|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.79e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5001398 194 FSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKDPKVLQSYYYAVSDFSVGG 269
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
4.47e-93 |
|
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: 300.82 E-value: 4.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 5001398 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.35e-34 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 128.16 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 540 LTAPGKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaraSQGGRAQVPLQETS-- 613
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP---GQEQTYSVRLHEENwr 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 614 EDVAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 79 DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1527 |
4.95e-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: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1071 GAREAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1151 KWSHLAIEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1291 RTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAAL------TQASSSVQAATVTVMGARTLLADLEGMKLQFPRP 1364
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpldkirARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEvlAKDSAKLAKALLRERKQAHRRASRLTSQ 1444
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR--RELLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1445 TQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSE-LLARLGSLDTHQAPAQALNETQWA 1523
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEeALEELPEPPDLEELERELERLERE 775
|
....
gi 5001398 1524 LERL 1527
Cdd:COG1196 776 IEAL 779
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.23e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.23e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKGC 962
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-965 |
5.05e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 5.05e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKGCRAC 965
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-961 |
1.77e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.77e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 916 SCKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKG 961
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
430-477 |
3.74e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 430 CTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPHNPAGC 477
Cdd:pfam00053 1 CDCNPHGSLsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
706-753 |
1.02e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 5001398 706 PCTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfaGQADDCQ 753
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLP--SQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
865-915 |
1.53e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 1.53e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 5001398 865 PCSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQP-GRGCR 915
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
866-914 |
3.24e-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: 59.67 E-value: 3.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 5001398 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1532 |
3.57e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1276 EKtvaswQHMATEAARTLQTAAQATLRQTE-PLTMARSRL----TA-----TFASQLHQgARAALTQASSSVQAATVTvm 1345
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAEeEVDELKSQLadyqQAldvqqTRAIQYQQ-AVQALERAKQLCGLPDLT-- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1346 gartlLADLEGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAE 1414
Cdd:PRK04863 437 -----ADNAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1415 VLAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRE 1485
Cdd:PRK04863 503 RRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 5001398 1486 SRISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1532
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| LamB |
smart00281 |
Laminin B domain; |
542-661 |
4.09e-11 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 61.89 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 542 APGKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgPQDARASQGGRAQVPLQETSEDVAP 618
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA-----EGPPLPDELTTVEVRFREENWQYYG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 5001398 619 --PLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARP 661
Cdd:smart00281 84 grPVTREDLMMVLANLTAILIRATYSQQMAG-SRLSDVSLEVAVP 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.47e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 5.47e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1528 |
2.37e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.62 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTlqTAAQATlrqtepltmarsrltatfASQLHQGARAA---LTQASSSVQ 1338
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKART--VAAEDT------------------AAQLAKAARTAeevLTKASEDAK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1339 AATvtvmgaRTLLADLEgmklqfprpkdqaALQRKADSVSDRLLA---------------DT---RKKT----KQAERML 1396
Cdd:NF041483 386 ATT------RAAAEEAE-------------RIRREAEAEADRLRGeaadqaeqlkgaakdDTkeyRAKTvelqEEARRLR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1397 GNAAPLSSSAKKKG--------REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATL 1449
Cdd:NF041483 447 GEAEQLRAEAVAEGerirgearREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1450 QQASqqvlaSEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWA 1523
Cdd:NF041483 527 ERTR-----AEAERLRAEAEEQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAE 601
|
....*
gi 5001398 1524 LERLR 1528
Cdd:NF041483 602 AERIR 606
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.58e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.58e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.24e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.24e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
4.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 5001398 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
5.77e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 5001398 430 CTCNPAGSLD-TCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPH 472
Cdd:smart00180 1 CDCDPGGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
382-428 |
4.78e-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: 4.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 382 PCDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSE--GGCR 428
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
810-857 |
8.56e-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: 52.74 E-value: 8.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-857 |
2.10e-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: 51.59 E-value: 2.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGC 427
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1531 |
2.74e-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: 59.03 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATL---RQTEpLTMARSRL---TATFASQLhQGARAALTQAsssVQAATVTV 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELrskREQE-VTELKKALeeeTRSHEAQL-QEMRQKHTQA---LEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1345 MGARTLLADLEGMKLQFPrpKDQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL 1423
Cdd:pfam01576 366 EQAKRNKANLEKAKQALE--SENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1424 --AKALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDI 1494
Cdd:pfam01576 443 esVSSLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQL 519
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 5001398 1495 ETLSELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1531
Cdd:pfam01576 520 STLQAQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
383-430 |
4.14e-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: 4.14e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-317 |
9.02e-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: 50.05 E-value: 9.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 270 RCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGT 317
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
6.60e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 964 ACRCSPLGAASAQCHY-NGTCVCRPGFEGYKCDRCHYNFF-LTADGTHCQ 1011
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.80e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 5001398 810 CQCsgNVDPNAVGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGS 853
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1579 |
1.26e-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: 53.52 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1083 LEGAVKAAREQLQRLNK-----GARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWSH 1154
Cdd:TIGR02168 300 LEQQKQILRERLANLERqleelEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEaELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1155 LAIEARALARSHRDTATKIAAT------------AWRALLASNTSyALLWNLLEGRVAlETQRDLEDRYQEVQAAQKALR 1222
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEierlearlerleDRRERLQQEIE-ELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1223 TAVAEvLPEAESVLATVQQVGADTAPYLALLASPGALPQK--SRAEDLGLKAKALEK----------------TVASWQH 1284
Cdd:TIGR02168 458 RLEEA-LEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKnqsglsgilgvlseliSVDEGYE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1285 MATEAArtLQTAAQATLrqTEPLTMARSrltatfasqlhqgARAALTQASSsvqaatvtvmGARTLLAdLEGMKLQFPRP 1364
Cdd:TIGR02168 537 AAIEAA--LGGRLQAVV--VENLNAAKK-------------AIAFLKQNEL----------GRVTFLP-LDSIKGTEIQG 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSdrLLADTRKKTKQAER----MLG---------NAAPLSSSAKKKGR----EAEVLAKD-----SAK 1422
Cdd:TIGR02168 589 NDREILKNIEGFLG--VAKDLVKFDPKLRKalsyLLGgvlvvddldNALELAKKLRPGYRivtlDGDLVRPGgvitgGSA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1423 LAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAER-VGAGLSEMEQQIRESRISL---EKDIETLS 1498
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLarlEAEVEQLE 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1499 ELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQrklslleqesqqQELQIQGFESDLAEIRADKQNLEAILHS 1578
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------------LEAQIEQLKEELKALREALDELRAELTL 814
|
.
gi 5001398 1579 L 1579
Cdd:TIGR02168 815 L 815
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
965-1002 |
1.70e-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: 1.70e-06
10 20 30
....*....|....*....|....*....|....*....
gi 5001398 965 CRCSPLGAASAQCH-YNGTCVCRPGFEGYKCDRCHYNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1263-1519 |
2.11e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.91 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTA----TFASQLHQGARAALTQASSSVQ 1338
Cdd:NF041483 480 RTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAerlrAEAEEQAEEVRAAAERAARELR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1339 AATVTVMGARTLLADLEGMKLQFPRPKDQAA--------------LQRKADSVSDRLLADT--RKKTKQ------AERML 1396
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAaeealadaraeaerIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLR 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1397 GNAAPLSSSAKKKGR------------EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEA 1461
Cdd:NF041483 640 TEAAADASAARAEGEnvavrlrseaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EA 708
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 1462 RRQELEEAERVGAGLSEMEQQIRESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1519
Cdd:NF041483 709 ARRRREAEETLGSARAEADQERERAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.13e-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: 44.65 E-value: 7.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 5001398 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1488 |
1.68e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.82 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRqteplTMARSRLTAt 1317
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAAR-----TRADAREDA- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1318 fasqlHQGARAALTQASSSVQAATVTvmgARTLLADLEGMKLQFPRPKDQAALQRKADSV--SDRLLADTrkkTKQAERM 1395
Cdd:NF041483 905 -----NRIRSDAAAQADRLIGEATSE---AERLTAEARAEAERLRDEARAEAERVRADAAaqAEQLIAEA---TGEAERL 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1396 LGNAAPLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVL 1457
Cdd:NF041483 974 RAEAAETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQL 1053
|
250 260 270
....*....|....*....|....*....|....*....
