdd:PRK04863 639 REReltverdELAARKQALDEEIERLsqpGGSED 672
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1560-1779 |
1.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1560 KSLSNVDAIleqtqndVRkaeQLLLDAKKarnkaegVKNTAESVKKALNDASRAQAAAEKAIQKAKndigltqnQLAQIQ 1639
Cdd:COG4913 204 KPIGDLDDF-------VR---EYMLEEPD-------TFEAADALVEHFDDLERAHEALEDAREQIE--------LLEPIR 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1640 setsASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEEtatmarDKANEAKEILDGELSDKyrtvqglmdnkakt 1719
Cdd:COG4913 259 ----ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL------EELRAELARLEAELERL-------------- 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1720 mQDAKHKAEQLRDEAKGLLkdAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAI 1779
Cdd:COG4913 315 -EARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1592-1768 |
1.73e-06 |
|
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: 51.18 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1592 KAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQieALKTKRA 1671
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKA--ADESERG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1672 NNSLDAARAEETATMAR--DKANEAKEIlDGELSDKYRTVQglmdNKAKTMQDAKHKAEQ-----------LRDEAKGL- 1737
Cdd:pfam00261 80 RKVLENRALKDEEKMEIleAQLKEAKEI-AEEADRKYEEVA----RKLVVVEGDLERAEEraelaeskiveLEEELKVVg 154
|
170 180 190
....*....|....*....|....*....|...
gi 528517572 1738 --LKDAQDKLQRLAELEKDYEENQKVLEGKARQ 1768
Cdd:pfam00261 155 nnLKSLEASEEKASEREDKYEEQIRFLTEKLKE 187
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
506-544 |
1.81e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 1.81e-06
10 20 30
....*....|....*....|....*....|....*....
gi 528517572 506 CDCDVGGATENQCSMETGQCQCRSHMIGRQCNQVESGYF 544
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1482-1783 |
2.45e-06 |
|
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: 52.52 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1482 EAKDRAQAALEKasdtknKVDHSNNDLRDLIKQIR------QFLMQEGADPDSI-----EAVANRvlELSIPASPKQI-- 1548
Cdd:pfam10174 390 DVKERKINVLQK------KIENLQEQLRDKDKQLAglkervKSLQTDSSNTDTAlttleEALSEK--ERIIERLKEQRer 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1549 --RHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAK-KARNKAE-GVKNtaESVKKALndasraqaaaEKAIQKA 1624
Cdd:pfam10174 462 edRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKeHASSLASsGLKK--DSKLKSL----------EIAVEQK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1625 KNDIGLTQNQLAQIQS--ETSASERDLNDAVDRL---------------GDLERQIEALK-TKRANNSLDAARAE---ET 1683
Cdd:pfam10174 530 KEECSKLENQLKKAHNaeEAVRTNPEINDRIRLLeqevarykeesgkaqAEVERLLGILReVENEKNDKDKKIAElesLT 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1684 ATMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKL----QRLAELEKDYEENQ 1759
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELdatkARLSSTQQSLAEKD 689
|
330 340
....*....|....*....|....*....
gi 528517572 1760 KVLEG----KARQLDG-LEDKMKAILNAI 1783
Cdd:pfam10174 690 GHLTNlraeRRKQLEEiLEMKQEALLAAI 718
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1455-1765 |
2.65e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQfLMQEGADpdsieavan 1534
Cdd:COG4372 71 ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ-LEAQIAE--------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 rvLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDvrKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQ 1614
Cdd:COG4372 141 --LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 AAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEEtATMARDKANEA 1694
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE-LEALEEAALEL 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 1695 KEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEakgLLKDAQDKLQRLAELEKDYEENQKVLEGK 1765
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI---LLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
267-319 |
3.04e-06 |
|
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: 45.81 E-value: 3.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 267 CFCYGHAS---ECAPiegirddiegmVHGRCVCKHNTKGLNCEQCDDFYNDLPWRP 319
Cdd:cd00055 2 CDCNGHGSlsgQCDP-----------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1564-1774 |
3.15e-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: 51.93 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1564 NVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAEsvKKALNDASRAQAAAEKAIQKAKndigltqnQLAQIQSETS 1643
Cdd:pfam05262 168 NVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKE--RESQEDAKRAQQLKEELDKKQI--------DADKAQQKAD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1644 ASErdlnDAVDRLGDLERQiealKTKRANNSLDAARAEETATMARDKANEAKEIldgelsdkyRTVQGLMDNKAKTMQDA 1723
Cdd:pfam05262 238 FAQ----DNADKQRDEVRQ----KQQEAKNLPKPADTSSPKEDKQVAENQKREI---------EKAQIEIKKNDEEALKA 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 528517572 1724 K-HKAEQLRDEAKGLLKDAQDK-LQRLAELEKDYEENQKVL-EGKARQLDGLED 1774
Cdd:pfam05262 301 KdHKAFDLKQESKASEKEAEDKeLEAQKKREPVAEDLQKTKpQVEAQPTSLNED 354
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1438-1787 |
4.01e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1438 CNGAVAVADTALDRSKH-AEKELDKAMGVVEElfKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHsnndlRDLIKQI- 1515
Cdd:pfam13868 11 LNSKLLAAKCNKERDAQiAEKKRIKAEEKEEE--RRLDEMMEEERERALEEEEEKEEERKEERKRYR-----QELEEQIe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1516 -RQFLMQEGADPDSIEAvaNRVLElsipaspKQIRHLADEIKDRVKSLSNVdailEQTQNDVRKAEQLLLDAK---KARN 1591
Cdd:pfam13868 84 eREQKRQEEYEEKLQER--EQMDE-------IVERIQEEDQAEAEEKLEKQ----RQLREEIDEFNEEQAEWKeleKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1592 KAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNdigltQNQLAQIQSETSA--SERD------LNDAVDRLGDLERQI 1663
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKERE-----IARLRAQQEKAQDekAERDelraklYQEEQERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1664 EALKTKRANNSLDAARAEETATMARDKANEAKEilDGELSDKYRTVQGLMDNKAKtMQDAKhKAEQLRDEAKGLLKDAQD 1743
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAER--EEEEFERMLRKQAEDEEIEQ-EEAEK-RRMKRLEHRRELEKQIEE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528517572 1744 K-LQRLAELEKDYEENQKVLEgkarqldgLEDKMKAILNAINRQI 1787
Cdd:pfam13868 302 ReEQRAAEREEELEEGERLRE--------EEAERRERIEEERQKK 338
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1197-1586 |
4.46e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1197 VQDLATRTKALTDRAKELQTTG--LTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQ 1274
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1275 QEGDLTAVQDSNYEASNALSTLEREAKELNLNADQLNrqldilknsnflgaydsIRASYNKSRDAEHRSNRsttdtpstv 1354
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLN-----------------EEAANLRERLESLERRI--------- 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1355 sqsADTRKKTERLIGQKRDdfnrknaaNKRTLTDLNAKVQNL--DLKKINEKVcgapgdaqcvdspcggagcrDDEGKRR 1432
Cdd:TIGR02168 834 ---AATERRLEDLEEQIEE--------LSEDIESLAAEIEELeeLIEELESEL--------------------EALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1433 cgglncngavAVADTALDRskhAEKELDKAMGVVEELFKQVADAKTKAQEAKDR-AQAALEKASdtknkvdhsnndLRDL 1511
Cdd:TIGR02168 883 ----------ASLEEALAL---LRSELEELSEELRELESKRSELRRELEELREKlAQLELRLEG------------LEVR 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1512 IKQIRQFLMQEGAdpDSIEAVANrvLELSIPASPKQIRHLADEIKDRVKSLSNV--DAI------------LEQTQNDVR 1577
Cdd:TIGR02168 938 IDNLQERLSEEYS--LTLEEAEA--LENKIEDDEEEARRRLKRLENKIKELGPVnlAAIeeyeelkerydfLTAQKEDLT 1013
|
....*....
