|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.49e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 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 |
3.49e-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: 301.20 E-value: 3.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 767956020 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.05e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.02 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 540 LTAPEKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaGHPREVELRFHLQETSED 615
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767956020 616 VAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1499 |
7.31e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1071 GAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1151 KWSHLATEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1291 RTLQTAAQATLRQ--TEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASA--GFAGMKLQFPRPKDQAALQR 1366
Cdd:COG1196 538 AALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1367 KADSVSDRLLADTR--------KKTKQAERMLGNAAPLSSSAKKK--GREAEVLAKDSAKLAKALLRERKQAHRRASRLT 1436
Cdd:COG1196 618 LGDTLLGRTLVAARleaalrraVTLAGRLREVTLEGEGGSAGGSLtgGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1437 SQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRE--------------------SRISLEKDIETLSELLA 1496
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEElleeeelleeealeelpeppDLEELERELERLEREIE 777
|
...
gi 767956020 1497 RLG 1499
Cdd:COG1196 778 ALG 780
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.20e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.20e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKGC 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 |
1.60e-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: 66.22 E-value: 1.60e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKGCRAC 965
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-961 |
4.04e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.07 E-value: 4.04e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 916 SCKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKG 961
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| LamB |
smart00281 |
Laminin B domain; |
542-661 |
1.78e-12 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 65.75 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 542 APEKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgpQDAGHPRE---VELRFHLQE-TSE 614
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA------EGPPLPDElttVEVRFREENwQYY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767956020 615 DVAPPLPPfHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARP 661
Cdd:smart00281 83 GGRPVTRE-DLMMVLANLTAILIRATYSQQMAG-SRLSDVSLEVAVP 127
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
430-477 |
3.84e-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: 3.84e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 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 767956020 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 |
1.56e-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: 1.56e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767956020 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 |
3.26e-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: 3.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767956020 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1522 |
5.19e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.93 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTL---QTAAQatlrqtepLTKLHQEARAALTQASSSVQAAT-VTVMGART 1337
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKARTVaaeDTAAQ--------LAKAARTAEEVLTKASEDAKATTrAAAEEAER 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1338 LLADLEASAGfagmklqfpRPKDQAALQrkADSVSDRLLADT---RKKT----KQAERMLGNAAPLSSSAKKKG------ 1404
Cdd:NF041483 398 IRREAEAEAD---------RLRGEAADQ--AEQLKGAAKDDTkeyRAKTvelqEEARRLRGEAEQLRAEAVAEGerirge 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 --REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATLQQASqqvlaSEARRQELEEA 1463
Cdd:NF041483 467 arREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETLERTR-----AEAERLRAEAE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767956020 1464 ERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWALERLR 1522
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAEAERIR 606
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.61e-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: 5.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.64e-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: 2.64e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.36e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.36e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
4.92e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767956020 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1526 |
5.71e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1276 EKtvaswQHMATEAARTLQTAAQATLRQTEpltklhQEARAALTQASSSVQA-------------ATVTVMGARTL--LA 1340
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAE------EEVDELKSQLADYQQAldvqqtraiqyqqAVQALERAKQLcgLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1341 DLEASaGFAGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAEV 1409
Cdd:PRK04863 434 DLTAD-NAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1410 LAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRES 1480
Cdd:PRK04863 504 RLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767956020 1481 RISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1526
Cdd:PRK04863 581 RMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
6.10e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 6.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767956020 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 |
4.90e-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: 4.90e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 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 |
8.78e-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: 8.78e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 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 |
2.13e-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: 2.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.64e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 2.64e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGC 427
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
383-430 |
4.21e-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: 4.21e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1525 |
5.18e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATLR-----QTEPLTK-LHQEARAALTQASSSVQAATVTVmgaRTLLADLEA 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELRskreqEVTELKKaLEEETRSHEAQLQEMRQKHTQAL---EELTEQLEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1345 SAGFAGM--KLQFPRPKDQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL--AK 1419
Cdd:pfam01576 368 AKRNKANleKAKQALESENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSELesVS 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1420 ALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDIETLS 1492
Cdd:pfam01576 447 SLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQLSTLQ 523
|
330 340 350
....*....|....*....|....*....|....*...
gi 767956020 1493 ELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1525
Cdd:pfam01576 524 AQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
8.48e-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: 8.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 964 ACRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF-LTADGTHCQ 1011
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-317 |
9.17e-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: 9.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 270 RCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGT 317
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
965-1002 |
1.11e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.11e-07
10 20 30
....*....|....*....|....*....|....*....
gi 767956020 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1570 |
4.26e-07 |
|
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: 55.06 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1078 EQMMSLEGAVKAAREQLQRLNkgARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHL 1155
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLN--NEIERLEARLERLEdrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1156 ATEARALARshrdtATKIAATAWRALLASNTSYALLWNLLEGRVALetQRDLEDRYQEVQAAQKA--------------- 1220
Cdd:TIGR02168 457 ERLEEALEE-----LREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLKNqsglsgilgvlseli 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1221 -----LRTAVAEVLPE---------AESVLATVQ---QVGADTAPYLALLASPGALPQKSRAE-------------DLGL 1270
Cdd:TIGR02168 530 svdegYEAAIEAALGGrlqavvvenLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREilkniegflgvakDLVK 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1271 KAKALEKTVASW-------------QHMA-----------------------------TEAARTLQTAAQATLRQT-EPL 1307
Cdd:TIGR02168 610 FDPKLRKALSYLlggvlvvddldnaLELAkklrpgyrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKiEEL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1308 TKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAE 1387
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1388 RMLGNAAPLSSSAKKKGREAEVL-AKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEE-AER 1465
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqIEE 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1466 VGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQRKLSLLEQESQQQ 1545
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLE------EALALLRSELEELSEELRE---LESKRSELRRELEEL 920
|
570 580
....*....|....*....|....*
gi 767956020 1546 ELQIQGFESDLAEIRADKQNLEAIL 1570
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1261-1513 |
5.57e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.83 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1261 QKSRAEDLGLKAKALEKtVASWQHMATEAARTLQTAAQ--ATLRQTEP---LTKLHQEARAALTqasssvqaatvtvmGA 1335
Cdd:NF041483 527 ERTRAEAERLRAEAEEQ-AEEVRAAAERAARELREETEraIAARQAEAaeeLTRLHTEAEERLT--------------AA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1336 RTLLADLEASAgfagmklqfprpkdqAALQRKADSVSDRLLADT--RKKTKQ------AERMLGNAAPLSSSAKKKGR-- 1405
Cdd:NF041483 592 EEALADARAEA---------------ERIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLRTEAAADASAARAEGEnv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1406 ----------EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEARRQELEEAERVGAGLSE 1472
Cdd:NF041483 657 avrlrseaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EAARRRREAEETLGSARAE 725
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767956020 1473 MEQQIRESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1513
Cdd:NF041483 726 ADQERERAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.77e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767956020 810 CQCsgNVDPNAVGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGS 853
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1002 |
2.60e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.60e-06
10 20 30
....*....|....*....|....*....|....*....