gi 5001398 1458 ASEARRQELE---EAER-----VGAGLSEMEQQIRESRI 1488
Cdd:NF041483 1054 TAKAQEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1016 |
3.96e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 5001398 965 CRCSPLGAASAQCH-YNGTCVCRPGFEGYKCDRChynffltADGTHCQQCPSC 1016
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRC-------APGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.70e-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: 42.34 E-value: 4.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 327 CNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHwDPRMPCQPC 383
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
754-802 |
1.65e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 1.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 754 PCPCPGQSACTTIPESGEVVCtHCPPGQRGRRCEVCDDGFFGDPLGLFG 802
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-377 |
4.32e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 4.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 5001398 326 PCNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHWDPR 377
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1411-1503 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1411 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1489
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 5001398 1490 LEKDIETLSELLAR 1503
Cdd:cd06503 115 LRKEVADLAVEAAE 128
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.62e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 5001398 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
755-807 |
3.94e-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: 36.95 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 5001398 755 CPCPGQSACTTIPESGEVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.04e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.04e-03
10 20
....*....|....*....|....*....
gi 5001398 348 HGGRCHhCRDHTAGPHCERCQENFYHWDP 376
Cdd:smart00180 16 DTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.79e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5001398 194 FSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKDPKVLQSYYYAVSDFSVGG 269
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
4.47e-93 |
|
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: 300.82 E-value: 4.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 5001398 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.35e-34 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 128.16 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 540 LTAPGKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaraSQGGRAQVPLQETS-- 613
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP---GQEQTYSVRLHEENwr 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 614 EDVAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 79 DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1527 |
4.95e-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: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1071 GAREAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1151 KWSHLAIEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1291 RTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAAL------TQASSSVQAATVTVMGARTLLADLEGMKLQFPRP 1364
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpldkirARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEvlAKDSAKLAKALLRERKQAHRRASRLTSQ 1444
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR--RELLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1445 TQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSE-LLARLGSLDTHQAPAQALNETQWA 1523
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEeALEELPEPPDLEELERELERLERE 775
|
....
gi 5001398 1524 LERL 1527
Cdd:COG1196 776 IEAL 779
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.23e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.23e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKGC 962
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-965 |
5.05e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 5.05e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKGCRAC 965
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-961 |
1.77e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.77e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 916 SCKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGSSIKG 961
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1075-1579 |
2.34e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1075 AFLEQMmgLEGAVKAAREQLQRLNKgarcaqagsQKTCTQLADLEAVlessEEEIlhaaailasleipQEGPSQPTKWSH 1154
Cdd:COG4717 41 AFIRAM--LLERLEKEADELFKPQG---------RKPELNLKELKEL----EEEL-------------KEAEEKEEEYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1155 LAIEARALARSHRDTATKIAAtaWRALLASNTSYALLWNLLEGRVALETQ-RDLEDRYQEVQAAQKALRTAVAEvLPEAE 1233
Cdd:COG4717 93 LQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEE-LEELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1234 SVLATVQQVgADTAPYLALLASPGALPQ-KSRAEDLGLKAKALEKTVASWQhmatEAARTLQTAAQATLRQTEPLTMARs 1312
Cdd:COG4717 170 AELAELQEE-LEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQ----EELEELEEELEQLENELEAAALEE- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1313 RLTATFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRpKDQAALQRKADSVsdrLLADTRKKTKQA 1392
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA-REKASLGKEAEEL---QALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1393 ErmlgnaapLSSSAKKKGREAEvLAKDSAKLAKALLRERKQAHRRASRLTSQ-TQATLQQASQQVLAS---------EAR 1462
Cdd:COG4717 320 E--------LEELLAALGLPPD-LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEagvedeeelRAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1463 RQELEEAERVGAGLSEMEQQIRESRISLEKDIETLS--ELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQRK 1540
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELE------EELEELEEELEELREELAE---LEAE 461
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 5001398 1541 lslleqesqqqelqIQGFESD--LAEIRADKQNLEAILHSL 1579
Cdd:COG4717 462 --------------LEQLEEDgeLAELLQELEELKAELREL 488
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
430-477 |
3.74e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 430 CTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPHNPAGC 477
Cdd:pfam00053 1 CDCNPHGSLsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
706-753 |
1.02e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 5001398 706 PCTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfaGQADDCQ 753
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLP--SQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
865-915 |
1.53e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 1.53e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 5001398 865 PCSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQP-GRGCR 915
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
866-914 |
3.24e-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: 59.67 E-value: 3.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 5001398 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1532 |
3.57e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1276 EKtvaswQHMATEAARTLQTAAQATLRQTE-PLTMARSRL----TA-----TFASQLHQgARAALTQASSSVQAATVTvm 1345
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAEeEVDELKSQLadyqQAldvqqTRAIQYQQ-AVQALERAKQLCGLPDLT-- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1346 gartlLADLEGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAE 1414
Cdd:PRK04863 437 -----ADNAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1415 VLAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRE 1485
Cdd:PRK04863 503 RRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 5001398 1486 SRISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1532
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| LamB |
smart00281 |
Laminin B domain; |
542-661 |
4.09e-11 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 61.89 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 542 APGKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgPQDARASQGGRAQVPLQETSEDVAP 618
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA-----EGPPLPDELTTVEVRFREENWQYYG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 5001398 619 --PLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARP 661
Cdd:smart00281 84 grPVTREDLMMVLANLTAILIRATYSQQMAG-SRLSDVSLEVAVP 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.47e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 5.47e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1528 |
2.37e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.62 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTlqTAAQATlrqtepltmarsrltatfASQLHQGARAA---LTQASSSVQ 1338
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKART--VAAEDT------------------AAQLAKAARTAeevLTKASEDAK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1339 AATvtvmgaRTLLADLEgmklqfprpkdqaALQRKADSVSDRLLA---------------DT---RKKT----KQAERML 1396
Cdd:NF041483 386 ATT------RAAAEEAE-------------RIRREAEAEADRLRGeaadqaeqlkgaakdDTkeyRAKTvelqEEARRLR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1397 GNAAPLSSSAKKKG--------REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATL 1449
Cdd:NF041483 447 GEAEQLRAEAVAEGerirgearREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1450 QQASqqvlaSEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWA 1523
Cdd:NF041483 527 ERTR-----AEAERLRAEAEEQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAE 601
|
....*
gi 5001398 1524 LERLR 1528
Cdd:NF041483 602 AERIR 606
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.58e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.58e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1198-1534 |
3.13e-10 |
|
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: 65.36 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1198 RVALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQVGADtapYLALLASPGALPQK--SRAEDLGLKAK 1273
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELeeLSARESDLEQDYQAASD---HLNLVQTALRQQEKieRYQEDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1274 ALEKtvaswQHMATEAARTLQTAAQATLRQTE-PLTMARSRLT---------ATFASQLHQgARAALTQASSSVQAATVT 1343
Cdd:COG3096 362 RLEE-----QEEVVEEAAEQLAEAEARLEAAEeEVDSLKSQLAdyqqaldvqQTRAIQYQQ-AVQALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1344 VMGARTLladlegmklqfprpkdQAALQRKADSVSDRLLadtrkktkQAERMLGnaapLSSSAKKKGREA---------E 1414
Cdd:COG3096 436 PENAEDY----------------LAAFRAKEQQATEEVL--------ELEQKLS----VADAARRQFEKAyelvckiagE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1415 VLAKDSAKLAKALLRE----RKQAHRRAS----------RLTSQTQAT------LQQASQQVLASEARRQELEEAERVGA 1474
Cdd:COG3096 488 VERSQAWQTARELLRRyrsqQALAQRLQQlraqlaeleqRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEAQLE 567
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1475 GLSEMEQQIRESRISLEKdieTLSELLARLGSLdTHQAPaqALNETQWALERLRLQLGSP 1534
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQ---QLEQLRARIKEL-AARAP--AWLAAQDALERLREQSGEA 621
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.24e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.24e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
4.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 5001398 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
5.77e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 5001398 430 CTCNPAGSLD-TCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPH 472
Cdd:smart00180 1 CDCDPGGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1072-1533 |
1.45e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 62.62 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1072 AREAFLEQMMGLEGAVKAAREQLQRLnkgARCAQAGSQKtctqLADLEAVLESSEEEILHAAAILASleipqegpSQPTK 1151
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARL---DELEALIDQW----LAELEQVIALRRAGGLEAALALVR--------SGEGK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1152 WSHLAIEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPE 1231
Cdd:COG5278 149 ALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1232 AESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASwQHMATEAARTLQTAAQATLRQTEPLTMAR 1311
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALA-AAAALAAAAALELAAAEALALAELELELL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1312 SRLTATFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEgmklqfpRPKDQAALQRKADSVSDRLLADTRKKTKQ 1391
Cdd:COG5278 308 LAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALL-------AEAAAAAAEEAEAAAEAAAAALAGLAEVE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1392 AERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAER 1471
Cdd:COG5278 381 AEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5001398 1472 VGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGS 1533
Cdd:COG5278 461 AEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1195-1525 |
3.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1195 LEGRVA-LETQRDLEDRYQEVQAAQKALrtavaevlpEAESVLATVQQVGADtapyLALLaspgalpqKSRAEDLGLKAK 1273
Cdd:COG1196 198 LERQLEpLERQAEKAERYRELKEELKEL---------EAELLLLKLRELEAE----LEEL--------EAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1274 ALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTAT-----FASQLHQGARAALTQASSSVQAATVTVMGAR 1348
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1349 TLLADLEgmklqfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALL 1428
Cdd:COG1196 337 EELEELE---------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1429 RERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLD 1508
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330
....*....|....*..