gi 528517572 1578 KAEQLLLDA 1586
Cdd:TIGR02168 1014 EAKETLEEA 1022
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1472-1780 |
5.23e-06 |
|
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: 51.28 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1472 QVADAKTKAQEAKDRAQAALE-KASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVA--NRVLELSIPASPKQI 1548
Cdd:pfam05557 13 QLQNEKKQMELEHKRARIELEkKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAelNRLKKKYLEALNKKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1549 RH--------------LADEIKDRVKSLSNVDAILEQTQNDV-RKAEQLLLDAKKARNkaegvkntAESVKKALNDASRA 1613
Cdd:pfam05557 93 NEkesqladareviscLKNELSELRRQIQRAELELQSTNSELeELQERLDLLKAKASE--------AEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1614 QAAAEKAIQKAKNDIgltqnqlaQIQSETSASERDLNDAVDRLGDLERQIEALK-------TKRANNSLdaaRAEETATM 1686
Cdd:pfam05557 165 LAEAEQRIKELEFEI--------QSQEQDSEIVKNSKSELARIPELEKELERLRehnkhlnENIENKLL---LKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1687 AR-----DKANEA-------KEILDGELSDKYRTVQ--GL-----MD--NKAKTMQ--DAKHKAEQ--LRDEAKGLLKDA 1741
Cdd:pfam05557 234 KRklereEKYREEaatleleKEKLEQELQSWVKLAQdtGLnlrspEDlsRRIEQLQqrEIVLKEENssLTSSARQLEKAR 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 528517572 1742 QDKLQRLAELEKDYEENQKVLEGKARQLDGLE----------DKMKAIL 1780
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQrrvllltkerDGYRAIL 362
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1441-1749 |
5.75e-06 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 51.15 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEA----KDRAQAALEKASDTKNKVDHSNNDLRDLIKQIR 1516
Cdd:COG5281 132 AAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAAaaaaLAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1517 QFLMQEGADPDSIEAVANRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQ--TQNDVRKAEQLLLDAKKARNKAE 1594
Cdd:COG5281 212 AAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAAAAAALALAAAAElaLTAQAEAAAAAAAAAAAAAQAAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1595 GVKNTAESVKKALNDASRAQA-----AAekaIQKAKNDIGLTQNQLAQIQSETSAserdLNDAVDRLGDLERQIEALKTK 1669
Cdd:COG5281 292 AAAAAAEAQALAAAAAAAAAQlaaaaAA---AAQALRAAAQALAALAQRALAAAA----LAAAAQEAALAAAAAALQAAL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1670 RANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAkhkAEQLRDEAKGLLKDAQDKLQRLA 1749
Cdd:COG5281 365 EAAAAAAAAELAAAGDWAAGAKAALAEYAD-SATNVAAQVAQAATSAFSGLTDA---LAGAVTTGKLLFDALASSIASIA 440
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1597-1774 |
5.91e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1597 KNTAESVKKALnDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLG---DLERQIEalKTKRANN 1673
Cdd:PRK04863 279 NERRVHLEEAL-ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQE--KIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1674 SLDA--ARAEEtATMARDKANEakeildgelsdkyrtvqGLMDNKAKTMQdakhkAEQLRDEAKGLLKDAQdklQRLAEL 1751
Cdd:PRK04863 356 DLEEleERLEE-QNEVVEEADE-----------------QQEENEARAEA-----AEEEVDELKSQLADYQ---QALDVQ 409
|
170 180
....*....|....*....|....*.
gi 528517572 1752 EK---DYEENQKVLEgKARQLDGLED 1774
Cdd:PRK04863 410 QTraiQYQQAVQALE-RAKQLCGLPD 434
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1435-1637 |
9.65e-06 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 50.54 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1435 GLNCNGAVAVADTA--LDRSKHAEKELDKAMGVVEELFKQVA-------------DAKTKAQEAKDRAQAALEKASD--- 1496
Cdd:pfam18971 593 ALNFNKAVAEAKSTgnYDEVKKAQKDLEKSLRKREHLEKEVEkklesksgnknkmEAKAQANSQKDEIFALINKEANrda 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1497 -----TKN----------KVDHSNNDLRDLIKQIRQFLMQEGAD----PDSIEAVANRVLELSI-PASPKQIRHLADEIK 1556
Cdd:pfam18971 673 raiayTQNlkgikrelsdKLEKISKDLKDFSKSFDEFKNGKNKDfskaEETLKALKGSVKDLGInPEWISKVENLNAALN 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1557 DrVKSLSNVD-AILEQTQNDVRKAEQLLLDAKKARNKAEGVkNTAESVKKALNDASRaqaaAEKAIQKAKNdigLTQNQL 1635
Cdd:pfam18971 753 E-FKNGKNKDfSKVTQAKSDLENSVKDVIINQKVTDKVDNL-NQAVSVAKAMGDFSR----VEQVLADLKN---FSKEQL 823
|
..
gi 528517572 1636 AQ 1637
Cdd:pfam18971 824 AQ 825
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1605-1779 |
9.98e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1605 KALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIE-ALK-----------TKRAN 1672
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARlALEkgredlarealERKAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1673 NSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQglmdNKAKTMQdAKHKA----EQLRDEAKGL-LKDAQDKLQR 1747
Cdd:COG1842 96 LEAQAEALEAQLAQLEEQVEKLKEALR-QLESKLEELK----AKKDTLK-ARAKAakaqEKVNEALSGIdSDDATSALER 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 528517572 1748 laelekdYEENQKVLEGKA---RQL---DGLEDKMKAI 1779
Cdd:COG1842 170 -------MEEKIEEMEARAeaaAELaagDSLDDELAEL 200
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1544-1657 |
1.04e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.60 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1544 SPKQIRHLADEIKDRvksLSNVDAILEQTQNDVRKAEQLLLDAK----KARNKAEGVKNTAESVKK-ALNDASRAQAAAE 1618
Cdd:NF012221 1669 SGKQLADAKQRHVDN---QQKVKDAVAKSEAGVAQGEQNQANAEqdidDAKADAEKRKDDALAKQNeAQQAESDANAAAN 1745
|
90 100 110
....*....|....*....|....*....|....*....
gi 528517572 1619 KAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLG 1657
Cdd:NF012221 1746 DAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNRQG 1784
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1450-1775 |
1.18e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1450 DRSK--HAE-KELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKqirqfLMQEgadp 1526
Cdd:pfam01576 89 ERSQqlQNEkKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK-----LLEE---- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 dsieavanRVLELSipaspkqiRHLADEiKDRVKSLSNV----DAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAES 1602
Cdd:pfam01576 160 --------RISEFT--------SNLAEE-EEKAKSLSKLknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1603 V---KKALNDASRAQ-AAAEKAIQKAKNDI-------GLTQNQLAQIQSETSASERDL-------NDAVDRLGDLERQIE 1664
Cdd:pfam01576 223 QiaeLQAQIAELRAQlAKKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLeseraarNKAEKQRRDLGEELE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1665 ALKTKrANNSLDAARA--------------------EET----ATMA--RDKANEAKEILDGELSDKYRTVQGLMDNKA- 1717
Cdd:pfam01576 303 ALKTE-LEDTLDTTAAqqelrskreqevtelkkaleEETrsheAQLQemRQKHTQALEELTEQLEQAKRNKANLEKAKQa 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1718 ------------KTMQDAKHKAEQLRDEAKGLLKDAQDKL-----QRlAELEKDYEENQKVLEGKARQLDGLEDK 1775
Cdd:pfam01576 382 lesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLseserQR-AELAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1544-1786 |
1.23e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1544 SPKQIRHLADEIKDRvKSLSNVDAILEQTQNDVrkaeQLLLDaKKARNKAEgvkntAESVKKALNDASRAQAAAEKAIQK 1623
Cdd:PRK11281 37 TEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQT----LALLD-KIDRQKEE-----TEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1624 AKNDIGLTQNQ------LAQIQSETSASERDLNDAVDRLGDLERQIEALKTK--RANNSLDAA--RAEETATMArDKANE 1693
Cdd:PRK11281 106 LKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQpeRAQAALYANsqRLQQIRNLL-KGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1694 AKEILDGELSDKYRTVQGLMDnkAKTmqdakhkaEQLRDEAKGllkdaQDKLQRLAELEKDYeenqkvlegKARQLDGLE 1773
Cdd:PRK11281 185 GGKALRPSQRVLLQAEQALLN--AQN--------DLQRKSLEG-----NTQLQDLLQKQRDY---------LTARIQRLE 240
|
250
....*....|...
gi 528517572 1774 DKMKAILNAINRQ 1786
Cdd:PRK11281 241 HQLQLLQEAINSK 253
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1546-1675 |
1.47e-05 |
|
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: 46.09 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLlldAKKARNKAEgvkntAESVKkalndasraQAAAEKAIQKAK 1625
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEI---AREAQQNYE-----RELVL---------HAEDIKALQALR 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 1626 NDIGLTQNQLAQIQSETSASERDLNDAVD----RLGDLERQIEALKTKRAN----NSL 1675
Cdd:pfam07926 64 EELNELKAEIAELKAEAESAKAELEESEEsweeQKKELEKELSELEKRIEDlneqNKL 121
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1543-1702 |
1.78e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1543 ASPKQIRHLADeikdrvksLSNVDAILEQTQndvRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQ 1622
Cdd:COG1579 1 AMPEDLRALLD--------LQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1623 KAKNDIGLTQNQLAQI---------QSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANE 1693
Cdd:COG1579 70 EVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
....*....