gi 767956020 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.17e-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: 7.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767956020 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1482 |
2.89e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.05 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRQtepltklHQEAR-- 1315
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAART-------RADARed 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1316 AALTQASSSVQAATVtVMGARTLLADLEASAGFAGMKLQFPRPKdqAALQRKADSV--SDRLLADTrkkTKQAERMLGNA 1393
Cdd:NF041483 904 ANRIRSDAAAQADRL-IGEATSEAERLTAEARAEAERLRDEARA--EAERVRADAAaqAEQLIAEA---TGEAERLRAEA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1394 APLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVLASEA 1455
Cdd:NF041483 978 AETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQLTAKA 1057
|
250 260 270
....*....|....*....|....*....|....*
gi 767956020 1456 RRQELE---EAER-----VGAGLSEMEQQIRESRI 1482
Cdd:NF041483 1058 QEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.78e-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: 4.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 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 |
2.34e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 754 PCPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPLGLFG 802
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-377 |
4.34e-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: 4.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767956020 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 ... |
1405-1497 |
2.96e-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: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1483
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 767956020 1484 LEKDIETLSELLAR 1497
Cdd:cd06503 115 LRKEVADLAVEAAE 128
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
755-807 |
3.10e-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: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767956020 755 CPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.68e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.68e-03
10 20 30
....*....|....*....|....*....|....*...
gi 767956020 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.10e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.10e-03
10 20
....*....|....*....|....*....
gi 767956020 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 |
2.49e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 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 |
3.49e-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: 301.20 E-value: 3.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 767956020 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.05e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.02 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 540 LTAPEKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaGHPREVELRFHLQETSED 615
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767956020 616 VAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1499 |
7.31e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1071 GAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1151 KWSHLATEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1291 RTLQTAAQATLRQ--TEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASA--GFAGMKLQFPRPKDQAALQR 1366
Cdd:COG1196 538 AALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1367 KADSVSDRLLADTR--------KKTKQAERMLGNAAPLSSSAKKK--GREAEVLAKDSAKLAKALLRERKQAHRRASRLT 1436
Cdd:COG1196 618 LGDTLLGRTLVAARleaalrraVTLAGRLREVTLEGEGGSAGGSLtgGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1437 SQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRE--------------------SRISLEKDIETLSELLA 1496
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEElleeeelleeealeelpeppDLEELERELERLEREIE 777
|
...
gi 767956020 1497 RLG 1499
Cdd:COG1196 778 ALG 780
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.20e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.20e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKGC 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 |
1.60e-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: 66.22 E-value: 1.60e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 917 CKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKGCRAC 965
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-961 |
4.04e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.07 E-value: 4.04e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 916 SCKCHPLGSQEDQCHPKTGQCTCRPGVTGQACDRCQLGFFGFSIKG 961
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| LamB |
smart00281 |
Laminin B domain; |
542-661 |
1.78e-12 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 65.75 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 542 APEKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgpQDAGHPRE---VELRFHLQE-TSE 614
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA------EGPPLPDElttVEVRFREENwQYY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767956020 615 DVAPPLPPfHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARP 661
Cdd:smart00281 83 GGRPVTRE-DLMMVLANLTAILIRATYSQQMAG-SRLSDVSLEVAVP 127
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
430-477 |
3.84e-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: 3.84e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 430 CTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPHNPAGC 477
Cdd:pfam00053 1 CDCNPHGSLsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1073-1525 |
4.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1073 REAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkw 1152
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1153 shlaTEARALARSHRDTATKIAATAwRALLASNTSYALLWNLLEgrVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEA 1232
Cdd:COG1196 323 ----EELAELEEELEELEEELEELE-EELEEAEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1233 ESVLATVQQVGADTAPYLALLASpgALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQ 1312
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER--LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1313 EARAALTQASSSVQAAtvtvmgARTLLADLEASAGFAGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGN 1392
Cdd:COG1196 474 LLEAALAELLEELAEA------AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1393 AAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQA------TLQQASQQVLASEARRQELEEAERV 1466
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavdLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767956020 1467 GAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQL 1525
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1075-1573 |
9.65e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1075 AFLEQMmsLEGAVKAAREQLQRLNKgarcaqagsQKTCTQLADLEAVlessEEEIlhaaailasleipQEGPSQPTKWSH 1154
Cdd:COG4717 41 AFIRAM--LLERLEKEADELFKPQG---------RKPELNLKELKEL----EEEL-------------KEAEEKEEEYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1155 LATEARALARSHRDTATKIAAtaWRALLASNTSYALLWNLLEGRVALETQ-RDLEDRYQEVQAAQKALRTAVAEvLPEAE 1233
Cdd:COG4717 93 LQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEE-LEELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1234 SVLATVQQVgADTAPYLALLASPGALPQ-KSRAEDLGLKAKALEKTVASWQhMATEAARTLQTAAQATLRQTEPLTKLHQ 1312
Cdd:COG4717 170 AELAELQEE-LEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQ-EELEELEEELEQLENELEAAALEERLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1313 E--------ARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQFPRPKDQAALQrkadsvsdrlLADTRKKTK 1384
Cdd:COG4717 248 ArlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----------ALPALEELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1385 QAErmlgnaapLSSSAKKKGREAEvLAKDSAKLAKALLRERKQAHRRASRLTSQ-TQATLQQASQQVLAS---------E 1454
Cdd:COG4717 318 EEE--------LEELLAALGLPPD-LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEagvedeeelR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1455 ARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLS--ELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQ 1532
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELE------EELEELEEELEELREELAE---LE 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767956020 1533 RKlslleqesqqqelqIQGFESD--LAEIRADKQNLEAILHSL 1573
Cdd:COG4717 460 AE--------------LEQLEEDgeLAELLQELEELKAELREL 488
|
|
| 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 767956020 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 |
1.56e-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: 1.56e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767956020 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 |
3.26e-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: 3.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767956020 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1522 |
5.19e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.93 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTL---QTAAQatlrqtepLTKLHQEARAALTQASSSVQAAT-VTVMGART 1337
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKARTVaaeDTAAQ--------LAKAARTAEEVLTKASEDAKATTrAAAEEAER 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1338 LLADLEASAGfagmklqfpRPKDQAALQrkADSVSDRLLADT---RKKT----KQAERMLGNAAPLSSSAKKKG------ 1404
Cdd:NF041483 398 IRREAEAEAD---------RLRGEAADQ--AEQLKGAAKDDTkeyRAKTvelqEEARRLRGEAEQLRAEAVAEGerirge 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 --REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATLQQASqqvlaSEARRQELEEA 1463
Cdd:NF041483 467 arREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETLERTR-----AEAERLRAEAE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767956020 1464 ERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWALERLR 1522
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAEAERIR 606
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.61e-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: 5.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.64e-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: 2.64e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.36e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.36e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1195-1527 |
4.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1195 LEGRVA-LETQRDLEDRYQEVQAAQKALrtavaevlpEAESVLATVQQVGADtapyLALLaspgalpqKSRAEDLGLKAK 1273
Cdd:COG1196 198 LERQLEpLERQAEKAERYRELKEELKEL---------EAELLLLKLRELEAE----LEEL--------EAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1274 ALEKTVAswqhmATEAARTLQTAAQATLRQTepltklHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGfagmKL 1353
Cdd:COG1196 257 ELEAELA-----ELEAELEELRLELEELELE------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLE----EL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1354 QfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAkALLRERKQAHRRAS 1433
Cdd:COG1196 322 E----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1434 RLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLgsLDTHQAPAQALNE 1513
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL--LELLAELLEEAAL 474
|
330
....*....|....