gi 5001398 1509 THQAPAQALNETQWALE 1525
Cdd:COG1196 488 EAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1531 |
4.47e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1071 GAREAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqpt 1150
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1151 kwSHLAIEARALARSHRDTATKIAA--TAWRALLAS-NTSYALLWNLLEgrvALETQRDLEDRYQEVQAAQKALRTAVAE 1227
Cdd:COG1196 358 --AELAEAEEALLEAEAELAEAEEEleELAEELLEAlRAAAELAAQLEE---LEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1228 VLPEAESVLATVQQVGADTAPYLALLASpgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQAtLRQTEPL 1307
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEA-----LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGF 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1308 TMARSRLTATFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEgmklqfprpKDQAALQRKADSVSDRL------ 1381
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE---------DDEVAAAAIEYLKAAKAgratfl 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1382 ----LADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVL 1457
Cdd:COG1196 578 pldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1458 A----SEARRQELEEAERV-GAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNET-QWALERLRLQL 1531
Cdd:COG1196 658 AggslTGGSRRELLAALLEaEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAlEEQLEAEREEL 737
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
382-428 |
4.78e-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: 4.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 382 PCDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSE--GGCR 428
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
810-857 |
8.56e-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: 52.74 E-value: 8.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-857 |
2.10e-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: 51.59 E-value: 2.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 5001398 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGC 427
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1531 |
2.74e-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: 59.03 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATL---RQTEpLTMARSRL---TATFASQLhQGARAALTQAsssVQAATVTV 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELrskREQE-VTELKKALeeeTRSHEAQL-QEMRQKHTQA---LEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1345 MGARTLLADLEGMKLQFPrpKDQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL 1423
Cdd:pfam01576 366 EQAKRNKANLEKAKQALE--SENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1424 --AKALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDI 1494
Cdd:pfam01576 443 esVSSLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQL 519
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 5001398 1495 ETLSELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1531
Cdd:pfam01576 520 STLQAQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
383-430 |
4.14e-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: 4.14e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-317 |
9.02e-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: 50.05 E-value: 9.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 5001398 270 RCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGT 317
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1070-1539 |
2.13e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 56.02 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1070 PGAREAFLEQMMGLEGAVKAAREQLQRLNKGARCAQagsqktctQLADLEAVLESSEEeiLHAAAILASLEIPQEG--PS 1147
Cdd:COG3899 721 YAEALRYLERALELLPPDPEEEYRLALLLELAEALY--------LAGRFEEAEALLER--ALAARALAALAALRHGnpPA 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1148 QPTKWSHLAI-------EARALARSHRDTATKIAATAWRALLASNTSYALLWnLLEGRVALETQRDLEDRYQEVQAAQKA 1220
Cdd:COG3899 791 SARAYANLGLlllgdyeEAYEFGELALALAERLGDRRLEARALFNLGFILHW-LGPLREALELLREALEAGLETGDAALA 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1221 LRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQAT 1300
Cdd:COG3899 870 LLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1301 LRQTEPLTMARSRLTATFASQLHQGARAALTQAsssvqAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDR 1380
Cdd:COG3899 950 AAAALAAALALAAAAAAAAAAALAAAAAAAAAA-----AAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAAL 1024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1381 LLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASE 1460
Cdd:COG3899 1025 AALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 1461 ARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1539
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALL 1183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1078-1528 |
2.89e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1078 EQMMGLEGAVKAAREQLQRLNKGARCAQAgsqktctQLADLEAVLESSEE---EILHAAAILASLEipqegpsqptkwsh 1154
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARE-------TRDEADEVLEEHEErreELETLEAEIEDLR-------------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1155 laiEARALARSHRDTATKIAATAWRAL--LASNTSYALLWNLLEG--RVALETQRD-LEDRYQEVQAAQKALRTAVAEVL 1229
Cdd:PRK02224 265 ---ETIAETEREREELAEEVRDLRERLeeLEEERDDLLAEAGLDDadAEAVEARREeLEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1230 PEAESVLATVQQVgadtapylallaspgalpqKSRAEDLGLKAKALEKTVAswqhmATEAARTLQTAAQATLRqtEPLTM 1309
Cdd:PRK02224 342 EEAESLREDADDL-------------------EERAEELREEAAELESELE-----EAREAVEDRREEIEELE--EEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1310 ARSRLT---------ATFASQL---HQGARAALTQASSSVQAATVTVMGARTLLAdlEGmklqfprpKDQAALQRKADSV 1377
Cdd:PRK02224 396 LRERFGdapvdlgnaEDFLEELreeRDELREREAELEATLRTARERVEEAEALLE--AG--------KCPECGQPVEGSP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1378 SDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKalLRERKQAhrrASRLTSQTQATLQQASQQVL 1457
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER--LEERRED---LEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5001398 1458 ASEARRQELE-EAERVGAGLSEMEQQIRESRI---SLEKDIETLSELLARLGSLDTHQAPAQALNEtqwALERLR 1528
Cdd:PRK02224 541 ELRERAAELEaEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERIRTLLAAIADAED---EIERLR 612
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
6.60e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 5001398 964 ACRCSPLGAASAQCHY-NGTCVCRPGFEGYKCDRCHYNFF-LTADGTHCQ 1011
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.80e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 5001398 810 CQCsgNVDPNAVGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGS 853
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1073-1504 |
1.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1073 REAFLEQMMGLEGAVKAAREQLQRLNKgarcAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKW 1152
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1153 SHLAIEARALARSHRDTATKIAATAWRALLASNTSYALlwNLLEGRVALETQRDLED---RYQEVQAAQKALRTAVAEV- 1228
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEAq 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1229 --LPEAESVLATVQQVGADTAPY---------------LALLASPGALPQKSRAEDLGLKAKALekTVASWQHMATEAAR 1291
Cdd:COG4717 220 eeLEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLVL--GLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1292 TLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQASSSVQAATvtvmGARTLLADLEGMKLQF---PRPKDQA 1368
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE----ELQELLREAEELEEELqleELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1369 ALQRKADSVSD----------RLLADTRKKTKQAERMLGNAAPlsssakkkGREAEVLAKDSAKLAKALLRERKQAHRRA 1438
Cdd:COG4717 374 ALLAEAGVEDEeelraaleqaEEYQELKEELEELEEQLEELLG--------ELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5001398 1439 SRLT--SQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLekdiETLSELLARL 1504
Cdd:COG4717 446 EELEelREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL----ELLEEAREEY 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1579 |
1.26e-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: 53.52 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1083 LEGAVKAAREQLQRLNK-----GARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWSH 1154
Cdd:TIGR02168 300 LEQQKQILRERLANLERqleelEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEaELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1155 LAIEARALARSHRDTATKIAAT------------AWRALLASNTSyALLWNLLEGRVAlETQRDLEDRYQEVQAAQKALR 1222
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEierlearlerleDRRERLQQEIE-ELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1223 TAVAEvLPEAESVLATVQQVGADTAPYLALLASPGALPQK--SRAEDLGLKAKALEK----------------TVASWQH 1284
Cdd:TIGR02168 458 RLEEA-LEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKnqsglsgilgvlseliSVDEGYE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1285 MATEAArtLQTAAQATLrqTEPLTMARSrltatfasqlhqgARAALTQASSsvqaatvtvmGARTLLAdLEGMKLQFPRP 1364
Cdd:TIGR02168 537 AAIEAA--LGGRLQAVV--VENLNAAKK-------------AIAFLKQNEL----------GRVTFLP-LDSIKGTEIQG 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSdrLLADTRKKTKQAER----MLG---------NAAPLSSSAKKKGR----EAEVLAKD-----SAK 1422
Cdd:TIGR02168 589 NDREILKNIEGFLG--VAKDLVKFDPKLRKalsyLLGgvlvvddldNALELAKKLRPGYRivtlDGDLVRPGgvitgGSA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1423 LAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAER-VGAGLSEMEQQIRESRISL---EKDIETLS 1498
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLarlEAEVEQLE 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1499 ELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQrklslleqesqqQELQIQGFESDLAEIRADKQNLEAILHS 1578
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------------LEAQIEQLKEELKALREALDELRAELTL 814
|
.