gi 528517572 1694 AKEILDGEL 1702
Cdd:COG1579 150 ELAELEAEL 158
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1455-1680 |
1.90e-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: 48.18 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQfLMQEGadpdsiEAVAN 1534
Cdd:pfam06008 45 LEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVAT-LGEND------FALPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 RVLElsipASPKQIRHLADEIKDR--VKSLSNVDAILEQTQNDVRKAEQLLldaKKARNKAEGVKNtaeSVKKALNDASR 1612
Cdd:pfam06008 118 SDLS----RMLAEAQRMLGEIRSRdfGTQLQNAEAELKAAQDLLSRIQTWF---QSPQEENKALAN---ALRDSLAEYEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 1613 AQAAAEKAIQKAkndigltQNQLAQIQ---SETSASERDLNDAVDRLGDLERQIEALkTKRANNSLDAARA 1680
Cdd:pfam06008 188 KLSDLRELLREA-------AAKTRDANrlnLANQANLREFQRKKEEVSEQKNQLEET-LKTARDSLDAANL 250
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1603-1782 |
2.06e-05 |
|
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: 47.75 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1603 VKKALNDASRAQAAAEK----AIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKrANNSLDAA 1678
Cdd:pfam04012 9 VRANIHEGLDKAEDPEKmleqAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTK-GNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1679 RAEETATMA---------RDKANEAKEILDGELSDKYRTVQGLMDNK---AKTMQDAKHKAEQLRDEAKGLLKDAQDKLQ 1746
Cdd:pfam04012 88 ALAEKKSLEkqaealetqLAQQRSAVEQLRKQLAALETKIQQLKAKKnllKARLKAAKAQEAVQTSLGSLSTSSATDSFE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528517572 1747 RL----AELE---KDYEENQKV--LEGKARQLDGLEDKMKAILNA 1782
Cdd:pfam04012 168 RIeekiEEREaraDAAAELASAvdLDAKLEQAGIQMEVSEDVLAR 212
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1586-1728 |
2.30e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 49.10 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1586 AKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDlnDAVDRLGDLeRQIEA 1665
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKTD--EAKARAEER-QQKAA 268
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1666 LKTKRANNSLDAARAEetATMARDKANEAKeildgelsDKYRTVQGLMDNKAKTMQDAKHKAE 1728
Cdd:PRK12472 269 QQAAEAATQLDTAKAD--AEAKRAAAAATK--------EAAKAAAAKKAETAKAATDAKLALE 321
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
331-383 |
2.48e-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: 43.11 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 331 CNCNGH---SNQCHFDmavylatgnisGGVCDnCLHNTMGSNCESCKPFYYQDPTR 383
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1546-1786 |
2.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAeSVKKALNDASRAQAAAEKAiqkaK 1625
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDAS----S 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1626 NDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEEtatmardkanEAKEILDGELSDK 1705
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED----------LARLELRALLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1706 YRTVqgLMDNKAKTMQDAkhkAEQLRDEAKGLLKDAQDKLQRL------------AELEKDYEENQKVLEgKARQL--DG 1771
Cdd:COG4913 755 FAAA--LGDAVERELREN---LEERIDALRARLNRAEEELERAmrafnrewpaetADLDADLESLPEYLA-LLDRLeeDG 828
|
250
....*....|....*
gi 528517572 1772 LEDKMKAILNAINRQ 1786
Cdd:COG4913 829 LPEYEERFKELLNEN 843
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1471-1722 |
3.05e-05 |
|
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: 47.33 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1471 KQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegadpdsIEAVANRVLELSIPASPKQIRH 1550
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQL-----------LEEELERTEERLAEALEKLEEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1551 L--ADEIKDRVKSLSNvdaileQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKAL----NDASRAQAAAEKAIQKA 1624
Cdd:pfam00261 70 EkaADESERGRKVLEN------RALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLvvveGDLERAEERAELAESKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1625 K---NDIGLTQNQLAQIQ-SETSASERDlndavdrlGDLERQIEALKTKRANNSLDAARAEETAtMARDKANEAKEILDG 1700
Cdd:pfam00261 144 VeleEELKVVGNNLKSLEaSEEKASERE--------DKYEEQIRFLTEKLKEAETRAEFAERSV-QKLEKEVDRLEDELE 214
|
250 260
....*....|....*....|..
gi 528517572 1701 ELSDKYRTVQGLMDnkaKTMQD 1722
Cdd:pfam00261 215 AEKEKYKAISEELD---QTLAE 233
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
331-382 |
3.32e-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: 42.73 E-value: 3.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 331 CNCNGH---SNQCHFdmavylatgniSGGVCDnCLHNTMGSNCESCKPFYYQDPT 382
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1195-1666 |
4.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1195 RIVQDLATRTKALTDRAKEL--QTTGLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTL 1272
Cdd:COG1196 302 QDIARLEERRRELEERLEELeeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1273 NQQEGDLTAVQDSNYEASNALSTLEREAKELNLNADQLNRQLDILKNS--NFLGAYDSIRASYNKSRDAEHRSNRSTTdt 1350
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEE-- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1351 pSTVSQSADTRKKTERLIGQKRDDFNRKNAANKRTLTDLNAKVQNLDL---KKINEKVCGAPGDAQCVDSPCGGAGCRDD 1427
Cdd:COG1196 460 -ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1428 EGKRRCGGLncnGAVAVADTALDRSKHAEKELDKAMGVVEELfkQVADAKTKAQEAKDRAQAALEKASDTknkVDHSNND 1507
Cdd:COG1196 539 ALEAALAAA---LQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGAAVDL---VASDLRE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1508 LRDLIKQIRQFLMQEGADPDSIEAVANRVLEL------------SIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQND 1575
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLagrlrevtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1576 VRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDigLTQNQLAQIQSETSASERDLNDAVDR 1655
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL--EEEELLEEEALEELPEPPDLEELERE 768
|
490
....*....|.
gi 528517572 1656 LGDLERQIEAL 1666
Cdd:COG1196 769 LERLEREIEAL 779
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1615-1785 |
4.29e-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: 47.02 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 AAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDA-----------ARAEET 1683
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAqqvnaesertlGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1684 ATMARDKANEAKEILD--------------GELSDKYRTVQGLMDN-KAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRL 1748
Cdd:pfam06008 88 AEAIKNLIDNIKEINEkvatlgendfalpsSDLSRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSP 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 528517572 1749 aelekdYEENQKVLEGKARQLDGLEDKMKAILNAINR 1785
Cdd:pfam06008 168 ------QEENKALANALRDSLAEYEAKLSDLRELLRE 198
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1453-1785 |
5.64e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1453 KHAEKELDKAMGVVEElfkqvadAKTKAQEAKDRA--QAALEKASDTKNKvdhsnndlRDLIKQIRQFLMQEGADPDSIE 1530
Cdd:COG3064 8 KAAEAAAQERLEQAEA-------EKRAAAEAEQKAkeEAEEERLAELEAK--------RQAEEEAREAKAEAEQRAAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1531 A-VANRVLElsipaspkqirhlADEIKDRVKSlsnvdAILEQTQNDVRKAEQLLlDAKKARNKAEgVKNTAESVKKALND 1609
Cdd:COG3064 73 AeAAKKLAE-------------AEKAAAEAEK-----KAAAEKAKAAKEAEAAA-AAEKAAAAAE-KEKAEEAKRKAEEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1610 AsRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATM-AR 1688
Cdd:COG3064 133 A-KRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAaAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1689 DKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQ 1768
Cdd:COG3064 212 ADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAA 291
|
330
....*....|....*..
gi 528517572 1769 LDGLEDKMKAILNAINR 1785
Cdd:COG3064 292 AAGLVLDDSAALAAELL 308
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1585-1705 |
5.78e-05 |
|
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: 47.41 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1585 DAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRlgdlerqie 1664
Cdd:TIGR04320 241 GNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQ--------- 311
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 528517572 1665 alKTKRANNSL-DAARAEETATMARDKANEAKEILDGELSDK 1705
Cdd:TIGR04320 312 --ALQTAQNNLaTAQAALANAEARLAKAKEALANLNADLAKK 351
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1489-1789 |
6.19e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1489 AALEKASDtKNKVDHSN----NDLRDLIKQIRQFLMQEGADPDSIEAvanrvlELSIPASPKQIRHLADEIK-------- 1556
Cdd:pfam12128 122 AELGRFMK-NAGIQRTNllntREYRSIIQNDRTLLGRERVELRSLAR------QFALCDSESPLRHIDKIAKamhskegk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1557 -DRVKSLsnVDAILEQ---TQNDVRKAE----------QLLLDAKKARNKAEGVKNTAESVKKA---LNDASRAQAAAEK 1619
Cdd:pfam12128 195 fRDVKSM--IVAILEDdgvVPPKSRLNRqqvehwirdiQAIAGIMKIRPEFTKLQQEFNTLESAelrLSHLHFGYKSDET 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1620 AIQKAKNDIGLTQNQLaqiQSETSASERDLNDAVDRL-GDLERQIEALKTKRANnsLDAAraeETATMARDKANEAKEIL 1698
Cdd:pfam12128 273 LIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSE--LEAL---EDQHGAFLDADIETAAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1699 DGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLK-DAQDKLQRLAE-LEKDYEENQKVLEGKARQLDGLEDKM 1776
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDkLAKIREARDRQLAVAEDDLQALESEL 424
|
330
....*....|...
gi 528517572 1777 KAILNAINRQIQI 1789
Cdd:pfam12128 425 REQLEAGKLEFNE 437
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1571-1748 |
7.11e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 45.01 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLlldakkarnkaegVKNTAESVKKALNDASRAQAAaeKAIQKAKNDIgltQNQLAQIQSetSASErdln 1650
Cdd:cd13769 2 QLSELIQKAQEA-------------INNLAQQVQKQLGLQNPEEVV--NTLKEQSDNF---ANNLQEVSS--SLKE---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1651 DAVDRLGDLERQIEALKTKRANNSLDAARAEETatmaRDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKhkaEQL 1730
Cdd:cd13769 58 EAKKKQGEVEEAWNEFKTKLSETVPELRKSLPV----EEKAQELQAKLQSGLQTLVTESQKLAKAISENSQKAQ---EEL 130
|
170
....*....|....*...