gi 767956020 1514 TQWALERLRLQLGS 1527
Cdd:COG1196 475 LEAALAELLEELAE 488
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
4.92e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767956020 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1526 |
5.71e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1276 EKtvaswQHMATEAARTLQTAAQATLRQTEpltklhQEARAALTQASSSVQA-------------ATVTVMGARTL--LA 1340
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAE------EEVDELKSQLADYQQAldvqqtraiqyqqAVQALERAKQLcgLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1341 DLEASaGFAGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAEV 1409
Cdd:PRK04863 434 DLTAD-NAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1410 LAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRES 1480
Cdd:PRK04863 504 RLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767956020 1481 RISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1526
Cdd:PRK04863 581 RMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
6.10e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 6.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767956020 430 CTCNPAGSLD-TCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPH 472
Cdd:smart00180 1 CDCDPGGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1072-1527 |
3.13e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 61.46 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1072 AREAFLEQMMSLEGAVKAAREQLQRLnkgARCAQAGSQKtctqLADLEAVLESSEEEILHAAAILASLEIPQEgpsqptK 1151
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARL---DELEALIDQW----LAELEQVIALRRAGGLEAALALVRSGEGKA------L 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1152 WSHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPE 1231
Cdd:COG5278 151 MDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1232 AESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLH 1311
Cdd:COG5278 231 ALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1312 QEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQFprpkDQAALQRKADSVSDRLLADTRKKTKQAERMLG 1391
Cdd:COG5278 311 AAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEA----AAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1392 NAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLS 1471
Cdd:COG5278 387 AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAE 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 1472 EMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGS 1527
Cdd:COG5278 467 ELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1198-1528 |
4.33e-09 |
|
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: 61.51 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1198 RVALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQVGADtapYLALLASPGALPQK--SRAEDLGLKAK 1273
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELeeLSARESDLEQDYQAASD---HLNLVQTALRQQEKieRYQEDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1274 ALEKtvaswQHMATEAARTLQTAAQATLRQTEpltKLHQEARAAL-----------TQASSSVQAatVTVMG-ARTL--L 1339
Cdd:COG3096 362 RLEE-----QEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLadyqqaldvqqTRAIQYQQA--VQALEkARALcgL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1340 ADLEAsAGFAGMklqfprpkdQAALQRKADSVSDRLLadtrkktkQAERMLGnaapLSSSAKKKGREA---------EVL 1410
Cdd:COG3096 432 PDLTP-ENAEDY---------LAAFRAKEQQATEEVL--------ELEQKLS----VADAARRQFEKAyelvckiagEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1411 AKDSAKLAKALLRE----RKQAHRRAS----------RLTSQTQAT------LQQASQQVLASEARRQELEEAERVGAGL 1470
Cdd:COG3096 490 RSQAWQTARELLRRyrsqQALAQRLQQlraqlaeleqRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767956020 1471 SEMEQQIRESRISLEKdieTLSELLARLGSLdTHQAPaqALNETQWALERLRLQLGSP 1528
Cdd:COG3096 570 EEQAAEAVEQRSELRQ---QLEQLRARIKEL-AARAP--AWLAAQDALERLREQSGEA 621
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
382-428 |
4.90e-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: 4.90e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 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 |
8.78e-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: 8.78e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 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 |
2.13e-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: 2.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.64e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 2.64e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767956020 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGC 427
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
383-430 |
4.21e-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: 4.21e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1525 |
5.18e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATLR-----QTEPLTK-LHQEARAALTQASSSVQAATVTVmgaRTLLADLEA 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELRskreqEVTELKKaLEEETRSHEAQLQEMRQKHTQAL---EELTEQLEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1345 SAGFAGM--KLQFPRPKDQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL--AK 1419
Cdd:pfam01576 368 AKRNKANleKAKQALESENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSELesVS 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1420 ALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDIETLS 1492
Cdd:pfam01576 447 SLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQLSTLQ 523
|
330 340 350
....*....|....*....|....*....|....*...
gi 767956020 1493 ELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1525
Cdd:pfam01576 524 AQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
8.48e-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: 8.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767956020 964 ACRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF-LTADGTHCQ 1011
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-317 |
9.17e-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: 9.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767956020 270 RCKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRPWARGT 317
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
965-1002 |
1.11e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.11e-07
10 20 30
....*....|....*....|....*....|....*....
gi 767956020 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1073-1559 |
1.61e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 56.30 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1073 REAFLEQMMSLEgavkAAREQLQRLNKGARCAQAGSQKTCTQLADLEAV---LESSEEEILHAAAILASLEIPQEGPSQP 1149
Cdd:pfam07111 86 RETSLQQKMRLE----AQAMELDALAVAEKAGQAEAEGLRAALAGAEMVrknLEEGSQRELEEIQRLHQEQLSSLTQAHE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1150 TKWSHLATEARALARSHRDTATKIAATAWRALLASNTSyallwNLLEGRVAlETQRDLEDRYQEVQAaqkaLRTAVAEVL 1229
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEA-----ELLRKQLS-KTQEELEAQVTLVES----LRKYVGEQV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1230 P----------EAESVLATVQQVGADTApylallaspgalpqksraeDLGLKAKALEKTVASWQHMateaartLQTAAQA 1299
Cdd:pfam07111 232 PpevhsqtwelERQELLDTMQHLQEDRA-------------------DLQATVELLQVRVQSLTHM-------LALQEEE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1300 TLRQTEPLTKLHQE----ARAALTQASSSVQAATVTVMGArtllaDLEASAGFAGMKLQFPRPKDQAALQRKADSVSDRL 1375
Cdd:pfam07111 286 LTRKIQPSDSLEPEfpkkCRSLLNRWREKVFALMVQLKAQ-----DLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1376 LADTRKKTkQAERMLGNAAPLSSSAKKKGREAEVLAKDSAK-----LAKALLRERKQAHRRASRLtSQTQATLQQASQQV 1450
Cdd:pfam07111 361 LQDKAAEV-EVERMSAKGLQMELSRAQEARRRQQQQTASAEeqlkfVVNAMSSTQIWLETTMTRV-EQAVARIPSLSNRL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1451 -----------------LASEARRQEL----EEAERVGAGLSEMEQQIRESRISLEKDIETLSELLA------------- 1496
Cdd:pfam07111 439 syavrkvhtikglmarkVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQqevgrareqgeae 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767956020 1497 RLGSLDTHQAPAQALNETQWALERLRLQL-----GSPGSLQRKLSLLEQESQQQELQIQGFESDLAEI 1559
Cdd:pfam07111 519 RQQLSEVAQQLEQELQRAQESLASVGQQLevarqGQQESTEEAASLRQELTQQQEIYGQALQEKVAEV 586
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1570 |
4.26e-07 |
|
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: 55.06 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1078 EQMMSLEGAVKAAREQLQRLNkgARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHL 1155
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLN--NEIERLEARLERLEdrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1156 ATEARALARshrdtATKIAATAWRALLASNTSYALLWNLLEGRVALetQRDLEDRYQEVQAAQKA--------------- 1220
Cdd:TIGR02168 457 ERLEEALEE-----LREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLKNqsglsgilgvlseli 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1221 -----LRTAVAEVLPE---------AESVLATVQ---QVGADTAPYLALLASPGALPQKSRAE-------------DLGL 1270
Cdd:TIGR02168 530 svdegYEAAIEAALGGrlqavvvenLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREilkniegflgvakDLVK 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1271 KAKALEKTVASW-------------QHMA-----------------------------TEAARTLQTAAQATLRQT-EPL 1307
Cdd:TIGR02168 610 FDPKLRKALSYLlggvlvvddldnaLELAkklrpgyrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKiEEL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1308 TKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAE 1387
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1388 RMLGNAAPLSSSAKKKGREAEVL-AKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEE-AER 1465
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqIEE 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1466 VGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQRKLSLLEQESQQQ 1545
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLE------EALALLRSELEELSEELRE---LESKRSELRRELEEL 920
|
570 580
....*....|....*....|....*
gi 767956020 1546 ELQIQGFESDLAEIRADKQNLEAIL 1570
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1193-1575 |
5.12e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1193 NLLEGRVAlETQRDLEdRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADtapyLALLASPGALPQKSR---AEDLG 1269
Cdd:PRK02224 209 NGLESELA-ELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELETLEAE----IEDLRETIAETEREReelAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1270 LKAKALEKTVASWQHMATEAARTlQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGfa 1349
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1350 gmKLQFPRPKDQAALQRKADSVSDR--LLADTRKKTKQAERMLGNAAplsssakkkgreaevLAKDSAKLAKALLRERKQ 1427
Cdd:PRK02224 360 --ELREEAAELESELEEAREAVEDRreEIEELEEEIEELRERFGDAP---------------VDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1428 AHRraSRLTSqTQATLQQASQQVlaSEARR-----------QELEEAERVgAGLSEMEQQ----------IRESRISLEK 1486
Cdd:PRK02224 423 ELR--EREAE-LEATLRTARERV--EEAEAlleagkcpecgQPVEGSPHV-ETIEEDRERveeleaeledLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1487 DI---ETLSELLARLGSLDTHQAPAQAL--------NETQWALERLRLQ---LGSPGSLQRKL-SLLEQESQQQELQIQG 1551
Cdd:PRK02224 497 RLeraEDLVEAEDRIERLEERREDLEELiaerretiEEKRERAEELRERaaeLEAEAEEKREAaAEAEEEAEEAREEVAE 576
|
410 420
....*....|....*....|....