gi 5001398 1579 L 1579
Cdd:TIGR02168 815 L 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1497 |
1.26e-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: 53.52 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1199 VALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADtapyLALLASPGALPQKSRAEDLGLKAKALEKT 1278
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1279 VASWQHMATEAARTLQTAAQATLrQTEPLTMARSRLTAT--FASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEG 1356
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1357 MKLQfprpkdQAALQRKADSVSDRLLADTRKKTKQAERMlgnaaplsSSAKKkgrEAEVLAKDSAKLAKALLRERKQAHR 1436
Cdd:TIGR02168 857 LAAE------IEELEELIEELESELEALLNERASLEEAL--------ALLRS---ELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5001398 1437 RASRLtSQTQATLQQASQQVL-----ASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETL 1497
Cdd:TIGR02168 920 LREKL-AQLELRLEGLEVRIDnlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
965-1002 |
1.70e-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: 1.70e-06
10 20 30
....*....|....*....|....*....|....*....
gi 5001398 965 CRCSPLGAASAQCH-YNGTCVCRPGFEGYKCDRCHYNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1286-1524 |
1.80e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1286 ATEAARTLQTAAQATLRQTEPLTMARSRLTATF-ASQLHQgARAALTQASSSVQAatvtvMGARTLLADLEGmklqfprp 1364
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEFlEEQLPE-LRKELEEAEAALEE-----FRQKNGLVDLSE-------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSDRL-----LADTRKKTKQAERMLGNAAPLSSSAKKKGREAEV---LAKDSAKLAKAL--------- 1427
Cdd:COG3206 213 EAKLLLQQLSELESQLAearaeLAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraqLAELEAELAELSarytpnhpd 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1428 ---LRERKQAHRRasRLTSQTQATLQQASQQVLASEARRQEL----EEAERVGAGLSEMEQQIREsrisLEKDIETLSE- 1499
Cdd:COG3206 293 viaLRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLqaqlAQLEARLAELPELEAELRR----LEREVEVAREl 366
|
250 260
....*....|....*....|....*...
gi 5001398 1500 ---LLARLGSLDThqapAQALNETQWAL 1524
Cdd:COG3206 367 yesLLQRLEEARL----AEALTVGNVRV 390
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1263-1519 |
2.11e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.91 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTA----TFASQLHQGARAALTQASSSVQ 1338
Cdd:NF041483 480 RTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAerlrAEAEEQAEEVRAAAERAARELR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1339 AATVTVMGARTLLADLEGMKLQFPRPKDQAA--------------LQRKADSVSDRLLADT--RKKTKQ------AERML 1396
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAaeealadaraeaerIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLR 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1397 GNAAPLSSSAKKKGR------------EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEA 1461
Cdd:NF041483 640 TEAAADASAARAEGEnvavrlrseaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EA 708
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 1462 RRQELEEAERVGAGLSEMEQQIRESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1519
Cdd:NF041483 709 ARRRREAEETLGSARAEADQERERAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1074-1576 |
3.09e-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: 52.37 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1074 EAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEI---------LHAAAILASLEIPQE 1144
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1145 GPSQPTKWSHLAIEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALetQRDLEDRYQEVQAAQKA---- 1220
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLKNqsgl 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1221 ----------------LRTAVAEVLPE---------AESVLATVQ---QVGADTAPYLALLASPGALPQKSRAE------ 1266
Cdd:TIGR02168 519 sgilgvlselisvdegYEAAIEAALGGrlqavvvenLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREilknie 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1267 -------DLGLKAKALEKTVASW---QHMATeaarTLQTAAQ-----------ATL---------------RQTEPLTMA 1310
Cdd:TIGR02168 599 gflgvakDLVKFDPKLRKALSYLlggVLVVD----DLDNALElakklrpgyriVTLdgdlvrpggvitggsAKTNSSILE 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1311 RSR-------LTATFASQLHQgARAALTQASSSVQAATVTVMGARTLLADLE----GMKLQFPR-PKDQAALQRKADSVS 1378
Cdd:TIGR02168 675 RRReieeleeKIEELEEKIAE-LEKALAELRKELEELEEELEQLRKELEELSrqisALRKDLARlEAEVEQLEERIAQLS 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1379 DRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVL--AKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQV 1456
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1457 LASEARRQELEE-AERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDthqapaQALNETQWALERLRLQLGSpg 1535
Cdd:TIGR02168 834 AATERRLEDLEEqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE------EALALLRSELEELSEELRE-- 905
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 5001398 1536 sLQRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAIL 1576
Cdd:TIGR02168 906 -LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1078-1344 |
6.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1078 EQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLeipqegpsqptkwshlai 1157
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1158 eARALARSHRDTatkiaaTAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLA 1237
Cdd:COG3883 92 -ARALYRSGGSV------SYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1238 TVQQvgadtapylallaspgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTAT 1317
Cdd:COG3883 165 ELEA-------------------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250 260
....*....|....*....|....*..
gi 5001398 1318 FASQLHQGARAALTQASSSVQAATVTV 1344
Cdd:COG3883 226 AAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1114-1529 |
6.82e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1114 QLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlaiEARALARSHRDTATKIAATAWRALLASNTSYAllwn 1193
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELE-----------------AELEELRLELEELELELEEAQAEEYELLAELA---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1194 LLEGRVALETQR--DLEDRYQEVQAAQKALRTAVAevlpEAESVLATVQQVGADTAPYLALLAspgALPQKSRAEDLGLK 1271
Cdd:COG1196 299 RLEQDIARLEERrrELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1272 AKALEKtVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLtatfasQLHQGARAALTQASSSVQAATVTVMGARTLL 1351
Cdd:COG1196 372 AELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1352 ADLEgmklqfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRER 1431
Cdd:COG1196 445 EEAA---------EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1432 KQAHRRASRLTSQ------TQATLQQASQQVLASEARRQELEEAERVGAGLSEmEQQIRESRISLEKdIETLSELLARLG 1505
Cdd:COG1196 516 LAGLRGLAGAVAVligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA-AKAGRATFLPLDK-IRARAALAAALA 593
|
410 420
....*....|....*....|....
gi 5001398 1506 SLDTHQAPAQALNETQWALERLRL 1529
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYV 617
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1289-1581 |
6.87e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1289 AARTLQTAA------QATLRQTEPLTMARSRLTATFASQLHQgaRAALTQASSSVQAATVTVMGART-LLADLEgmklqF 1361
Cdd:PRK02224 232 ARETRDEADevleehEERREELETLEAEIEDLRETIAETERE--REELAEEVRDLRERLEELEEERDdLLAEAG-----L 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1362 PRPKDQAALQRKAD------SVSDRLL---ADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKAL----- 1427
Cdd:PRK02224 305 DDADAEAVEARREEledrdeELRDRLEecrVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrre 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1428 --------------------------------LRERKQAHRraSRLTSqTQATLQQASQQVlaSEARR-----------Q 1464
Cdd:PRK02224 385 eieeleeeieelrerfgdapvdlgnaedfleeLREERDELR--EREAE-LEATLRTARERV--EEAEAlleagkcpecgQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1465 ELEEAERVgAGLSEMEQQ----------IRESRISLEKDI---ETLSELLARLGSLDTHQAPAQAL--------NETQWA 1523
Cdd:PRK02224 460 PVEGSPHV-ETIEEDRERveeleaeledLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLEELiaerretiEEKRER 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5001398 1524 LERLRLQ---LGSPGSLQRKL-SLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPE 1581
Cdd:PRK02224 539 AEELRERaaeLEAEAEEKREAaAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA 600
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.13e-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: 44.65 E-value: 7.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 5001398 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1411-1585 |
1.11e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1411 REAEVLAKDSAKLAKALLrERKQAHRRASRLTSQtqatLQQASQQVlasEARRQELEEAERvgaGLSEMEQQIRESRISL 1490
Cdd:COG4372 21 KTGILIAALSEQLRKALF-ELDKLQEELEQLREE----LEQAREEL---EQLEEELEQARS---ELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1491 EKDIETLSELLARLGSLDTHQAPAQA-LNETQWALERLRLQLgspGSLQRKLSLLEQESQQQELQIQGFESDLAEIRADK 1569
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEeLEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170
....*....|....*.