gi 528517572 1731 RDEAKGLLKDAQDKLQRL 1748
Cdd:cd13769 131 QKATKQAYDIAVEAAQNL 148
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1455-1750 |
8.67e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.14 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1455 AEKELDKAMGVVEELFKQVADAKtkaqEAKDRaqaalEKASDTKNKVDHSNNDLRDLIKQIrqflmqegadPDSIEAVAN 1534
Cdd:PRK04778 166 ALDELEKQLENLEEEFSQFVELT----ESGDY-----VEAREILDQLEEELAALEQIMEEI----------PELLKELQT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1535 RVlelsipasPKQIrhlaDEIKDRVKSLS---------NVDAILEQTQNDVRKAEQLL--LDAKKARNKAEG-------- 1595
Cdd:PRK04778 227 EL--------PDQL----QELKAGYRELVeegyhldhlDIEKEIQDLKEQIDENLALLeeLDLDEAEEKNEEiqeridql 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1596 -------------VKNTAESVKKALndaSRAQAA-----------------AEKAIQKAK---NDIGLTQNQLAQIQSET 1642
Cdd:PRK04778 295 ydilerevkarkyVEKNSDTLPDFL---EHAKEQnkelkeeidrvkqsytlNESELESVRqleKQLESLEKQYDEITERI 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1643 SASERDLNDAVDRLGDLERQIEALKTKRA--NNSLDAARAEETAtmARDKANEakeiLDGELSDKYRTVQ-----GL--- 1712
Cdd:PRK04778 372 AEQEIAYSELQEELEEILKQLEEIEKEQEklSEMLQGLRKDELE--AREKLER----YRNKLHEIKRYLEksnlpGLped 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528517572 1713 -MDNKAKT---MQDAKHKAEQLR---DEAKGLLKDAQDKLQRLAE 1750
Cdd:PRK04778 446 yLEMFFEVsdeIEALAEELEEKPinmEAVNRLLEEATEDVETLEE 490
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1479-1791 |
8.77e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1479 KAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAvanrvLELSIPASPKQIRHLADEIKdR 1558
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIER-----LSIEYNNAMDDYNNLKSALN-E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1559 VKSLSNVDAILEQtqnDVRKAEQLLLDAKKARNKaegVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQI 1638
Cdd:PRK01156 244 LSSLEDMKNRYES---EIKTAESDLSMELEKNNY---YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1639 QSETSASErdlnDAVDRLGDLER-QIEALKTKRANNSLDaaraeetatmardkaneaKEILD-GELSDKYRTVQGLMDNK 1716
Cdd:PRK01156 318 DAEINKYH----AIIKKLSVLQKdYNDYIKKKSRYDDLN------------------NQILElEGYEMDYNSYLKSIESL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1717 AKTMQDAKHKAEQLRDEAKGLLK----DAQDKLQRLAELEKDYEEnqkvLEGKARQLDGLEDKMKAILNAINRQIQIYN 1791
Cdd:PRK01156 376 KKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQD----ISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
982-1025 |
9.54e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 528517572 982 CRCsnNIDLSDPESCDKRTGQCLkCLYNTEGPDCSVCRSGYYGD 1025
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1471-1736 |
1.50e-04 |
|
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: 45.37 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1471 KQVADAKTkAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFlmqegadpdsieavanrvlelsipasPKQIRh 1550
Cdd:pfam12795 3 DELEKAKL-DEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDA--------------------------PAELR- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1551 ladEIKDRVKSLSNVDAILEQTQNDVRKAEQLlldakkarnkaegvkntaESvkkALNDASRAQAAAEKAIQKAKNDIGL 1630
Cdd:pfam12795 55 ---ELRQELAALQAKAEAAPKEILASLSLEEL------------------EQ---RLLQTSAQLQELQNQLAQLNSQLIE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1631 TQNQLAQIQSETSASERDLNDAVDRLGDL--------ERQIEALKTKRA-----NNSLDAARA-----EETATMARDKAN 1692
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNRLNGPappgeplsEAQRWALQAELAalkaqIDMLEQELLsnnnrQDLLKARRDLLT 190
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 528517572 1693 EAKEILDGELsdkyRTVQGLMDNK--AKTMQDAKHkAEQLRDEAKG 1736
Cdd:pfam12795 191 LRIQRLEQQL----QALQELLNEKrlQEAEQAVAQ-TEQLAEEAAG 231
|
|
| tape_meas_lam_C |
TIGR01541 |
phage tail tape measure protein, lambda family; This model represents a relatively ... |
1571-1694 |
1.51e-04 |
|
phage tail tape measure protein, lambda family; This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273681 [Multi-domain] Cd Length: 332 Bit Score: 45.99 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1571 QTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDI-----------GLTQ------N 1633
Cdd:TIGR01541 7 TQQIADRKLKKLNTADEKSLQSRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIraqnkrqldrfGLGDkqrerlD 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 1634 QLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEA 1694
Cdd:TIGR01541 87 ARLQIDRTFRKQQRDLNKAMTAKGLAGSDLYKEQLAAIKASLNEALAELHAYYAAEDALQG 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1441-1647 |
1.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLM 1520
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1521 QEGA--------------------------------DPDSIEAVANRV--LELSIPASPKQIRHLA---DEIKDRVKSLS 1563
Cdd:COG4942 91 EIAElraeleaqkeelaellralyrlgrqpplalllSPEDFLDAVRRLqyLKYLAPARREQAEELRadlAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1564 NVDAILEQTQNDVRKAEQLLLDAKKARnkaegvkntaesvKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETS 1643
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAER-------------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....
gi 528517572 1644 ASER 1647
Cdd:COG4942 238 AAAE 241
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1205-1399 |
1.65e-04 |
|
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: 46.49 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1205 KALTDRAKELQTTGLTRAFERRFKELEDML-AQARDIVNARNATAEAVTTL---------MGMIEVLRAQIGETTDTL-N 1273
Cdd:COG5185 309 KATESLEEQLAAAEAEQELEESKRETETGIqNLTAEIEQGQESLTENLEAIkeeienivgEVELSKSSEELDSFKDTIeS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1274 QQEGDLTAVQDSNYEASNALSTLEREAKELNLNADQLNRQLDILKNSNFlgaydsirASYNKSRDAEHRSNRSTTDTPST 1353
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE--------EVSKLLNELISELNKVMREADEE 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528517572 1354 VSQSADTR-KKTERLIGQKRDDFNRKNAANKRTLTDLNAKVQNLDLK 1399
Cdd:COG5185 461 SQSRLEEAyDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAK 507
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1577-1669 |
1.67e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 43.16 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1577 RKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRA---QAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAV 1653
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKesqAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDLL 80
|
90
....*....|....*.
gi 528517572 1654 DRLGDLERQIEALKTK 1669
Cdd:pfam04871 81 LLLGDLEEKVEKYKAR 96
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1551-1637 |
1.92e-04 |
|
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: 45.87 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1551 LADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESV------------KKALNDASRAQAAAE 1618
Cdd:TIGR04320 252 PPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElanaqaqalqtaQNNLATAQAALANAE 331
|
90
....*....|....*....
gi 528517572 1619 KAIQKAKNDIGLTQNQLAQ 1637
Cdd:TIGR04320 332 ARLAKAKEALANLNADLAK 350
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1546-1792 |
2.33e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSL-SNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNT-----------AESVKKALN--DAS 1611
Cdd:PRK04778 101 RKAKHEINEIESLLDLIeEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSllanrfsfgpaLDELEKQLEnlEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1612 RAQA----------AAEKAIQKAKNDIGLTQNQLAQI-------QSETSASERDLNDAVDRL---------GDLERQIEA 1665
Cdd:PRK04778 181 FSQFveltesgdyvEAREILDQLEEELAALEQIMEEIpellkelQTELPDQLQELKAGYRELveegyhldhLDIEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1666 LKTKRANN-----SLDAARAEETATMARDKANEAKEILDGELsDKYRTVQGLMDNKAKTMQDAKHKAEQLRDE------- 1733
Cdd:PRK04778 261 LKEQIDENlalleELDLDEAEEKNEEIQERIDQLYDILEREV-KARKYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqs 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1734 ---AKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAI----NRQIQIYNT 1792
Cdd:PRK04778 340 ytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLeeieKEQEKLSEM 405
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1192-1754 |
2.72e-04 |
|
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: 46.16 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1192 DWDRIVQDLATRTKALTDRAKELQTTGLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMI-----EVLRAQIG 1266
Cdd:COG5271 299 ADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEdeaagEAADESEG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1267 ETTDTLNQQEGDLTAVQDSNYEASNALSTLE-REAKELNLNADQL-------NRQLDILKNSNFLGAYDSIRASYNKSRD 1338
Cdd:COG5271 379 ADTDAAADEADAAADDSADDEEASADGGTSPtSDTDEEEEEADEDasageteDESTDVTSAEDDIATDEEADSLADEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1339 AEHRSNRSTTDTPSTVSQSADTRKKTERLIGQKRDDFNRKNAANKRTL---------------TDLNAKVQNLDLKKINE 1403
Cdd:COG5271 459 AEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSdeltaeetsaddgadTDAAADPEDSDEDALED 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1404 KVCGAPgDAQCVDSPcggagcrDDEGKRRCGGLNCNGAVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEA 1483
Cdd:COG5271 539 ETEGEE-NAPGSDQD-------ADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1484 -KDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLMQEGADPDSIEAVANRVLELSIPASPKQIRHLADEIKDRVKSL 1562
Cdd:COG5271 611 dDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1563 SNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSET 1642
Cdd:COG5271 691 ASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLE 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1643 SASERDLNDAVDRLGDLERQIEALKTKRAN-----NSLDAARAEETATMARDKANEAKEILDGELSDKYRTVQGlMDNKA 1717
Cdd:COG5271 771 EALEEEKADAEEAATDEEAEAAAEEKEKVAdedqdTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAE-DDEED 849
|
570 580 590
....*....|....*....|....*....|....*..