gi 767956020 1552 FESDLAEIRADKQNLEAILHSLPE 1575
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAA 600
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1261-1513 |
5.57e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.83 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1261 QKSRAEDLGLKAKALEKtVASWQHMATEAARTLQTAAQ--ATLRQTEP---LTKLHQEARAALTqasssvqaatvtvmGA 1335
Cdd:NF041483 527 ERTRAEAERLRAEAEEQ-AEEVRAAAERAARELREETEraIAARQAEAaeeLTRLHTEAEERLT--------------AA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1336 RTLLADLEASAgfagmklqfprpkdqAALQRKADSVSDRLLADT--RKKTKQ------AERMLGNAAPLSSSAKKKGR-- 1405
Cdd:NF041483 592 EEALADARAEA---------------ERIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLRTEAAADASAARAEGEnv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1406 ----------EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEARRQELEEAERVGAGLSE 1472
Cdd:NF041483 657 avrlrseaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EAARRRREAEETLGSARAE 725
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767956020 1473 MEQQIRESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1513
Cdd:NF041483 726 ADQERERAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1073-1498 |
6.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1073 REAFLEQMMSLEGAVKAAREQLQRLNKgarcAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKW 1152
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1153 SHLATEARALARSHRDTATKIAATAWRALLASNTSYALlwNLLEGRVALETQRDLED---RYQEVQAAQKALRTAVAEV- 1228
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEAq 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1229 --LPEAESVLATVQQVGADTAPY---------------LALLASPGALPQKSRAED-------LGLKAKALEKTVASWQH 1284
Cdd:COG4717 220 eeLEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIagvlflvLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1285 MATEAARTLQTAAQATLRQTEpLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAgfAGMKLQfPRPKDQAAL 1364
Cdd:COG4717 300 LGKEAEELQALPALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLE-ELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1365 QRKADSVSD----------RLLADTRKKTKQAERMLGNAAPlsssakkkGREAEVLAKDSAKLAKALLRERKQAHRRASR 1434
Cdd:COG4717 376 LAEAGVEDEeelraaleqaEEYQELKEELEELEEQLEELLG--------ELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 1435 LT--SQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLekdiETLSELLARL 1498
Cdd:COG4717 448 LEelREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL----ELLEEAREEY 509
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.77e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767956020 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 ... |
1083-1573 |
1.10e-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: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1083 LEGAVKAAREQLQRLNK-----GARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWSH 1154
Cdd:TIGR02168 300 LEQQKQILRERLANLERqleelEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEaELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1155 LATEARALARSHRDTATKIAAT------------AWRALLASNTSyALLWNLLEGRVAlETQRDLEDRYQEVQAAQKALR 1222
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEierlearlerleDRRERLQQEIE-ELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1223 TAVAEvLPEAESVLATVQQVGADTAPYLALLASPGALPQK--SRAEDLGLKAKALektvasWQHmATEAARTLQTAAQat 1300
Cdd:TIGR02168 458 RLEEA-LEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKAL------LKN-QSGLSGILGVLSE-- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1301 LRQTEPltKLHQEARAALtqaSSSVQAATV----TVMGARTLLAdlEASAGFAGM------KLQFPRPKDQAALQRKADS 1370
Cdd:TIGR02168 528 LISVDE--GYEAAIEAAL---GGRLQAVVVenlnAAKKAIAFLK--QNELGRVTFlpldsiKGTEIQGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1371 VSdrLLADTRKKTKQAER----MLG---------NAAPLSSSAKKKGR----EAEVLAKD-----SAKLAKALLRERKQA 1428
Cdd:TIGR02168 601 LG--VAKDLVKFDPKLRKalsyLLGgvlvvddldNALELAKKLRPGYRivtlDGDLVRPGgvitgGSAKTNSSILERRRE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1429 HRRASRLTSQTQATLQQASQQVLASEARRQELEEAER-VGAGLSEMEQQIRESRISL---EKDIETLSELLARLGSLDTH 1504
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTE 758
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956020 1505 QAPAQALNETQWALERLRLQLGSPGSLQrklslleqesqqQELQIQGFESDLAEIRADKQNLEAILHSL 1573
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEE------------LEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1078-1328 |
1.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1078 EQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwSHLAT 1157
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR------------EELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1158 EARALARSHRDTatkiaaTAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLA 1237
Cdd:COG3883 91 RARALYRSGGSV------SYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1238 TVQQVGADTApylALLASpgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAA 1317
Cdd:COG3883 165 ELEAAKAELE---AQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|.
gi 767956020 1318 LTQASSSVQAA 1328
Cdd:COG3883 237 AAAAAAAASAA 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1114-1523 |
1.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1114 QLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlatEARALARSHRDTATKIAATAWRALLASNTSYAllwn 1193
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELE-----------------AELEELRLELEELELELEEAQAEEYELLAELA---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1194 LLEGRVALETQR--DLEDRYQEVQAAQKALRTAVAevlpEAESVLATVQQVGADTAPYLALLAspgALPQKSRAEDLGLK 1271
Cdd:COG1196 299 RLEQDIARLEERrrELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1272 AKALEKtVASWQHMATEAARTLQTAAQATLRQTEPLTKL--HQEARAALTQASSSVQAATVTVMGARTLLADLEASAGfa 1349
Cdd:COG1196 372 AELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1350 gmklqfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAH 1429
Cdd:COG1196 449 ---------EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1430 RRASRLTSQ------TQATLQQASQQVLASEARRQELEEAERVGAGLSEmEQQIRESRISLEKdIETLSELLARLGSLDT 1503
Cdd:COG1196 520 RGLAGAVAVligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA-AKAGRATFLPLDK-IRARAALAAALARGAI 597
|
410 420
....*....|....*....|
gi 767956020 1504 HQAPAQALNETQWALERLRL 1523
Cdd:COG1196 598 GAAVDLVASDLREADARYYV 617
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1002 |
2.60e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.60e-06
10 20 30
....*....|....*....|....*....|....*....