gi 5001398 1570 QNLEAILHSLPENCAS 1585
Cdd:COG4372 167 AALEQELQALSEAEAE 182
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1488 |
1.68e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.82 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRqteplTMARSRLTAt 1317
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAAR-----TRADAREDA- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1318 fasqlHQGARAALTQASSSVQAATVTvmgARTLLADLEGMKLQFPRPKDQAALQRKADSV--SDRLLADTrkkTKQAERM 1395
Cdd:NF041483 905 -----NRIRSDAAAQADRLIGEATSE---AERLTAEARAEAERLRDEARAEAERVRADAAaqAEQLIAEA---TGEAERL 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1396 LGNAAPLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVL 1457
Cdd:NF041483 974 RAEAAETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQL 1053
|
250 260 270
....*....|....*....|....*....|....*....
gi 5001398 1458 ASEARRQELE---EAER-----VGAGLSEMEQQIRESRI 1488
Cdd:NF041483 1054 TAKAQEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1365-1531 |
1.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSDRL--------LADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHR 1436
Cdd:COG1196 206 ERQAEKAERYRELKEELkeleaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1437 RASRLtSQTQATLQQASQQVLASEARRQELEEAervgagLSEMEQQIRESRISLEKDIETLSELLARLGSLDT-HQAPAQ 1515
Cdd:COG1196 286 AQAEE-YELLAELARLEQDIARLEERRRELEER------LEELEEELAELEEELEELEEELEELEEELEEAEEeLEEAEA 358
|
170
....*....|....*.
gi 5001398 1516 ALNETQWALERLRLQL 1531
Cdd:COG1196 359 ELAEAEEALLEAEAEL 374
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1078-1504 |
1.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1078 EQMMGLEGAVKAAREQLQRLNkgARCAQAGSQktctQLADLE---AVLESSEEEILHAAAILASL--EIPQEGPSQPTKW 1152
Cdd:COG4913 309 AELERLEARLDALREELDELE--AQIRGNGGD----RLEQLEreiERLERELEERERRRARLEALlaALGLPLPASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1153 SHLAIEARALARSHRDTATKIAATAWRALLAsntsyalLWNLLEGRVALETQRD-LEDR---Y-QEVQAAQKALRTA--- 1224
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAA-------LRDLRRELRELEAEIAsLERRksnIpARLLALRDALAEAlgl 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1225 -------VAE---VLPE-------AESVLAT-----------------------------VQQVGADTAPYLALLASPGA 1258
Cdd:COG4913 456 deaelpfVGElieVRPEeerwrgaIERVLGGfaltllvppehyaaalrwvnrlhlrgrlvYERVRTGLPDPERPRLDPDS 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1259 LPQKsraedlgLKAKA------LEKTVAS-WQHMATEAARTLQTAAQA-----------TLRQTEPLTMARSRL------ 1314
Cdd:COG4913 536 LAGK-------LDFKPhpfrawLEAELGRrFDYVCVDSPEELRRHPRAitragqvkgngTRHEKDDRRRIRSRYvlgfdn 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1315 ---TATFASQLHQgARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRL--LADTRKKT 1389
Cdd:COG4913 609 rakLAALEAELAE-LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerLDASSDDL 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1390 KQAERMLgnaaplsSSAKKKGREAEvlakdsAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEa 1469
Cdd:COG4913 688 AALEEQL-------EELEAELEELE------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE- 753
|
490 500 510
....*....|....*....|....*....|....*
gi 5001398 1470 ERVGAGLSEMEQQIREsriSLEKDIETLSELLARL 1504
Cdd:COG4913 754 RFAAALGDAVERELRE---NLEERIDALRARLNRA 785
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1311-1536 |
2.01e-05 |
|
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: 49.26 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1311 RSRLTATFASQLHQGARAA--LTQASSSVQAAtvtVMGARTllaDLEGMKLQFPRPKDQA-ALQRKADSVSDRL------ 1381
Cdd:pfam05701 263 KAELAAYMESKLKEEADGEgnEKKTSTSIQAA---LASAKK---ELEEVKANIEKAKDEVnCLRVAAASLRSELekekae 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1382 LADTRkktkQAERMlgnaaplsSSAKKKGREAEvLAKDSAKLAKALLRErKQAHRRASRLTSQTQATLQQASQQVLASEA 1461
Cdd:pfam05701 337 LASLR----QREGM--------ASIAVSSLEAE-LNRTKSEIALVQAKE-KEAREKMVELPKQLQQAAQEAEEAKSLAQA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1462 RRQEL----EEAERVGAGLSEMEQQIRESRisleKDIE--TLSELLARlgsldthqAPAQALNETQWAlERLRLQLGSPG 1535
Cdd:pfam05701 403 AREELrkakEEAEQAKAAASTVESRLEAVL----KEIEaaKASEKLAL--------AAIKALQESESS-AESTNQEDSPR 469
|
.
gi 5001398 1536 S 1536
Cdd:pfam05701 470 G 470
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1016 |
3.96e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 5001398 965 CRCSPLGAASAQCH-YNGTCVCRPGFEGYKCDRChynffltADGTHCQQCPSC 1016
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRC-------APGYYGDGPPGC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1196-1471 |
4.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1196 EGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEA--ESVLATVQQVGADTAPYLALLASPGAlPQKSRAEDLGL--- 1270
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAA-EAKKKADEAKKaee 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1271 KAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQASSSVQAATVTVMGARTL 1350
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1351 LADLEGMKLQFPRPKDQAALQ----RKADSVSDRLL------ADTRKKT----KQAERMLGNAAPLSSSAKKKGREAEVL 1416
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEqlkkkeAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5001398 1417 AK---DSAKLAKALLRERKQAhRRASRLTSQTQATLQQASQQVLASEARRQELEEAER 1471
Cdd:PTZ00121 1681 KKaeeDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1194-1498 |
4.19e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1194 LLEGRVALETQRDLEDRYQEVQAAQKA-LRTAVAEVLpEAESVLATVQQvGADTAPYLALlASPGALPQKSRAEDL-GLK 1271
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEArAEAAEEEVD-ELKSQLADYQQ-ALDVQQTRAI-QYQQAVQALERAKQLcGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1272 AKALEKtVASWQHM-------ATEAARTLQT---AAQATLRQ-TEPLTMARSRLTATFASQLHQGARAALTQASSSVQAA 1340
Cdd:PRK04863 434 DLTADN-AEDWLEEfqakeqeATEELLSLEQklsVAQAAHSQfEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1341 tVTVMGARTLLADLEGmklqfpRPKDQAALQRkadsvsdrLLADTRKktkQAERMLGNAAPLSSSAKKKGREAEVL---A 1417
Cdd:PRK04863 513 -EQLQQLRMRLSELEQ------RLRQQQRAER--------LLAEFCK---RLGKNLDDEDELEQLQEELEARLESLsesV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1418 KDSAKLAKALLRERKQAHRRASRLTSQT------QATLQQASQQVLASEARRQELEE-----AERVGAgLSEMEQQIRES 1486
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARApawlaaQDALARLREQSGEEFEDSQDVTEymqqlLERERE-LTVERDELAAR 653
|
330
....*....|..
gi 5001398 1487 RISLEKDIETLS 1498
Cdd:PRK04863 654 KQALDEEIERLS 665
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.70e-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: 42.34 E-value: 4.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 327 CNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHwDPRMPCQPC 383
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1203-1431 |
6.25e-05 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 47.31 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1203 TQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSR-AEDLGLKAKALEKTVAS 1281
Cdd:COG0515 247 LAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAaAAAAAAAAAAAAAPAAA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1282 WQHMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEGMKLQF 1361
Cdd:COG0515 327 AAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1362 PRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRER 1431
Cdd:COG0515 407 AAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAA 476
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1404-1504 |
7.42e-05 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 44.22 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1404 SSAKKKGREAEvlakdsaKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLA---SEARRQeLEEAERvgaglsEME 1480
Cdd:PRK07353 46 AEAKERLAEAE-------KLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAeaqAEAQAS-KEKARR------EIE 111
|
90 100
....*....|....*....|....*
gi 5001398 1481 QQIRESRISLEKDIETLSEL-LARL 1504
Cdd:PRK07353 112 QQKQAALAQLEQQVDALSRQiLEKL 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1501 |
8.68e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1083 LEGAVKAAREQLQRLNKGARCAQagsqktctQLADLEAvlessEEEILHAAAILASLEipqegpSQPTKWSHLAIEARAL 1162
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAE--------RYKELKA-----ELRELELALLVLRLE------ELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1163 ARSHRDTATKIAAtawrallasntsYALLWNLLEGRValetqRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQV 1242
Cdd:TIGR02168 252 EEELEELTAELQE------------LEEKLEELRLEV-----SELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1243 GADTAPYLALLASpgalpQKSRAEDLGLKAKALEKTVASwqhmaTEAARTLQTAAQATLRQTEPltMARSRLTAtfASQL 1322
Cdd:TIGR02168 315 ERQLEELEAQLEE-----LESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELE--ELESRLEE--LEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1323 HQGARAALTQASSSVQAATVTVMGARTLLADLEGMKlqfprpkdqaalqrkadsvsDRLLADTRKKTKQAERMLGNAAPL 1402
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR--------------------ERLQQEIEELLKKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1403 SSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRltsQTQATLQQASQQVLASEARRQELEeaervgaGLSEMEQQ 1482
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALD---AAERELAQLQARLDSLERLQENLE-------GFSEGVKA 510
|
410
....*....|....*....