gi 528517572 1718 KTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKD 1754
Cdd:COG5271 850 DDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDAD 886
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1688-1788 |
3.22e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1688 RDKANEAKEIL--DGELSDKyrtvqglmdnkAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGK 1765
Cdd:cd16269 177 QSKEAEAEAILqaDQALTEK-----------EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK 245
|
90 100
....*....|....*....|...
gi 528517572 1766 arqldgLEDKMKAILNAINRQIQ 1788
Cdd:cd16269 246 ------MEEERENLLKEQERALE 262
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1618-1788 |
3.46e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 43.88 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1618 EKAIQKAKNDIGLTQNQLAQI----------QSETSASERDLNDAVDRLGDLERQiEALKTKRANNSLdAARAEETATMA 1687
Cdd:cd07596 3 DQEFEEAKDYILKLEEQLKKLskqaqrlvkrRRELGSALGEFGKALIKLAKCEEE-VGGELGEALSKL-GKAAEELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1688 RDKANEAKEILDGELSDKYRTVQGLMD------NKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKV 1761
Cdd:cd07596 81 EAQANQELVKLLEPLKEYLRYCQAVKEtlddraDALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESA 160
|
170 180
....*....|....*....|....*..
gi 528517572 1762 LEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:cd07596 161 LEEARKRYEEISERLKEELKRFHEERA 187
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1446-1788 |
4.26e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.59 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1446 DTALDrSKHAEKELDKAMGVVEELFKQVADA-KTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFL--MQE 1522
Cdd:PTZ00440 393 ETLLD-SEYFISKYTNIISLSEHTLKAAEDVlKENSQKIADYALYSNLEIIEIKKKYDEKINELKKSINQLKTLIsiMKS 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1523 G-----ADPDSIEAVANRVLELSIPASP-KQIRHLADEIKDRVKSlsnvdaILEQTQNDVRKAEQLlldaKKARNKAEG- 1595
Cdd:PTZ00440 472 FydliiSEKDSMDSKEKKESSDSNYQEKvDELLQIINSIKEKNNI------VNNNFKNIEDYYITI----EGLKNEIEGl 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1596 ---VKNTAESVKKALNDasraqaaaEKAIQKAKNDIgltQNQLAQIqSETSASERDLNDAVDRLGDLERQIEALktkran 1672
Cdd:PTZ00440 542 ielIKYYLQSIETLIKD--------EKLKRSMKNDI---KNKIKYI-EENVDHIKDIISLNDEIDNIIQQIEEL------ 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1673 NSLDAARAEETATMARDKANEAKEILDgELSDkyRTVQGLMDNKAKTMQDAK---HKAEQLRDeAKGLLKDAQDKLQRLA 1749
Cdd:PTZ00440 604 INEALFNKEKFINEKNDLQEKVKYILN-KFYK--GDLQELLDELSHFLDDHKylyHEAKSKED-LQTLLNTSKNEYEKLE 679
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528517572 1750 ELEKDYEENQ-KVLEGKARQLDGLEDK-MKAILNAINRQIQ 1788
Cdd:PTZ00440 680 FMKSDNIDNIiKNLKKELQNLLSLKENiIKKQLNNIEQDIS 720
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1621-1779 |
4.34e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1621 IQKAK--NDIGLTQNQLAQIQSETS-ASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARA--EETATMARDKANEAK 1695
Cdd:pfam06160 31 LSKVKklNLTGETQEKFEEWRKKWDdIVTKSLPDIEELLFEAEELNDKYRFKKAKKALDEIEEllDDIEEDIKQILEELD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1696 EILD---------GELSDKYRTVQglmdnkaKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAEL--EKDYEENQKVLEG 1764
Cdd:pfam06160 111 ELLEseeknreevEELKDKYRELR-------KTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELteSGDYLEAREVLEK 183
|
170
....*....|....*
gi 528517572 1765 KARQLDGLEDKMKAI 1779
Cdd:pfam06160 184 LEEETDALEELMEDI 198
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1541-1792 |
4.49e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1541 IPASPKQIRHLADEIKDRVKSLSNVDA---ILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAAA 1617
Cdd:PRK01156 144 ISGDPAQRKKILDEILEINSLERNYDKlkdVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1618 EKAIQKAKNDIGL---TQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKT-----KRANNSLDAARAEETATMARD 1689
Cdd:PRK01156 224 SIEYNNAMDDYNNlksALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEleerhMKIINDPVYKNRNYINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1690 KAN--EAKEIL---DGELSDKYRTVQGLMD---------NKAKTMQDAKHKAEQLR---DEAKGLLKDAQDKLQRLAELE 1752
Cdd:PRK01156 304 KNDieNKKQILsniDAEINKYHAIIKKLSVlqkdyndyiKKKSRYDDLNNQILELEgyeMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528517572 1753 KDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQIYNT 1792
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISS 423
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1529-1782 |
4.98e-04 |
|
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: 44.95 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1529 IEAVANRVLELSIPASPKQIRHLADEIKDRVKSLsnVDAILEQTQNDVRKAEQLLLDAKKARNKAEG-VKNTAESVKKAL 1607
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKL--VEQNTDLRLEKLGENAESSKRLNENANNLIKqFENTKEKIAEYT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1608 NDASRAQAAAEKAIQKAKNDIgltQNQLAQIQSETSASERDLNDAVDR-LGDLERQIEALKTKRAN--NSLDAARAEETA 1684
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEA---EQELEESKRETETGIQNLTAEIEQgQESLTENLEAIKEEIENivGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1685 TMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEakgllkdaqdklqrLAELEKDYEENQKVLEG 1764
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ--------------IEQATSSNEEVSKLLNE 445
|
250
....*....|....*...
gi 528517572 1765 KARQLDGLEDKMKAILNA 1782
Cdd:COG5185 446 LISELNKVMREADEESQS 463
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1547-1788 |
6.09e-04 |
|
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: 43.56 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1547 QIRHLADEIKDRVKSLSN--VDA-ILEQTQNDV-RKAEQLLLDAKKARNKAEGVKNTAEsvkKALNDASRAQAAAEKAIQ 1622
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAhkIQIeILEKELSSLaQETEELQKKATQTLAKAQQVNAESE---RTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1623 KAKNDIGLTQnQLAQIQSETSASE--RDLNDAVDRLGDLerQIEALKTKRANNSLDAARAEETatMARdkANEAKEILDG 1700
Cdd:pfam06008 97 NIKEINEKVA-TLGENDFALPSSDlsRMLAEAQRMLGEI--RSRDFGTQLQNAEAELKAAQDL--LSR--IQTWFQSPQE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1701 ELSDKYRTVQGLMDNKAKTMQDAkhkaEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAIL 1780
Cdd:pfam06008 170 ENKALANALRDSLAEYEAKLSDL----RELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSL 245
|
....*...
gi 528517572 1781 NAINRQIQ 1788
Cdd:pfam06008 246 DAANLLLQ 253
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1527-1794 |
6.49e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1527 DSIEAVANRVLELSIPASpkQIRHLADEIKDRVKSLSNVDAILEQTQNDVRK-AEQLLLDAKKARNKAEGVKNTAESVK- 1604
Cdd:pfam04108 14 ELLTDARSLLEELVVLLA--KIAFLRRGLSVQLANLEKVREGLEKVLNELKKdFKQLLKDLDAALERLEETLDKLRNTPv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1605 -KALNDASRAQA-----AAEKAIQKAKNDIgltQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAA 1678
Cdd:pfam04108 92 ePALPPGEEKQKtlldfIDEDSVEILRDAL---KELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1679 RAEETATMardkANEAKEILDgELSDKYRtvqglmdnkaKTMQDAKHKAEQLRDEAKGLLKDAQD------KLQ-RLAEL 1751
Cdd:pfam04108 169 LLKELESL----EEEMASLLE-SLTNHYD----------QCVTAVKLTEGGRAEMLEVLENDARElddvvpELQdRLDEM 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1752 EKDYEENQKVLEGKA----------RQLDGLEDKMKAILNAINRQIQIYNTCQ 1794
Cdd:pfam04108 234 ENNYERLQKLLEQKNslidellsalQLIAEIQSRLPEYLAALKEFEERWEEEK 286
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1570-1787 |
6.71e-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: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1570 EQTQNDVRKAEQLLLDAKKARNKAEgvKNTAESVKKALNDAsRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSA-SERD 1648
Cdd:COG3064 66 QRAAELAAEAAKKLAEAEKAAAEAE--KKAAAEKAKAAKEA-EAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAeEERK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1649 LNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAE 1728
Cdd:COG3064 143 AAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1729 QLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQI 1787
Cdd:COG3064 223 ARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVV 281
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1538-1734 |
6.76e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1538 ELSIPASpKQIrhLADEIKD-RVKSLSN---VDAILEQTQNDVRKAEQLL--------LDAKKARNKAEGVKNTAESVKK 1605
Cdd:pfam05262 155 QIVIPLK-KNI--LSGNVSDvDTDSISDkkvVEALREDNEKGVNFRRDMTdlkeresqEDAKRAQQLKEELDKKQIDADK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1606 ALNDASRAQAAAEKaiQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLER-QIEalkTKRANNSLDAARAEETA 1684
Cdd:pfam05262 232 AQQKADFAQDNADK--QRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKaQIE---IKKNDEEALKAKDHKAF 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1685 TMARDKANEAKEILDGELSDKyRTVQGLMDNKAKTMQDAKHKAEQLRDEA 1734
Cdd:pfam05262 307 DLKQESKASEKEAEDKELEAQ-KKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1228-1396 |
7.14e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1228 KELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQQEGDLTAVQDSNYEASNALSTLEREAKELN--- 1304
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1305 ---LNADQLNRQLD----ILKNSNFLGAYDSIR--ASYNKSRDAEHRSNRSTTDTPSTVSQSADTRKKT-ERLIG---QK 1371
Cdd:COG4942 107 aelLRALYRLGRQPplalLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAElEALLAeleEE 186
|
170 180
....*....|....*....|....*
gi 528517572 1372 RDDFNRKNAANKRTLTDLNAKVQNL 1396
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAEL 211
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1680-1794 |
7.42e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1680 AEETATMARDKA------NEAKEILDgELSDKYRTVQ---GLMDNKAKTMQDAKHK-AEQLRDEAKGLLKDAQDKLQRLA 1749
Cdd:smart00787 150 DENLEGLKEDYKllmkelELLNSIKP-KLRDRKDALEeelRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 528517572 1750 ELEKDYEENQKVLEGKArqldgleDKMKAILNAINRQIQIYNTCQ 1794
Cdd:smart00787 229 ELEEELQELESKIEDLT-------NKKSELNTEIAEAEKKLEQCR 266
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1451-1625 |
8.64e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1451 RSKHAEKELDKAmgvvEELFKQVADAKTKAQEAKDRAQAALEK-ASDTKNKVDHSNNDLRDLIKQIrqflmQEGADPDSI 1529
Cdd:PRK09510 102 RLKQLEKERLAA----QEQKKQAEEAAKQAALKQKQAEEAAAKaAAAAKAKAEAEAKRAAAAAKKA-----AAEAKKKAE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1530 EAVANRvlelsipASPKQIRHLADEIKDRVKSLSNVDAILEQTQndvrKAEQLllDAKKARNKAEGVKNTAESVKKALND 1609
Cdd:PRK09510 173 AEAAKK-------AAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK----KAAAE--AKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170
....*....|....*.