gi 767956020 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1070-1576 |
2.65e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1070 PGAREAFLEQMMSLeGAVKAAREQLQRLNKGARCAQAGSQktcTQLADLEAVLESSEEEILHAAaiLASLEipQEGPSQP 1149
Cdd:PRK02224 148 PSDRQDMIDDLLQL-GKLEEYRERASDARLGVERVLSDQR---GSLDQLKAQIEEKEEKDLHER--LNGLE--SELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1150 TKWSHLaTEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRD-LEDRYQEVQAAQKALRTAVAEV 1228
Cdd:PRK02224 220 EEIERY-EEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREeLAEEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1229 L-------PEAESVLATVQQVGADTAPYLALL--ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQA 1299
Cdd:PRK02224 299 LaeaglddADAEAVEARREELEDRDEELRDRLeeCRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1300 TLRQTEPLTKLHQEARAAltqaSSSVQAATVTVMGARTLLADLEASAGFAGMKLQFPRpkdqAALQRKADSVSD--RLLA 1377
Cdd:PRK02224 379 VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREERDELREREAELE----ATLRTARERVEEaeALLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1378 ---------------------DTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKalLRERKQAhrrASRLT 1436
Cdd:PRK02224 451 agkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER--LEERRED---LEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1437 SQTQATLQQASQQVLASEARRQELE-EAERVGAGLSEMEQQIRESRI---SLEKDIETLSELLARLGSLDTHQAPAQALN 1512
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERIRTLLAAIADAE 605
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 1513 EtqwALERLRLQLGSPGSL--QRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPEN 1576
Cdd:PRK02224 606 D---EIERLREKREALAELndERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEK 668
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1086-1522 |
5.59e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1086 AVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlaTEARALARS 1165
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE----------------EEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1166 HRDTATKI-AATAWRALLASNTsyallwNLLEGRVA-LETQ-RDLEDRYQEVQAAQKA---------------------L 1221
Cdd:PRK02224 400 FGDAPVDLgNAEDFLEELREER------DELREREAeLEATlRTARERVEEAEALLEAgkcpecgqpvegsphvetieeD 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1222 RTAVAEVLPEAESVLATVQQVGA--DTAPYLALLASpgalpqksRAEDLGLKAKALEKTVAswQHMATEAARTLQTAaqa 1299
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEErlERAEDLVEAED--------RIERLEERREDLEELIA--ERRETIEEKRERAE--- 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1300 TLR-QTEPLTKLHQEARAALTQASSSVQAATVTVmgartllADLEasagfagmklqfprpKDQAALQRKADSVSD--RLL 1376
Cdd:PRK02224 541 ELReRAAELEAEAEEKREAAAEAEEEAEEAREEV-------AELN---------------SKLAELKERIESLERirTLL 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1377 ADTRKKTKQAERMlgnaaplsssAKKKGREAEVLAKDSAKLAKalLRERKQahrrasrltsQTQATLQQAsqqvlASEAR 1456
Cdd:PRK02224 599 AAIADAEDEIERL----------REKREALAELNDERRERLAE--KRERKR----------ELEAEFDEA-----RIEEA 651
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956020 1457 RQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSL-DTHqapaQALNETQWALERLR 1522
Cdd:PRK02224 652 REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELrERR----EALENRVEALEALY 714
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1070-1533 |
6.27e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 51.40 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1070 PGAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAgsqktCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQP 1149
Cdd:COG3899 721 YAEALRYLERALELLPPDPEEEYRLALLLELAEALYL-----AGRFEEAEALLERALAARALAALAALRHGNPPASARAY 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1150 TKWSHLAT----EARALARSHRDTATKIAATAWRALLASNTSYALLWnLLEGRVALETQRDLEDRYQEVQAAQKALRTAV 1225
Cdd:COG3899 796 ANLGLLLLgdyeEAYEFGELALALAERLGDRRLEARALFNLGFILHW-LGPLREALELLREALEAGLETGDAALALLALA 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1226 AEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTE 1305
Cdd:COG3899 875 AAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAAL 954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1306 PLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQFPRPKDQ-AALQRKADSVSDRLLADTRKKTK 1384
Cdd:COG3899 955 AAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAaAAALAAALLAAALAALAAAAAAA 1034
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1385 QAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAE 1464
Cdd:COG3899 1035 ALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAAL 1114
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956020 1465 RVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1533
Cdd:COG3899 1115 ALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALL 1183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1491 |
6.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1199 VALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADtapyLALLASPGALPQKSRAEDLGLKAKALEKT 1278
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1279 VASWQHMATeaartLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLqfprp 1358
Cdd:TIGR02168 778 AEAEAEIEE-----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----- 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1359 KDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLtSQ 1438
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQ 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767956020 1439 TQATLQQASQQVL-----ASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETL 1491
Cdd:TIGR02168 927 LELRLEGLEVRIDnlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.17e-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: 7.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767956020 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1405-1579 |
1.10e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 REAEVLAKDSAKLAKALLrERKQAHRRASRLTSQtqatLQQASQQVlasEARRQELEEAERvgaGLSEMEQQIRESRISL 1484
Cdd:COG4372 21 KTGILIAALSEQLRKALF-ELDKLQEELEQLREE----LEQAREEL---EQLEEELEQARS---ELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1485 EKDIETLSELLARLGSLDTHQAPAQA-LNETQWALERLRLQLgspGSLQRKLSLLEQESQQQELQIQGFESDLAEIRADK 1563
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEeLEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170
....*....|....*.
gi 767956020 1564 QNLEAILHSLPENCAS 1579
Cdd:COG4372 167 AALEQELQALSEAEAE 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1495 |
1.46e-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: 50.06 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1083 LEGAVKAAREQLQRLNKGARCAQagsqktctQLADLEAvlessEEEILHAAAILASLEipqegpSQPTKWSHLATEARAL 1162
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAE--------RYKELKA-----ELRELELALLVLRLE------ELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1163 ARSHRDTATKIAAtawrallasntsYALLWNLLEGRValetqRDLEDRYQEVQAAQKALRTAVAEVlpeaesvlatVQQV 1242
Cdd:TIGR02168 252 EEELEELTAELQE------------LEEKLEELRLEV-----SELEEEIEELQKELYALANEISRL----------EQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1243 GAdtapylallaspgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQatlrQTEPLTKLHQEARAALTQAS 1322
Cdd:TIGR02168 305 QI----------------LRERLANLERQLEELEAQLEELESKLDELAEELAELEE----KLEELKEELESLEAELEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1323 SSVQAATVTVMGARTLLadLEASAGFAGMKLQfpRPKDQAALQRKADSVSDrlLADTRKKTKQaERMLGNAAPLSSSAKK 1402
Cdd:TIGR02168 365 AELEELESRLEELEEQL--ETLRSKVAQLELQ--IASLNNEIERLEARLER--LEDRRERLQQ-EIEELLKKLEEAELKE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1403 KGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQAtLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRI 1482
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
410
....*....|...
gi 767956020 1483 SLEKDIETLSELL 1495
Cdd:TIGR02168 517 GLSGILGVLSELI 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1114-1358 |
1.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1114 QLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlaTEARALARSHRDTATKIAATAwRALLASNTSYALLWN 1193
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK----------------KEEKALLKQLAALERRIAALA-RRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1194 LLegrvaletqRDLEDRYQEVQAAQKALRTAVAEVLPEAesvlatvQQVGAdtAPYLALLASPGALPQ------------ 1261
Cdd:COG4942 84 EL---------AELEKEIAELRAELEAQKEELAELLRAL-------YRLGR--QPPLALLLSPEDFLDavrrlqylkyla 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1262 ---KSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAA-------------QATLRQTEPLTKLHQEARAALTQASSSV 1325
Cdd:COG4942 146 parREQAEELRADLAELAALRAELEAERAELEALLAELEeeraalealkaerQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|...