gi 5001398 1483 IRESRISLEKDIETLSELL 1501
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSELI 529
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1074-1519 |
9.68e-05 |
|
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: 47.25 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1074 EAFLEQMMglegAVKAAREQLQRLNKGARCAQAGSQKTCTQLAD---------------------LEAVLESSEEEILHA 1132
Cdd:COG3096 361 ERLEEQEE----VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqaldvqqtraiqyqqavqaLEKARALCGLPDLTP 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1133 AAILASLEIPQEGPSQPTKwSHLAIEAR-ALARSHR---DTA----TKIA-----ATAW---RALLASNTSYAllwNLLE 1196
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATE-EVLELEQKlSVADAARrqfEKAyelvCKIAgeverSQAWqtaRELLRRYRSQQ---ALAQ 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1197 GRVALETQ-RDLEDRYQEVQAAQKAL-------------RTAVAEVLPEAESVLATVQQVGADtapylallASPGALPQK 1262
Cdd:COG3096 513 RLQQLRAQlAELEQRLRQQQNAERLLeefcqrigqqldaAEELEELLAELEAQLEELEEQAAE--------AVEQRSELR 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAKALEKTVASWqHMATEAARTLQT--------------AAQATLRQTEPLTMARSRLTAT------FASQL 1322
Cdd:COG3096 585 QQLEQLRARIKELAARAPAW-LAAQDALERLREqsgealadsqevtaAMQQLLEREREATVERDELAARkqalesQIERL 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1323 HQGARAALTQASS-------------------------------SVQAATVT-VMGARTLLADLEGMklqfprPKDQAAL 1370
Cdd:COG3096 664 SQPGGAEDPRLLAlaerlggvllseiyddvtledapyfsalygpARHAIVVPdLSAVKEQLAGLEDC------PEDLYLI 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1371 QRKADSVSDRLL-------ADTRKKTKQAER--------MLGNAAPlSSSAKKKGREAEVLAKDSAKLAkALLRERKQAH 1435
Cdd:COG3096 738 EGDPDSFDDSVFdaeeledAVVVKLSDRQWRysrfpevpLFGRAAR-EKRLEELRAERDELAEQYAKAS-FDVQKLQRLH 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1436 RRASRLTSQTQATLQQASQQVLASEARRQeLEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLD--THQAP 1513
Cdd:COG3096 816 QAFSQFVGGHLAVAFAPDPEAELAALRQR-RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLAdeTLADR 894
|
....*.
gi 5001398 1514 AQALNE 1519
Cdd:COG3096 895 LEELRE 900
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1404-1502 |
1.08e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 44.38 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1404 SSAKKKGREAEVLAKDsaklAKALLrerKQAHRRASRLTSQTQAtlqQASQQVlaSEARRQELEEAER-VGAGLSEMEQQ 1482
Cdd:PRK05759 45 AAAERAKKELELAQAK----YEAQL---AEARAEAAEIIEQAKK---RAAQII--EEAKAEAEAEAARiKAQAQAEIEQE 112
|
90 100
....*....|....*....|
gi 5001398 1483 IRESRISLEKDIETLSELLA 1502
Cdd:PRK05759 113 RKRAREELRKQVADLAVAGA 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1073-1302 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1073 REAFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEI---LHAAAILASLEIPQE--GPS 1147
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRALYRLGRQPPLALllSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1148 QPTKWSHLAIEARALARSHRDTATKIAATawRALLASNtsyallwnllegRVALETQRD-LEDRYQEVQAAQKALRTAVA 1226
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAAL------------RAELEAERAeLEALLAELEEERAALEALKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5001398 1227 evlpEAESVLATVQQVGADtapylallaspgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLR 1302
Cdd:COG4942 196 ----ERQKLLARLEKELAE---------------LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1115-1539 |
1.48e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.78 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1115 LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWS----------------------HLAIeARALARSHRD-TA 1170
Cdd:COG3899 607 LELLAAVLGLSEAELAAALEELVAAGlLVPRGDAGGGRYRfrhdlvreaayaslppeerralHRRI-ARALEARGPEpLE 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1171 TKIAATAWRALLASNTSYALLWNLLEGRVALET-----------------QRDLEDRYQ--------------------- 1212
Cdd:COG3899 686 ERLFELAHHLNRAGERDRAARLLLRAARRALARgayaealryleralellPPDPEEEYRlalllelaealylagrfeeae 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1213 ---------EVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASpgALPQKSRAEDLGLKAKALEKTVASWQ 1283
Cdd:COG3899 766 alleralaaRALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL--ALAERLGDRRLEARALFNLGFILHWL 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1284 HMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPR 1363
Cdd:COG3899 844 GPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAA 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1364 PKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTS 1443
Cdd:COG3899 924 AAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLA 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1444 QTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWA 1523
Cdd:COG3899 1004 AAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAA 1083
|
490
....*....|....*.
gi 5001398 1524 LERLRLQLGSPGSLQR 1539
Cdd:COG3899 1084 AAAALAAALAAAALAA 1099
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
754-802 |
1.65e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 1.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 5001398 754 PCPCPGQSACTTIPESGEVVCtHCPPGQRGRRCEVCDDGFFGDPLGLFG 802
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1380-1534 |
2.49e-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: 44.71 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1380 RLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS 1459
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5001398 1460 EARRQELEEAERVGAGLSEMEQQIRESRIS-LEKDIETLSELLaRLGSLDTHQAPAQA-LNETQWALERLRLQLGSP 1534
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEI-RSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSP 167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1531 |
2.80e-04 |
|
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: 45.71 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1053 LLGEAPRGDVYQ-GHHLLPGARE--AFLEQMMGLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLA---DLEAVLESSE 1126
Cdd:COG3096 484 IAGEVERSQAWQtARELLRRYRSqqALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1127 EEILHAAAILASleipqegpsqptkwshlAIEARALARSHRD-TATKIA-----ATAWRAL------LASNTSYAL---- 1190
Cdd:COG3096 564 AQLEELEEQAAE-----------------AVEQRSELRQQLEqLRARIKelaarAPAWLAAqdalerLREQSGEALadsq 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1191 -----LWNLLEGRVALETQRDledryqEVQAAQKALRTAVAEVL----PEAESVLATVQQVGA------------DTAPY 1249
Cdd:COG3096 627 evtaaMQQLLEREREATVERD------ELAARKQALESQIERLSqpggAEDPRLLALAERLGGvllseiyddvtlEDAPY 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1250 LALLASPGA----LPQKSRA-----------EDLGL-------------KAKALEKTV---------------------- 1279
Cdd:COG3096 701 FSALYGPARhaivVPDLSAVkeqlagledcpEDLYLiegdpdsfddsvfDAEELEDAVvvklsdrqwrysrfpevplfgr 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1280 -ASWQHMAT------EAARTLQTAAqATLRQTEPLTMARSRLTATFASQLHQG----ARAALTQASSSVQAAtvtvmgar 1348
Cdd:COG3096 781 aAREKRLEElraerdELAEQYAKAS-FDVQKLQRLHQAFSQFVGGHLAVAFAPdpeaELAALRQRRSELERE-------- 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1349 tlLADLEGMKLQFPRPKDQA-----ALQRKADSVSdrLLADT--RKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKdsa 1421
Cdd:COG3096 852 --LAQHRAQEQQLRQQLDQLkeqlqLLNKLLPQAN--LLADEtlADRLEELREELDAAQEAQAFIQQHGKALAQLEP--- 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1422 kLAkALLRERKQAHRRASRLTSQTQATLQQASQQVLASE---ARRQEL--EEAERVGAGLSEM-----------EQQIRE 1485
Cdd:COG3096 925 -LV-AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevvQRRPHFsyEDAVGLLGENSDLneklrarleqaEEARRE 1002
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 5001398 1486 SRISLEKDIETLSELLARLGSLDT-HQAPAQALNETQWALERLRLQL 1531
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKSsRDAKQQTLQELEQELEELGVQA 1049
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1365-1527 |
3.09e-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: 45.14 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1365 KDQAALQRKADSVSDRLlADTRKKTKQAERMLGNaapLSSSAKKKGREAEVLAKDSAKLAKALLRERK------------ 1432
Cdd:COG4942 41 KELAALKKEEKALLKQL-AALERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1433 ----------------QAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIET 1496
Cdd:COG4942 117 grqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|..