gi 528517572 1610 ASRAQAAAEKAIQKAK 1625
Cdd:PRK09510 240 KAAAAKAAEKAAAAKA 255
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1587-1787 |
9.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1587 KKARNKAEGVKNTAESVkkaLNDASR-AQAAAEKAIQKAKNDIgltqnqlAQIQSETsasERDLNDAVDRLGDLERQIEa 1665
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI---LEEAKKeAEAIKKEALLEAKEEI-------HKLRNEF---EKELRERRNELQKLEKRLL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1666 lktkrannsldaaRAEETAtmarDKANEAKEILDGELSDKYRTVQGLMDNkaktmqdakhkAEQLRDEAKGLLKDAQDKL 1745
Cdd:PRK12704 93 -------------QKEENL----DRKLELLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQEL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528517572 1746 QRLAELEKDyeenqkvlEGKARQLDGLEDKMKAILNAINRQI 1787
Cdd:PRK12704 145 ERISGLTAE--------EAKEILLEKVEEEARHEAAVLIKEI 178
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1446-1719 |
1.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1446 DTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIrQFLMQEgad 1525
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL-ESLQEE--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1526 pdsIEAVANRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKK 1605
Cdd:COG4372 166 ---LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1606 ALNDASRAQAAAEKAIQkakNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETAT 1685
Cdd:COG4372 243 ELEEDKEELLEEVILKE---IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
250 260 270
....*....|....*....|....*....|....
gi 528517572 1686 MARDKANEAKEILDGELSDKYRTVQGLMDNKAKT 1719
Cdd:COG4372 320 ALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1198-1408 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1198 QDLATRTKALTDRAKELQTtgLTRAFERRFKELEDMLAQARDIVNARNATAEAVTTLMGMIEVLRAQIGETTDTLNQQEG 1277
Cdd:COG4372 87 EQLQAAQAELAQAQEELES--LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1278 DLTAVQ--DSNYEASNALSTLEREAKELNLNADQLnRQLDILKNSNFLGAYDSIRASYNKSRDAEHRSNRSTTDTPSTVS 1355
Cdd:COG4372 165 ELAALEqeLQALSEAEAEQALDELLKEANRNAEKE-EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1356 QSADTRKKTERLIGQKRDDFNRKNAANKRTLTDLNAKVQNLDLKKINEKVCGA 1408
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
290-322 |
1.34e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|...
gi 528517572 290 VHGRCVCKHNTKGLNCEQCDDFYNDLPWRPAEG 322
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1546-1791 |
1.45e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1546 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVR---------KAEQLLLDAKKARNKAEGVKNTAESVK--KALNDASRAQ 1614
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINnsnnkikilEQQIKDLNDKLKKNKDKINKLNSDLSKinSEIKNDKEQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 AAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKR---------ANNSLDAARAEETAT 1685
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnllekeklnIQKNIDKIKNKLLKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1686 MAR----DKANEAKEILDGELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGL--LKDAQDKLQrlaeleKDYEENQ 1759
Cdd:TIGR04523 200 ELLlsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLnqLKDEQNKIK------KQLSEKQ 273
|
250 260 270
....*....|....*....|....*....|..
gi 528517572 1760 KVLEGKARQLDGLEDKmkaiLNAINRQIQIYN 1791
Cdd:TIGR04523 274 KELEQNNKKIKELEKQ----LNQLKSEISDLN 301
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1449-1594 |
1.51e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1449 LDRSKHAEKELDKAMGV---VEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFlmQEGAD 1525
Cdd:COG1340 149 LEKAKKALEKNEKLKELraeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--QEKAD 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 1526 pdsieavanrvlELSipaspKQIRHLADEIKDRVKSLSNvdaiLEQTQNDVRKAEqlllDAKKARNKAE 1594
Cdd:COG1340 227 ------------ELH-----EEIIELQKELRELRKELKK----LRKKQRALKREK----EKEELEEKAE 270
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1581-1788 |
1.53e-03 |
|
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: 42.74 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1581 QLLLDAKKARNKAEgvkntAESVKKALNDASRAQAaaeKAIQKAKNDIGLTQNQLAQIQSETSASERDLND--------- 1651
Cdd:cd22656 98 ELIDDLADATDDEE-----LEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETlekalkdll 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1652 -------AVDRLGDLERQIEALK---TKRANNSLDAARAEEtatmardKANEAKEILDGELSDKYRTVQGLMDNKAKTMQ 1721
Cdd:cd22656 170 tdeggaiARKEIKDLQKELEKLNeeyAAKLKAKIDELKALI-------ADDEAKLAAALRLIADLTAADTDLDNLLALIG 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1722 DAKHKAEQLRDEAKGLLKDaqdkLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:cd22656 243 PAIPALEKLQGAWQAIATD----LDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
331-384 |
1.61e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 331 CNCNG---HSNQCHFDmavylatgnisGGVCDnCLHNTMGSNCESCKPFYYQDPTRD 384
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| BAR_RhoGAP_Rich-like |
cd07595 |
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ... |
1577-1754 |
1.65e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.
Pssm-ID: 153279 [Multi-domain] Cd Length: 244 Bit Score: 42.32 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1577 RKAEQL---LLDAKKarnKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDigltQNQLAQIQSETSA---SERDLN 1650
Cdd:cd07595 8 EKTEVLsdeLLQIEK---RVEAVKDACQNIHKKLISCLQGQSGEDKDKRLKKLP----EYGLAQSMLESSKelpDDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1651 DAVDRLGDL-----------ERQIEALKTKRANNSLDaaraEETATMARDKANEAKEILDGE-LSDKYRTVqglmdNKAK 1718
Cdd:cd07595 81 KVLKLCGEAqntlarelvdhEMNVEEDVLSPLQNILE----VEIPNIQKQKKRLSKLVLDMDsARSRYNAA-----HKSS 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 528517572 1719 TMQDAKHKAEQLRDEakgllkdaQDKLQRLAELEKD 1754
Cdd:cd07595 152 GGQGAAAKVDALKDE--------YEEAELKLEQCRD 179
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
910-980 |
1.66e-03 |
|
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: 38.10 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517572 910 PCPCPEGPNSGrhfaASCYQDNrsqqVVCNCNQGYTGtvkrsagavlnrPRCDECAPGYFGDPSKPGGqCQ 980
Cdd:cd00055 1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTG------------RRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1441-1784 |
1.66e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.09 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1441 AVAVADTALDRSKHAEKELDKAMGVVEELFKQVADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNDLRDLIKQIRQFLM 1520
Cdd:COG0840 40 LTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1521 QEGADPDSIEAVANRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTA 1600
Cdd:COG0840 120 LAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1601 ESVKKALndASRAQAAAEKAIQKAKNDigLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIealktKRANNSLDAArA 1680
Cdd:COG0840 200 LLLSRSI--TRPLRELLEVLERIAEGD--LTVRIDVDSKDEIGQLADAFNRMIENLRELVGQV-----RESAEQVASA-S 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1681 EETATMARDKANEAKEildgeLSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQK 1760
Cdd:COG0840 270 EELAASAEELAAGAEE-----QAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRE 344
|
330 340
....*....|....*....|....