gi 767956020 1326 QAATVTVMGARTLLADLEASAGFAGMKLQFPRP 1358
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1482 |
2.89e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.05 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRQtepltklHQEAR-- 1315
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAART-------RADARed 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1316 AALTQASSSVQAATVtVMGARTLLADLEASAGFAGMKLQFPRPKdqAALQRKADSV--SDRLLADTrkkTKQAERMLGNA 1393
Cdd:NF041483 904 ANRIRSDAAAQADRL-IGEATSEAERLTAEARAEAERLRDEARA--EAERVRADAAaqAEQLIAEA---TGEAERLRAEA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1394 APLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVLASEA 1455
Cdd:NF041483 978 AETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQLTAKA 1057
|
250 260 270
....*....|....*....|....*....|....*
gi 767956020 1456 RRQELE---EAER-----VGAGLSEMEQQIRESRI 1482
Cdd:NF041483 1058 QEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1521 |
3.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1250 LALLASPGALPQKSRAEDLGLKAKALEKTVAswqhmateaartlqtAAQATLRQTEpltKLHQEARAALTQASSSVQAAT 1329
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIA---------------ELEKELAALK---KEEKALLKQLAALERRIAALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1330 VTVMGARTLLADLEASAGFAGMKLQfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKkkgreaev 1409
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIA----ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1410 lakdSAKLAKALLRERKQahrrasrLTSQTQATLQQASQQVLASEARRQELEEAErvgaglsemeQQIRESRISLEKDIE 1489
Cdd:COG4942 137 ----RLQYLKYLAPARRE-------QAEELRADLAELAALRAELEAERAELEALL----------AELEEERAALEALKA 195
|
250 260 270
....*....|....*....|....*....|...
gi 767956020 1490 TLSELLARL-GSLDTHQAPAQALNETQWALERL 1521
Cdd:COG4942 196 ERQKLLARLeKELAELAAELAELQQEAEELEAL 228
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1088-1486 |
3.48e-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: 48.49 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1088 KAAREQLQRLNKgarcaQAGSQKtctqlaDLEAVLESSEEEILHAAAILASLeipQEGpsqptKWSHLATEARALARSHR 1167
Cdd:pfam05701 229 KQAEEELQRLNQ-----QLLSAK------DLKSKLETASALLLDLKAELAAY---MES-----KLKEEADGEGNEKKTST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1168 DTatkiaatawRALLASntsyallwnllegrvaleTQRDLEDRYQEVQAAQ---KALRTAVAEVLPEAE---SVLATVQQ 1241
Cdd:pfam05701 290 SI---------QAALAS------------------AKKELEEVKANIEKAKdevNCLRVAAASLRSELEkekAELASLRQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1242 VGAdtapylalLASPGALpqkSRAEDLGLKAKALE----KTVASWQHMaTEAARTLQTAAQatlrQTEPLTKLHQEARAA 1317
Cdd:pfam05701 343 REG--------MASIAVS---SLEAELNRTKSEIAlvqaKEKEAREKM-VELPKQLQQAAQ----EAEEAKSLAQAAREE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1318 LTQASS-SVQA-ATVTVMGARTLLADLEASAGFAGMKLQFPRPKdqaALQRKADSVSDRLLADTRKK-TKQAERMlgnaA 1394
Cdd:pfam05701 407 LRKAKEeAEQAkAAASTVESRLEAVLKEIEAAKASEKLALAAIK---ALQESESSAESTNQEDSPRGvTLSLEEY----Y 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1395 PLSssakKKGREAEVLAKDSAKLAKALLRERKQAHRRasrltsqTQATLQQASQQvlaSEARRQEL----EEAERVGAGL 1470
Cdd:pfam05701 480 ELS----KRAHEAEELANKRVAEAVSQIEEAKESELR-------SLEKLEEVNRE---MEERKEALkialEKAEKAKEGK 545
|
410
....*....|....*.
gi 767956020 1471 SEMEQQIRESRISLEK 1486
Cdd:pfam05701 546 LAAEQELRKWRAEHEQ 561
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.78e-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: 4.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 327 CNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHwDPRMPCQPC 383
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1073-1302 |
5.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1073 REAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEI---LHAAAILASLEIPQE--GPS 1147
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRALYRLGRQPPLALllSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1148 QPTKWSHLATEARALARSHRDTATKIAATawRALLASNtsyallwnllegRVALETQRD-LEDRYQEVQAAQKALRTAVA 1226
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAAL------------RAELEAERAeLEALLAELEEERAALEALKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956020 1227 evlpEAESVLATVQQVGADtapylallaspgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLR 1302
Cdd:COG4942 196 ----ERQKLLARLEKELAE---------------LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1286-1518 |
5.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1286 ATEAARTLQTAAQATLRQTepLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQfprpkDQAALQ 1365
Cdd:COG3206 147 PELAAAVANALAEAYLEQN--LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE-----AKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1366 RKADSVSDRL-----LADTRKKTKQAERMLGNAAPLSSSAKKKGREAEV---LAKDSAKLAKAL------------LRER 1425
Cdd:COG3206 220 QLSELESQLAearaeLAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraqLAELEAELAELSarytpnhpdviaLRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1426 KQAHRRasRLTSQTQATLQQASQQVLASEARRQEL----EEAERVGAGLSEMEQQIREsrisLEKDIETLSE----LLAR 1497
Cdd:COG3206 300 IAALRA--QLQQEAQRILASLEAELEALQAREASLqaqlAQLEARLAELPELEAELRR----LEREVEVARElyesLLQR 373
|
250 260
....*....|....*....|.
gi 767956020 1498 LGSLDThqapAQALNETQWAL 1518
Cdd:COG3206 374 LEEARL----AEALTVGNVRV 390
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1398-1498 |
7.39e-05 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 44.22 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1398 SSAKKKGREAEvlakdsaKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLA---SEARRQeLEEAERvgaglsEME 1474
Cdd:PRK07353 46 AEAKERLAEAE-------KLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAeaqAEAQAS-KEKARR------EIE 111
|
90 100
....*....|....*....|....*
gi 767956020 1475 QQIRESRISLEKDIETLSEL-LARL 1498
Cdd:PRK07353 112 QQKQAALAQLEQQVDALSRQiLEKL 136
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1398-1496 |
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 767956020 1398 SSAKKKGREAEVLAKDsaklAKALLrerKQAHRRASRLTSQTQAtlqQASQQVlaSEARRQELEEAER-VGAGLSEMEQQ 1476
Cdd:PRK05759 45 AAAERAKKELELAQAK----YEAQL---AEARAEAAEIIEQAKK---RAAQII--EEAKAEAEAEAARiKAQAQAEIEQE 112
|
90 100
....*....|....*....|
gi 767956020 1477 IRESRISLEKDIETLSELLA 1496
Cdd:PRK05759 113 RKRAREELRKQVADLAVAGA 132
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1078-1533 |
1.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1078 EQMMSLEGAVKAAREQLQRLNkgARCAQAGSQktctQLADLE---AVLESSEEEILHAAAILASL--EIPQEGPSQPTKW 1152
Cdd:COG4913 309 AELERLEARLDALREELDELE--AQIRGNGGD----RLEQLEreiERLERELEERERRRARLEALlaALGLPLPASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1153 SHLATEARALARSHRDTATKIAATAWRALLAsntsyalLWNLLEGRVALETQRD-LEDR---Y-QEVQAAQKALRTA--- 1224
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAA-------LRDLRRELRELEAEIAsLERRksnIpARLLALRDALAEAlgl 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1225 -------VAE---VLPE-------AESVLAT-----------------------------VQQVGADTAPYLALLASPGA 1258
Cdd:COG4913 456 deaelpfVGElieVRPEeerwrgaIERVLGGfaltllvppehyaaalrwvnrlhlrgrlvYERVRTGLPDPERPRLDPDS 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1259 LPQKsraedlgLKAKAlektvaswqHMATEAARTLqTAAQATLRQTEPLTKLHQEARAaltqasssvqaatVTVMGartl 1338
Cdd:COG4913 536 LAGK-------LDFKP---------HPFRAWLEAE-LGRRFDYVCVDSPEELRRHPRA-------------ITRAG---- 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1339 ladleasagfagmklQFPRPKDQAALQRKADSVSDRLL-ADTRKKTKQAERMLGNAAplsssakkkgREAEVLAKDSAKL 1417
Cdd:COG4913 582 ---------------QVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELE----------EELAEAEERLEAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1418 AKAL--LRERKQAHRRASRLTSqTQATLQQASQQVLASEARRQELEEAervGAGLSEMEQQIRESRISLEKDIETLSELL 1495
Cdd:COG4913 637 EAELdaLQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDAS---SDDLAALEEQLEELEAELEELEEELDELK 712
|
490 500 510
....*....|....*....|....*....|....*...