gi 5001398 1497 LSELLARL-GSLDTHQAPAQALNETQWALERL 1527
Cdd:COG4942 197 RQKLLARLeKELAELAAELAELQQEAEELEAL 228
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1188-1465 |
3.33e-04 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 45.00 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1188 YAL---LWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVL------------ATVQQVGADTAPYLAL 1252
Cdd:COG0515 192 YSLgvtLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVlralakdpeeryQSAAELAAALRAVLRS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1253 LASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQ 1332
Cdd:COG0515 272 LAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAAL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1333 ASSSVQAATVTVMGARTLLADLEGmkLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGRE 1412
Cdd:COG0515 352 LAAAAALAAAAAAAAAAAAAAAAA--AAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 5001398 1413 AEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQE 1465
Cdd:COG0515 430 AAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALALA 482
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1224-1468 |
3.79e-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: 43.94 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1224 AVAEVLPEAESVLATVqqvgADTAPYLallaSPGALPQKSRAEDLGLKAKALEktvaswqHMATEAaRTLQTAAQATLRQ 1303
Cdd:pfam06008 6 SLTGALPAPYKINYNL----ENLTKQL----QEYLSPENAHKIQIEILEKELS-------SLAQET-EELQKKATQTLAK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1304 TEPL------TMARSRLTATFASQLHQGARAALTQASSSVQAATVTVMGA-RTLLADLEGMkLQFPRPKDQAALQRKADS 1376
Cdd:pfam06008 70 AQQVnaeserTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDlSRMLAEAQRM-LGEIRSRDFGTQLQNAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1377 V---SDRLLADTRK--KTKQAE-RMLGNAAplsssakkkgreAEVLAKDSAKL--AKALLRERKQAHRRASRLTSQTQAT 1448
Cdd:pfam06008 149 ElkaAQDLLSRIQTwfQSPQEEnKALANAL------------RDSLAEYEAKLsdLRELLREAAAKTRDANRLNLANQAN 216
|
250 260
....*....|....*....|
gi 5001398 1449 LQQASQQVLASEARRQELEE 1468
Cdd:pfam06008 217 LREFQRKKEEVSEQKNQLEE 236
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-377 |
4.32e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 4.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 5001398 326 PCNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHWDPR 377
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1204-1537 |
4.94e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1204 QRDLEDRYQEVQAAQK-----ALRTAVAEVLPEAEsVLATVQQVGADTAPYLAL--LASPGALPQKSRAEDLGLKAKAL- 1275
Cdd:COG3064 2 QEALEEKAAEAAAQERleqaeAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1276 --EKTVASWQ-HMATEAARTLQTAAQATLRQTEPLTmARSRLTAtfasqlhQGARAALTQASSSVQAATVTVMGARTLLA 1352
Cdd:COG3064 81 eaEKAAAEAEkKAAAEKAKAAKEAEAAAAAEKAAAA-AEKEKAE-------EAKRKAEEEAKRKAEEERKAAEAEAAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1353 DLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKkgREAEVLAKDSAKLAKALLRERK 1432
Cdd:COG3064 153 EAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA--AAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1433 QAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISL--EKDIETLSELLARLGSLDTH 1510
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLaaAAAGLVLDDSAALAAELLGA 310
|
330 340
....*....|....*....|....*..
gi 5001398 1511 QAPAQALNETQWALERLRLQLGSPGSL 1537
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASL 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1158-1587 |
9.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1158 EARALARSHRDTATKIAAtaWRALLASNTSYA--LLWNLLEGRvaletQRDLEDRYQEVQAAQKALRTAVAEVLPEAESV 1235
Cdd:COG4913 256 PIRELAERYAAARERLAE--LEYLRAALRLWFaqRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1236 LATVQQVGADtapylallaspgalpqksRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLT 1315
Cdd:COG4913 329 EAQIRGNGGD------------------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1316 A--TFASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQA--ALQRKADSVSDRL-----LADTR 1386
Cdd:COG4913 391 AllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdALAEALGLDEAELpfvgeLIEVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1387 KKTKQ----AERMLGNAApLS---------------SSAKKKGR-------------EAEVLAKDS--AKL--------- 1423
Cdd:COG4913 471 PEEERwrgaIERVLGGFA-LTllvppehyaaalrwvNRLHLRGRlvyervrtglpdpERPRLDPDSlaGKLdfkphpfra 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1424 -AKALLRERK-----------QAHRRA---SRLTSQTQATLQ------QASQQVLASEARRQ------ELEEAERVgagL 1476
Cdd:COG4913 550 wLEAELGRRFdyvcvdspeelRRHPRAitrAGQVKGNGTRHEkddrrrIRSRYVLGFDNRAKlaaleaELAELEEE---L 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1477 SEMEQQIREsrisLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERL-----RLQLGSPG---------SLQRKLS 1542
Cdd:COG4913 627 AEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELeaeleRLDASSDDlaaleeqleELEAELE 702
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 5001398 1543 LLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPENCASWQ 1587
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1307-1526 |
9.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1307 LTMARSRLTATFASQLHQGARAALTQASSSVQAATVTVmgaRTLLADLEGMKLQFPRPKDQ-AALQRKADSVSDRLlADT 1385
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAEL---DALQAELEELNEEYNELQAElEALQAEIDKLQAEI-AEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1386 RKKTKQAERMLGNAAplsSSAKKKGREA---EVLAkDSAKLAKALlrerkqahRRA---SRLTSQTQATLQQASQQVLAS 1459
Cdd:COG3883 78 EAEIEERREELGERA---RALYRSGGSVsylDVLL-GSESFSDFL--------DRLsalSKIADADADLLEELKADKAEL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5001398 1460 EARRQELEEAErvgAGLSEMEQQIRESRISLEKDIETLSELLARLGS-LDTHQAPAQALNETQWALER 1526
Cdd:COG3883 146 EAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQEALLAQLSAeEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1395-1574 |
1.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1395 MLGNAAPLSSSAKKKGREAEvLAKDSAKLaKALLRERKQAHRRASRLTSQtqatLQQASQQVLASEARRQELE-EAERVG 1473
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAE-LEQLQQEI-AELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEqELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1474 AGLSEMEQQIREsrisLEKDIETLSELLARlgsldthQAPAQALNETQWALERLrLQLGSPGSLQRKLSLLEQESQQQEL 1553
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAE-------LLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180
....*....|....*....|.
gi 5001398 1554 QIQGFESDLAEIRADKQNLEA 1574
Cdd:COG4942 151 QAEELRADLAELAALRAELEA 171
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1411-1495 |
1.61e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 40.37 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1411 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS---EARRQELEEAERVGAGLSEMEQQIRE-- 1485
Cdd:pfam00430 40 AEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAaeaEAERIIEQAAAEIEQEKDRALAELRQqv 119
|
90
....*....|...
gi 5001398 1486 ---SRISLEKDIE 1495
Cdd:pfam00430 120 valAVQIAEKLLE 132
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1216-1509 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1216 AAQKALRTAVAEV---LPEAESVLATVQQVGADTAPYLALLAspGALPQKS--RAEDLGLKAKALEKTVASwqhmATEAA 1290
Cdd:COG3096 836 AELAALRQRRSELereLAQHRAQEQQLRQQLDQLKEQLQLLN--KLLPQANllADETLADRLEELREELDA----AQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1291 RTLQtAAQATLRQTEPLTmarSRLTATFASqlHQGARAALTQASSSvqaatvtvmgartlladlegmklqfprpkdQAAL 1370
Cdd:COG3096 910 AFIQ-QHGKALAQLEPLV---AVLQSDPEQ--FEQLQADYLQAKEQ------------------------------QRRL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1371 QRKADSVSD---RLLADTRKKtkqAERMLGNAAPLSSSAKKKGREAEvlakdsaklakallrerkQAHRRASRLTSQTQA 1447
Cdd:COG3096 954 KQQIFALSEvvqRRPHFSYED---AVGLLGENSDLNEKLRARLEQAE------------------EARREAREQLRQAQA 1012
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5001398 1448 TLQQASqQVLAS-----EARRQELEEAERVGAGL-----SEMEQQIRESRISLEkdiETLSELLARLGSLDT 1509
Cdd:COG3096 1013 QYSQYN-QVLASlkssrDAKQQTLQELEQELEELgvqadAEAEERARIRRDELH---EELSQNRSRRSQLEK 1080
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1403-1530 |
1.85e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1403 SSSAKKKGREAEVLAKDSAKlaKALLRERKQAHRRASRLTSQT-----------------QATLQQASQQVLASEARRQE 1465
Cdd:pfam01576 128 TTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSNLaeeeekakslsklknkhEAMISDLEERLKKEEKGRQE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1466 LEEAERVGAG--------LSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQA--------LNETQWALERLRL 1529
Cdd:pfam01576 206 LEKAKRKLEGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaqISELQEDLESERA 285
|
.
gi 5001398 1530 Q 1530
Cdd:pfam01576 286 A 286
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1159-1539 |
2.21e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.70 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1159 ARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLAT 1238
Cdd:COG3903 569 ERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAA 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1239 VQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQAtlrqtepltMARSRLTATF 1318
Cdd:COG3903 649 AAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAA---------ALAAAAAAAA 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1319 ASQLHQGARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFprpkDQAALQRKADSVSDRLLADTRKKTKQAERMLGN 1398
Cdd:COG3903 720 AAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAA----LAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1399 AAPLSSSAkkkGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSE 1478
Cdd:COG3903 796 AAAAAAAA---AAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAA 872
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5001398 1479 MEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1539
Cdd:COG3903 873 AAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| TNFRSF6B |
cd10575 |
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ... |
684-777 |
2.80e-03 |
|
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.