gi 528517572 1761 VLEGKARQLDGLEDKMKAILNAIN 1784
Cdd:COG0840 345 SVEETAETIEELGESSQEIGEIVD 368
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1649-1788 |
1.73e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1649 LNDAVDRLGDLERQIEaLKTKRANNSLDAARAEETATMARDKANEAKeildgelsdkyrtvqglmdnkaktMQDAKHKAE 1728
Cdd:COG1842 14 INALLDKAEDPEKMLD-QAIRDMEEDLVEARQALAQVIANQKRLERQ------------------------LEELEAEAE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1729 QLRDEAKGLLKDAQDKL-----QRLAELEKDYEENQKVLEgkarQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG1842 69 KWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA----QLEEQVEKLKEALRQLESKLE 129
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1585-1788 |
2.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1585 DAKKARNKAEGVKNT--AESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETS--ASERDLNDAVDRLGDLE 1660
Cdd:COG3206 146 DPELAAAVANALAEAylEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1661 RQIEALKTKRAnnsldaaraeetatmardkaneakeildgELSDKYRTVQGLMDNKAKTMqdakhkAEQLRDEAkgllkd 1740
Cdd:COG3206 226 SQLAEARAELA-----------------------------EAEARLAALRAQLGSGPDAL------PELLQSPV------ 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528517572 1741 AQDKLQRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINRQIQ 1788
Cdd:COG3206 265 IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
|
| PHA00430 |
PHA00430 |
tail fiber protein |
1543-1695 |
2.05e-03 |
|
tail fiber protein
Pssm-ID: 222790 [Multi-domain] Cd Length: 568 Bit Score: 42.96 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1543 ASPKQIRHLADEIKDRvkslsnvDAI-LEQTQ-------NDVRKAEQLLLDAKKARNKAEGVKNTAeSVKKALNDASRAQ 1614
Cdd:PHA00430 131 ARGRRIVNLADAVDDG-------DAVpLGQIKtwnqsawNARNEANRSRNEADRARNQAERFNNES-GASATNTKQWRSE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1615 AAAEK-AIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTKRANNSLDAARAEETATMARDKANE 1693
Cdd:PHA00430 203 ADGSNsEANRFKGYADSMTSSVEAAKGQAESSSKEANTAGDYATKAAASASAAHASEVNAANSATAAATSANRAKQQADR 282
|
..
gi 528517572 1694 AK 1695
Cdd:PHA00430 283 AK 284
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1522-1694 |
2.19e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1522 EGADPDSIEAVANRVLELSipaspkqiRHLADEIKDRVKSlsnvDAIlEQTQNDVRKAEQLLLDAKKA----RNKaEGVK 1597
Cdd:COG3524 145 RAFDPEDAQAIAEALLAES--------EELVNQLSERARE----DAV-RFAEEEVERAEERLRDAREAllafRNR-NGIL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1598 NTAESVKKALNDASRAQAaaekaiQKAKndiglTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKTK----RANN 1673
Cdd:COG3524 211 DPEATAEALLQLIATLEG------QLAE-----LEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARltgaSGGD 279
|
170 180
....*....|....*....|..
gi 528517572 1674 SLDAARAE-ETATMARDKANEA 1694
Cdd:COG3524 280 SLASLLAEyERLELEREFAEKA 301
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1565-1775 |
2.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1565 VDAILEqtqND------VRKAEQLLlDAKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKNDIGLTQNQLAQI 1638
Cdd:PRK03918 137 IDAILE---SDesrekvVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1639 QSETSASERDLNDAVDRLGDLER---QIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLmdn 1715
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKEL--- 288
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1716 kaktmqdaKHKAEQLRdEAKGLLKDAQDKLQRLAELEKDYEENQKVLEgkaRQLDGLEDK 1775
Cdd:PRK03918 289 --------KEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIE---ERIKELEEK 336
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1582-1778 |
2.22e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 42.64 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1582 LLLDAKKARNKAEGVKNTAESVKKAlNDASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAvdrlGDLER 1661
Cdd:PRK15374 13 YTQNPRLAEAAFEGVRKNTDFLKAA-DKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAAREKLSSE----GQLTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1662 QIEALKTKRANNSLDAARAEETATMARDKANEAKEIldgELSDKYRTVQGLMDNKAKTMQDAKHK---AEQLRDEAKGLL 1738
Cdd:PRK15374 88 LLGKLMTLLGDVSLSQLESRLAVWQAMIESQKEMGI---QVSKEFQTALGEAQEATDLYEASIKKtdtAKSVYDAAEKKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 528517572 1739 KDAQDKLQRLAELEKDYEENQKVLEGKARqlDGLEDKMKA 1778
Cdd:PRK15374 165 TQAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAKEAL 202
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1554-1784 |
2.27e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1554 EIKDRVKSLSNvdaILEQTQNDVRKAEQLlldaKKARNKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKND----IG 1629
Cdd:PTZ00440 857 EFNENNQIVDN---IIKDIENMNKNINII----KTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDniiqKN 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1630 LTQNQLAQIQSETSASERDLNDAvdRLGDLERQIEAL-----KTKRANNSLDAARAEETatmarDKANEAKEILDGE--- 1701
Cdd:PTZ00440 930 EKLNLLNNLNKEKEKIEKQLSDT--KINNLKMQIEKTleyydKSKENINGNDGTHLEKL-----DKEKDEWEHFKSEidk 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1702 LSDKYRTVQGLMDNKAKT------------MQDAKHKAEQLRDEAKGLLKDAQDKLQRLaELEKDYEENQKVLegKARQL 1769
Cdd:PTZ00440 1003 LNVNYNILNKKIDDLIKKqhddiielidklIKEKGKEIEEKVDQYISLLEKMKTKLSSF-HFNIDIKKYKNPK--IKEEI 1079
|
250
....*....|....*
gi 528517572 1770 DGLEDKMKAILNAIN 1784
Cdd:PTZ00440 1080 KLLEEKVEALLKKID 1094
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1485-1734 |
2.27e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1485 DRAQAA---LEKASDTKNKVDHSNNDLRDLIKQIrQFLMQegaDPDSIEAVANRVLELSipASPKQIRHLADEIKD---R 1558
Cdd:COG3096 893 DRLEELreeLDAAQEAQAFIQQHGKALAQLEPLV-AVLQS---DPEQFEQLQADYLQAK--EQQRRLKQQIFALSEvvqR 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1559 VKSLSNVDA--ILEQTQNDVRKAEQLLLDAKKARNKAegvKNTAESVKKALNDASRAQAAAEKAIQkAKNDIgltqnqla 1636
Cdd:COG3096 967 RPHFSYEDAvgLLGENSDLNEKLRARLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSSRD-AKQQT-------- 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1637 qiqsetsaserdlndavdrLGDLERQIEALKTKrannslDAARAEETATMARDKANEAKEILDGELS--DKYRTVQ-GLM 1713
Cdd:COG3096 1035 -------------------LQELEQELEELGVQ------ADAEAEERARIRRDELHEELSQNRSRRSqlEKQLTRCeAEM 1089
|
250 260
....*....|....*....|.
gi 528517572 1714 DNKAKTMQDAKHKAEQLRDEA 1734
Cdd:COG3096 1090 DSLQKRLRKAERDYKQEREQV 1110
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
290-317 |
4.09e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 4.09e-03
10 20
....*....|....*....|....*...
gi 528517572 290 VHGRCVCKHNTKGLNCEQCDDFYNDLPW 317
Cdd:smart00180 16 DTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1552-1644 |
4.25e-03 |
|
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: 39.34 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1552 ADEIKDrvkSLSNVDAILEQTQNDVRKAEQLLldaKKARNKAEGV----KNTAESVKKALNDasRAQAAAEKAIQKAKND 1627
Cdd:cd06503 32 EEKIAE---SLEEAEKAKEEAEELLAEYEEKL---AEARAEAQEIieeaRKEAEKIKEEILA--EAKEEAERILEQAKAE 103
|
90
....*....|....*...