gi 767956020 1496 ARLGSLDTHQAPAQALnetqwaLERLRLQLGSPGSLQR 1533
Cdd:COG4913 713 GEIGRLEKELEQAEEE------LDELQDRLEAAEDLAR 744
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1225-1482 |
1.14e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1225 VAEVLPEAESVLATVQQVGADT------APYLALLASPGALPQKSRAEDLGLKAKALEKTVASwqhmatEAARTLQT--- 1295
Cdd:TIGR02794 24 YHSVKPEPGGGAEIIQAVLVDPgavaqqANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA------EQARQKELeqr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1296 -AAQATLRQTEP-----LTKLHQEARAALTQASSSVQAATVTvmGARTLLADLEASAGFAGMKlqfprpKDQAALQRKAD 1369
Cdd:TIGR02794 98 aAAEKAAKQAEQaakqaEEKQKQAEEAKAKQAAEAKAKAEAE--AERKAKEEAAKQAEEEAKA------KAAAEAKKKAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1370 SVSDRLLADTRKKT---KQAERmlGNAAPLSSSAKKKgreAEVLAKDSAKLAKAlLRERKQAHRRASRLTSQTQATLQQA 1446
Cdd:TIGR02794 170 EAKKKAEAEAKAKAeaeAKAKA--EEAKAKAEAAKAK---AAAEAAAKAEAEAA-AAAAAEAERKADEAELGDIFGLASG 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 767956020 1447 SQQVLASEARRQELEEAERVGAGlseMEQQIRESRI 1482
Cdd:TIGR02794 244 SNAEKQGGARGAAAGSEVDKYAA---IIQQAIQQNL 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1283-1501 |
1.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1283 QHMAT-EAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQ-AATVTVMGARTLLADLEAsagfagmKLQfprpKD 1360
Cdd:COG4913 232 EHFDDlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEA-------ELE----EL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1361 QAALQRKADSVSDrlLADTRKKTKQAERMLGNAAplsssAKKKGREAEVLAKDSAKLAKALlRERKQAHRRASRLTSQTQ 1440
Cdd:COG4913 301 RAELARLEAELER--LEARLDALREELDELEAQI-----RGNGGDRLEQLEREIERLEREL-EERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767956020 1441 ATLQqASQQVLAsEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSL 1501
Cdd:COG4913 373 LPLP-ASAEEFA-ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1216-1503 |
1.80e-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: 46.48 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1216 AAQKALRTAVAEV---LPEAESVLATVQQVGADTAPYLALLAspGALPQKS--RAEDLGLKAKALEKTVASwqhmATEAA 1290
Cdd:COG3096 836 AELAALRQRRSELereLAQHRAQEQQLRQQLDQLKEQLQLLN--KLLPQANllADETLADRLEELREELDA----AQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1291 RTLQtAAQATLRQTEPLtklhqearaaltqasssvqaatvtvmgARTLLADLEAsagFAGMKLQFPRPKD-QAALQRKAD 1369
Cdd:COG3096 910 AFIQ-QHGKALAQLEPL---------------------------VAVLQSDPEQ---FEQLQADYLQAKEqQRRLKQQIF 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1370 SVSD---RLLADTRKKtkqAERMLGNAAPLSSSAKKKGREAEvlakdsaklakallrerkQAHRRASRLTSQTQATLQQA 1446
Cdd:COG3096 959 ALSEvvqRRPHFSYED---AVGLLGENSDLNEKLRARLEQAE------------------EARREAREQLRQAQAQYSQY 1017
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956020 1447 SqQVLAS-----EARRQELEEAERVGAGL-----SEMEQQIRESRISLEkdiETLSELLARLGSLDT 1503
Cdd:COG3096 1018 N-QVLASlkssrDAKQQTLQELEQELEELgvqadAEAEERARIRRDELH---EELSQNRSRRSQLEK 1080
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1194-1492 |
1.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1194 LLEGRVALETQRDLEDRYQEVQAAQKA-LRTAVAEVLpEAESVLATVQQvGADTAPYLALlaspgalpQKSRAEDLGLKA 1272
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEArAEAAEEEVD-ELKSQLADYQQ-ALDVQQTRAI--------QYQQAVQALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1273 KAL----EKTVASWQHMATEAARTLQTAAQAtLRQTEPLTKLHQEARAALTQASSSVQAATVTV------MGARTLLADL 1342
Cdd:PRK04863 427 KQLcglpDLTADNAEDWLEEFQAKEQEATEE-LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1343 E----ASAGFAGMKLQFPRPKDQAALQRKADsvsdRLLADTRKktkQAERMLGNAAPLSSSAKKKGREAEVL---AKDSA 1415
Cdd:PRK04863 506 ReqrhLAEQLQQLRMRLSELEQRLRQQQRAE----RLLAEFCK---RLGKNLDDEDELEQLQEELEARLESLsesVSEAR 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1416 KLAKALLRERKQAHRRASRLTSQT------QATLQQASQQVLASEARRQELEE-----AERVGAgLSEMEQQIRESRISL 1484
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARApawlaaQDALARLREQSGEEFEDSQDVTEymqqlLERERE-LTVERDELAARKQAL 657
|
....*...