Pssm-ID: 276901 [Multi-domain] Cd Length: 163 Bit Score: 40.08 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 684 CEsCAPGYKREMPqggpyascvpcTCNQHGTCDPNTGICVCSHHTEGPSCERCLPGFYgNPFAGQADDCQP-CPCPGQSA 762
Cdd:cd10575 80 CE-CKPGYYMEHG-----------FCLRHSSCPPGEGVIKLGTPYSDTQCEPCPPGFF-SASSSSTEPCQPhTNCTQGGL 146
|
90
....*....|....*..
gi 5001398 763 CTTIP--ESGEVVCTHC 777
Cdd:cd10575 147 ETNVPgnDYHDTLCTSC 163
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1411-1503 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1411 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1489
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 5001398 1490 LEKDIETLSELLAR 1503
Cdd:cd06503 115 LRKEVADLAVEAAE 128
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1413-1536 |
3.06e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1413 AEVLAKdsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQvLASEA--RRQELEEAervgagLSEMEQQIRESRISL 1490
Cdd:COG1842 47 AQVIAN-----QKRLERQLEELEAEAEKWEEKARLALEKGRED-LAREAleRKAELEAQ------AEALEAQLAQLEEQV 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 5001398 1491 EKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGS 1536
Cdd:COG1842 115 EKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.62e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 5001398 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
755-807 |
3.94e-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: 36.95 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 5001398 755 CPCPGQSACTTIPESGEVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.04e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.04e-03
10 20
....*....|....*....|....*....
gi 5001398 348 HGGRCHhCRDHTAGPHCERCQENFYHWDP 376
Cdd:smart00180 16 DTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
1427-1504 |
4.25e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 39.22 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1427 LLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEA--ERVGAGLSEMEQQIRESRIS-LEKDIETLSELLAR 1503
Cdd:TIGR02473 7 LLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQalEKVGAGTSALELSNYQRFIRqLDQRIQQQQQELAL 86
|
.
gi 5001398 1504 L 1504
Cdd:TIGR02473 87 L 87
|
|
| COG4371 |
COG4371 |
Uncharacterized membrane protein [Function unknown]; |
1281-1383 |
4.48e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 443499 Cd Length: 238 Bit Score: 40.69 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1281 SWQHMATEAARTLQTAAQATLRQtepLTMA-RSRLTA-TFA---SQLHQGARAALTQASSSVQAATVTvmgarTLLADLE 1355
Cdd:COG4371 107 YWVYASAESQQTSLEQAEAKFNQ---LALAeRSKFTEeTLSnvnGQLRQATAKATTLAAEEPGEYIVV-----TLLVATR 178
|
90 100 110
....*....|....*....|....*....|..
gi 5001398 1356 GmKLQFPRPKDQA----ALQRKADSVSDRLLA 1383
Cdd:COG4371 179 G-KLELPKINSADdlrqALRQLGSIGSDRLLA 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1263-1505 |
4.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1263 SRAEDLGLKAK----ALEKTVASWQHMAteaartlqtAAQATLRQTEPLtmaRSRLTATFASQLHQGARAALTQASSSVQ 1338
Cdd:COG4913 238 ERAHEALEDAReqieLLEPIRELAERYA---------AARERLAELEYL---RAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1339 AATVTVMGARTLLADLEGmklqfprpkDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAK 1418
Cdd:COG4913 306 RLEAELERLEARLDALRE---------ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1419 DSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELeEAErvgagLSEMEQqiRESRISlEKDIETLS 1498
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL-EAE-----IASLER--RKSNIP-ARLLALRD 447
|
....*..
gi 5001398 1499 ELLARLG 1505
Cdd:COG4913 448 ALAEALG 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1504 |
5.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1250 LALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTlQTAAQATLRQTEPLTMARSRLTATFASQLHQgARAA 1329
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAA-LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1330 LTQASSSVQAATVTVMGARTLLADLEgmklqfprpkdqAALQRKADSVSDRLLADtRKKTKQAERMLGNAAPLSSSAKKK 1409
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELL------------RALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1410 GREAEVLAKDSAKLAKALLRERKQahrrasrlTSQTQATLQQASQQVLASEARRQELeeAERVGAGLSEMEQQIREsris 1489
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAE--------LEALLAELEEERAALEALKAERQKL--LARLEKELAELAAELAE---- 217
|
250
....*....|....*
gi 5001398 1490 LEKDIETLSELLARL 1504
Cdd:COG4942 218 LQQEAEELEALIARL 232
|
|
| TNFRSF5 |
cd13407 |
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 ... |
681-756 |
5.48e-03 |
|
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection.
Pssm-ID: 276912 [Multi-domain] Cd Length: 161 Bit Score: 39.31 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 681 GQFCESCAPGYKREMP-QGGPYASCVPCT-------------CNQHGTCDPNTG-------------ICVC--SHHTEGP 731
Cdd:cd13407 10 GRCCSLCPPGQKLVSDcTEATDTECLPCEegefqdtwnrerhCHQHRYCDPNLGlrvqtegtaetdtTCTCqeGQHCTSE 89
|
90 100 110
....*....|....*....|....*....|...
gi 5001398 732 SCERCL------PGFYGNPFAGQADD--CQPCP 756
Cdd:cd13407 90 ACETCAlhtsckPGFGVKQIATGVSDtiCEPCP 122
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1315-1521 |
5.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1315 TATFASQLHQGARAALTQASSsVQAatvtvmGARTLLADLEGMKLQFPRPKDQ-AALQRKADSVSDRLladtRKKTKQAE 1393
Cdd:COG4372 22 TGILIAALSEQLRKALFELDK-LQE------ELEQLREELEQAREELEQLEEElEQARSELEQLEEEL----EELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1394 RMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKallrERKQAHRRASRLTSQtQATLQQASQQvlaseaRRQELEEAERvg 1473
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQK----ERQDLEQQRKQLEAQ-IAELQSEIAE------REEELKELEE-- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 5001398 1474 aGLSEMEQQIRESRISLEK-DIETLSELLARLGSLDTHQAPAQALNETQ 1521
Cdd:COG4372 158 -QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEA 205
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1115-1333 |
6.08e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 41.15 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1115 LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHLAIEARALARSHRDTATKIAATAWRALLASNTSYALLWNL 1194
Cdd:COG0515 262 AAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1195 LEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKA 1274
Cdd:COG0515 342 AAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALA 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5001398 1275 LEKTVASWQHMATEAARTLQTAAQATLRQTEPLTMARSRLTATFASQLHQGARAALTQA 1333
Cdd:COG0515 422 AAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALA 480
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1412-1503 |
9.64e-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: 38.23 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1412 EAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAER-VGAGLSEMEQQIRESRISL 1490
Cdd:COG0711 42 EAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKA-EAE----AEAERiIAQAEAEIEQERAKALAEL 116
|
90
....*....|...
gi 5001398 1491 EKDIETLSELLAR 1503
Cdd:COG0711 117 RAEVADLAVAIAE 129
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1324-1532 |
9.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1324 QGARAALTQASSSVQAAT-----VTVMGARTLLAD-LEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAErmlg 1397
Cdd:COG3206 64 QSSDVLLSGLSSLSASDSpletqIEILKSRPVLERvVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIE---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5001398 1398 naapLSSSAKKKGREAEVLAKdsakLAKALLRERKQAHRRASRLTSQ-TQATLQQASQQVLASEARRQEL---------- 1466
Cdd:COG3206 140 ----ISYTSPDPELAAAVANA----LAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFrqknglvdls 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5001398 1467 EEAERVGAGLSEMEQQIRESRI----------SLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLG 1532
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAelaeaearlaALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT 287
|
|
| |