gi 528517572 1628 IGLTQNQ-LAQIQSETSA 1644
Cdd:cd06503 104 IEQEKEKaLAELRKEVAD 121
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1465-1666 |
4.57e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.47 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1465 VVEELFKQVADAKTKAQEAKD----RAQAALEKASDTKNKVDHSNNDLRDLIKQIRQflmqegADPDSIEAVANRVLELS 1540
Cdd:cd21116 31 LLPSLNTHQALARAHALEWLNeikpKLLSLPNDIIGYNNTFQSYYPDLIELADNLIK------GDQGAKQQLLQGLEALQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1541 ipaspKQIRHLADEIKDRVKSL----SNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKNTAESVKKALNDASRAQAA 1616
Cdd:cd21116 105 -----SQVTKKQTSVTSFINELttfkNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528517572 1617 AEKAIQKAKNDIGLTQNQLAQIQSETsaserDLNDAVDRLGDLERQIEAL 1666
Cdd:cd21116 180 LDSDIKELITDLEDAESSIDAAFLQA-----DLKAAKADWNQLYEQAKSL 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1629-1783 |
4.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1629 GLTQNQLAQIQSETSASERDLNDAVDRLGDLERQieaLKTKRANnsldaaraeetATMARDKAneakEILDGELSDKYRT 1708
Cdd:PRK00409 498 GLPENIIEEAKKLIGEDKEKLNELIASLEELERE---LEQKAEE-----------AEALLKEA----EKLKEELEEKKEK 559
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528517572 1709 VQglmDNKAKTMQDAKHKAEQLRDEAKgllKDAQDKLQRLAELEKdyeenQKVLEGKARQldgLEDKMKAILNAI 1783
Cdd:PRK00409 560 LQ---EEEDKLLEEAEKEAQQAIKEAK---KEADEIIKELRQLQK-----GGYASVKAHE---LIEARKRLNKAN 620
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
911-979 |
4.82e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 4.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517572 911 CPCPEGPNSGrhfaASCYQdnrsQQVVCNCNQGYTGtvkrsagavlnrPRCDECAPGYFGDPSKPGGQC 979
Cdd:pfam00053 1 CDCNPHGSLS----DTCDP----ETGQCLCKPGVTG------------RHCDRCKPGYYGLPSDPPQGC 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1609-1774 |
5.31e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1609 DASRAQAAAEKAIQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLE---RQIEALKTKRANNSLDAARAEEtAT 1685
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQQEKIERYQEDLEELTERLEE-QE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1686 MARDKANEAKEILdgelsdkyrtvqglmdnkaktmQDAKHKAEQLRDEAKGLLKDAQ---DKLQRLAeleKDYEENQKVL 1762
Cdd:COG3096 368 EVVEEAAEQLAEA----------------------EARLEAAEEEVDSLKSQLADYQqalDVQQTRA---IQYQQAVQAL 422
|
170
....*....|..
gi 528517572 1763 EgKARQLDGLED 1774
Cdd:COG3096 423 E-KARALCGLPD 433
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1474-1788 |
5.58e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.22 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1474 ADAKTKAQEAKDRAQAALEKASDTKNKVDHSNNdLRDLIKQIRQFLMQEGadpDSIEAVANRVLElsipaspkqirhlad 1553
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAF-LRRGLSVQLANLEKVR---EGLEKVLNELKK--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1554 EIKDRVKSLSNVDAILEQTQNDVRK---AEQLLLDAKKARN-----KAEGVKNTAESVKKALNDASRAQAAAEKAIQKAK 1625
Cdd:pfam04108 64 DFKQLLKDLDAALERLEETLDKLRNtpvEPALPPGEEKQKTlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRFD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1626 NDIGLTQNQLAQIQSETSAS----------ERDLNDAVDRLGDLERQIEalKTKRANNSLDAARAEETATMARDkANEAK 1695
Cdd:pfam04108 144 DDLRDLQKELESLSSPSESIsliptllkelESLEEEMASLLESLTNHYD--QCVTAVKLTEGGRAEMLEVLEND-ARELD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1696 EILD------GELSDKYRTVQGLMDNKAKTMQDAKHKAEQLRDeakglLKDAQDK-LQRLAELEKDYEENQKVLEGKARQ 1768
Cdd:pfam04108 221 DVVPelqdrlDEMENNYERLQKLLEQKNSLIDELLSALQLIAE-----IQSRLPEyLAALKEFEERWEEEKETIEDYLSE 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 528517572 1769 LDGL------------------------EDKMKAILNAINRQIQ 1788
Cdd:pfam04108 296 LEDLrefyegfpsaygsllleverrrewAEKMKKILRKLAEELD 339
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1639-1788 |
6.05e-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: 40.12 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1639 QSETSASERDLNDAVDRLGDLERQIEALKTKRanNSLDAArAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKAK 1718
Cdd:cd00176 25 STDYGDDLESVEALLKKHEALEAELAAHEERV--EALNEL-GEQLIEEGHPDAEEIQERLE-ELNQRWEELRELAEERRQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1719 TMQDAKHKAEQLRD---------EAKGLLKD---------AQDKLQRLAELEKDYEENQ---KVLEGKARQLdgLEDKMK 1777
Cdd:cd00176 101 RLEEALDLQQFFRDaddleqwleEKEAALASedlgkdlesVEELLKKHKELEEELEAHEprlKSLNELAEEL--LEEGHP 178
|
170
....*....|.
gi 528517572 1778 AILNAINRQIQ 1788
Cdd:cd00176 179 DADEEIEEKLE 189
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1573-1695 |
6.53e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1573 QNDVRKAEQLLLDAKKARnKAEGVKNTAESVKKALNDASRAQAAAEKAIQKAKND----------------IGLTQNQLA 1636
Cdd:PRK05035 516 NSAVIAAREARKAQARAR-QAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAeaeeevdpkkaavaaaIARAKAKKA 594
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528517572 1637 QIQSETSASERDLNDAVDRLGDLERQIEALKTKRA--------NNSLDAARAEETATMARDKANEAK 1695
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAeqqanaepEEPVDPRKAAVAAAIARAKARKAA 661
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1448-1571 |
7.17e-03 |
|
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: 39.00 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1448 ALDRSKHAEKELDKAmgvVEELFKQVADAKTKAQ----EAKDRAQAALEKA-SDTKNKVDHSNNDLRDLIKQIRQflmqe 1522
Cdd:COG0711 39 GLAEAERAKEEAEAA---LAEYEEKLAEARAEAAeiiaEARKEAEAIAEEAkAEAEAEAERIIAQAEAEIEQERA----- 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 528517572 1523 gadpDSIEAVANRVLELSIPASPKQIRHLADEikDRVKSLsnVDAILEQ 1571
Cdd:COG0711 111 ----KALAELRAEVADLAVAIAEKILGKELDA--AAQAAL--VDRFIAE 151
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1472-1674 |
7.41e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 40.21 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1472 QVADAKtKAQEAKDRAQAALEKASDT-------KNKVDHSNNDLRDLIK-QIRQfLMQEGADPDSIEavanrVLELSIpa 1543
Cdd:COG0330 90 RITDPA-KFLYNVENAEEALRQLAESalrevigKMTLDEVLSTGRDEINaEIRE-ELQEALDPYGIE-----VVDVEI-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1544 spKQIRhLADEIKDRVkslsnvdaileqtqNDVRKAEQlllDAKKARNKAEGVKNTAEsvkkalndaSRAQAAAEKAIQK 1623
Cdd:COG0330 161 --KDID-PPEEVQDAM--------------EDRMKAER---EREAAILEAEGYREAAI---------IRAEGEAQRAIIE 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528517572 1624 AKndiGLTQNQLAQIQSETSASERdLNDAVDRLGDL--ERQIEALKTKRANNS 1674
Cdd:COG0330 212 AE---AYREAQILRAEGEAEAFRI-VAEAYSAAPFVlfYRSLEALEEVLSPNS 260
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1709-1788 |
7.55e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.05 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1709 VQGLMDNkaktMQDAKHKAEQLRDEAKGLLKDAQDKLQRLAELEKDYEENQKVL-----EGKARQLDGLEDKMKAILNAI 1783
Cdd:COG2825 31 VQRILQE----SPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLseeerQKKERELQKKQQELQRKQQEA 106
|
....*
gi 528517572 1784 NRQIQ 1788
Cdd:COG2825 107 QQDLQ 111
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1621-1764 |
7.77e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1621 IQKAKNDIGLTQNQLAQIQSETSASERDLNDAVDRLGDLERQIEALKT--KRANNSLDAARAEETATmARDKANEAKEIL 1698
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEelEEKKEKLQEEEDKLLEE-AEKEAQQAIKEA 582
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1699 DGELSDKYRTVQGLMDnkaktMQDAKHKAEQLrDEAKGLLKDAQDKLQrlAELEKDYEENQKVLEG 1764
Cdd:PRK00409 583 KKEADEIIKELRQLQK-----GGYASVKAHEL-IEARKRLNKANEKKE--KKKKKQKEKQEELKVG 640
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
1673-1788 |
8.74e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 39.98 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1673 NSLDAARAEeTATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQDAKHKaeqlrdeakgLLKDAQDKLQRLAELE 1752
Cdd:cd07651 60 NSLDTLRLE-TESMAKSHLKFAKQIRQ-DLEEKLAAFASSYTQKRKKIQSHMEK----------LLKKKQDQEKYLEKAR 127
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 528517572 1753 KDYEENQKVLEGKARQ---LDGLE-DKMKAILNAINRQIQ 1788
Cdd:cd07651 128 EKYEADCSKINSYTLQsqlTWGKElEKNNAKLNKAQSSIN 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1651-1785 |
9.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517572 1651 DAVDRLGDLERQIEALKTKRAnnsldaaraeeTATMARDKANEAKEILDgELSDKYRTVQGLMDNKAKTMQdAKHKAEQL 1730
Cdd:COG4913 607 DNRAKLAALEAELAELEEELA-----------EAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVAS-AEREIAEL 673
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517572 1731 RDEAKGLLKDAQD--KL-QRLAELEKDYEENQKVLEGKARQLDGLEDKMKAILNAINR 1785
Cdd:COG4913 674 EAELERLDASSDDlaALeEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1569-1624 |
9.90e-03 |
|
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: 36.59 E-value: 9.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517572 1569 LEQTQNdvrKAEQLLLDAKKARNKAEGVKNTAEsvkKALNDASRAQAAAEKAIQKA 1624
Cdd:pfam11839 3 VEELQS---KADQAEQDAAAAQSAADSAKAKAD---EAAARANAAEAAAEEAQQAA 52
|
|
| |