gi 767956020 1485 EKDIETLS 1492
Cdd:PRK04863 658 DEEIERLS 665
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
754-802 |
2.34e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767956020 754 PCPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPLGLFG 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 ... |
1374-1528 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1374 RLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS 1453
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956020 1454 EARRQELEEAERVGAGLSEMEQQIRESRIS-LEKDIETLSELLaRLGSLDTHQAPAQA-LNETQWALERLRLQLGSP 1528
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEI-RSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSP 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1156-1508 |
2.86e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1156 ATEARALARSHRDTATKIAATAWRALLASNTSyallwnlLEGRVAlETQRDLEDRyqEVQAAQKALRTAVAEVLPEAESv 1235
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALERQKEA-------IERQLA-SLEEELEKL--TEEISELEKRLEEIEQLLEELN- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1236 lATVQQVGADTapYLALlaspgalpqKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAA---QATLRQTEPLTKLHQ 1312
Cdd:TIGR02169 279 -KKIKDLGEEE--QLRV---------KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeiDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1313 EARAALTQASSSVQAATVTVMGARTLLADLEASAGFAGMKL-QFPRPKDQaaLQRKADSV---SDRLLADTRKKTKQAER 1388
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkDYREKLEK--LKREINELkreLDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1389 MlgnaaplssSAKKKGREAEVLAKDSAKLAKALlrERKQAHRRASrltsQTQATLQQASQQVLASEAR-----------R 1457
Cdd:TIGR02169 425 L---------NAAIAGIEAKINELEEEKEDKAL--EIKKQEWKLE----QLAADLSKYEQELYDLKEEydrvekelsklQ 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767956020 1458 QELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPA 1508
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-377 |
4.34e-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: 4.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767956020 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]; |
1287-1534 |
5.54e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1287 TEAARTLQTAAQATLRQTEPLTKLHQEARAaltQASSSVQAATVTVMGArTLLADLEASAGFAGMKLQFPR-----PKDQ 1361
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQ---KAKEEAEEERLAELEA-KRQAEEEAREAKAEAEQRAAElaaeaAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1362 AALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQA 1441
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1442 TLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERL 1521
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250
....*....|...
gi 767956020 1522 RLQLGSPGSLQRK 1534
Cdd:COG3064 240 TEEAALGGAEEAA 252
|
|
| TNFRSF6B |
cd10575 |
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ... |
684-777 |
5.57e-04 |
|
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: 42.39 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 684 CEsCAPGYKREMPqggpyascvpcTCNQHGTCDPNTGICVCSHHTEGPSCERCLPGFYgNPFAGQADDCQP-CPCPGQSA 762
Cdd:cd10575 80 CE-CKPGYYMEHG-----------FCLRHSSCPPGEGVIKLGTPYSDTQCEPCPPGFF-SASSSSTEPCQPhTNCTQGGL 146
|
90
....*....|....*..
gi 767956020 763 CTTIP--ESREVVCTHC 777
Cdd:cd10575 147 ETNVPgnDYHDTLCTSC 163
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1159-1533 |
8.55e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 44.24 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1159 ARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLAT 1238
Cdd:COG3903 569 ERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAA 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1239 VQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLtkLHQEARAAL 1318
Cdd:COG3903 649 AAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAA--AAAAAAAAA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1319 TQASSSVQAATVTVMGARTLLADLEASAGFAGMKLQfprpkDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSS 1398
Cdd:COG3903 727 LLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAA-----LAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAA 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1399 SAkkkGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIR 1478
Cdd:COG3903 802 AA---AAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAA 878
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767956020 1479 ESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1533
Cdd:COG3903 879 AAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1089-1499 |
8.97e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1089 AAREQLQRLNKGARCAQAGSQKT---CTQLADLEAVLESSEE---EILHAAAILASLEIPQEGpsqptKWSHLATEARAL 1162
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLkerEQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCG-----SCIHPNPARQDI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1163 ARSHRDTA--TKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDryQEVQA-AQKalRTAVAEVLPeaesvlaTV 1239
Cdd:TIGR00618 521 DNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ--QSFSIlTQC--DNRSKEDIP-------NL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1240 QQVGADTAPYLallaspgalPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQatlRQTEPLTKLHQEArAALT 1319
Cdd:TIGR00618 590 QNITVRLQDLT---------EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQ-LTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1320 QASSSVQAATVTVMGARTLLADLEASAgfagmKLQfpRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSS 1399
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQ-----KMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1400 AKKKGREAEVLAKDSAKLAKALLRERKQAHRRASrltsqtqatlQQASQQVLASEARRQELEEAERvgaglsEMEQQIRE 1479
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAH----------FNNNEEVTAALQTGAELSHLAA------EIQFFNRL 793
|
410 420
....*....|....*....|
gi 767956020 1480 srisLEKDIETLSELLARLG 1499
Cdd:TIGR00618 794 ----REEDTHLLKTLEAEIG 809
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1188-1465 |
1.18e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 43.46 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1188 YAL---LWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVL------------ATVQQVGADTAPYLAL 1252
Cdd:COG0515 192 YSLgvtLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVlralakdpeeryQSAAELAAALRAVLRS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1253 LASPGALPQKSRAEDLGLKAKALEktVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTV 1332
Cdd:COG0515 272 LAAAAAAAAAAAAAAAAAAAAAAA--AAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1333 MGARTLLADLEASAGFAGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAK 1412
Cdd:COG0515 350 ALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767956020 1413 DSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAER 1465
Cdd:COG0515 430 AAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALALA 482
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1568 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1389 MLGNAAPLSSSAKKKGREAEvLAKDSAKLaKALLRERKQAHRRASRLTSQtqatLQQASQQVLASEARRQELE-EAERVG 1467
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAE-LEQLQQEI-AELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEqELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1468 AGLSEMEQQIREsrisLEKDIETLSELLARlgsldthQAPAQALNETQWALERLrLQLGSPGSLQRKLSLLEQESQQQEL 1547
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAE-------LLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180
....*....|....*....|.
gi 767956020 1548 QIQGFESDLAEIRADKQNLEA 1568
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 ... |
1405-1489 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS---EARRQELEEAERVGAGLSEMEQQIRE-- 1479
Cdd:pfam00430 40 AEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAaeaEAERIIEQAAAEIEQEKDRALAELRQqv 119
|
90
....*....|...
gi 767956020 1480 ---SRISLEKDIE 1489
Cdd:pfam00430 120 valAVQIAEKLLE 132
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1397-1524 |
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 767956020 1397 SSSAKKKGREAEVLAKDSAKlaKALLRERKQAHRRASRLTSQT-----------------QATLQQASQQVLASEARRQE 1459
Cdd:pfam01576 128 TTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSNLaeeeekakslsklknkhEAMISDLEERLKKEEKGRQE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1460 LEEAERVGAG--------LSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQA--------LNETQWALERLRL 1523
Cdd:pfam01576 206 LEKAKRKLEGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaqISELQEDLESERA 285
|
.
gi 767956020 1524 Q 1524
Cdd:pfam01576 286 A 286
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1405-1497 |
2.96e-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: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1405 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1483
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 767956020 1484 LEKDIETLSELLAR 1497
Cdd:cd06503 115 LRKEVADLAVEAAE 128
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1407-1530 |
3.04e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1407 AEVLAKdsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQvLASEA--RRQELEEAervgagLSEMEQQIRESRISL 1484
Cdd:COG1842 47 AQVIAN-----QKRLERQLEELEAEAEKWEEKARLALEKGRED-LAREAleRKAELEAQ------AEALEAQLAQLEEQV 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767956020 1485 EKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGS 1530
Cdd:COG1842 115 EKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
755-807 |
3.10e-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: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767956020 755 CPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1262-1497 |
3.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1262 KSRAEDLGLKAKALEKTVASWQHMATEAARTLQTA-AQATLRQTEpltklhqEARAALTQASSSVQAATVTVMGARTLLA 1340
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELE-------AELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1341 DLEasagfagmklqfprpKDQAALQRKADSVSDRlLADTRKKTKQAERMLGNAAPLSSSAKKKG----REAEVLAKDSAK 1416
Cdd:COG4913 703 ELE---------------EELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRALleerFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1417 LAKALLRERKQAHRRASRLTSQTQATLQQ-------ASQQVLAS-------EARRQELEEaervgAGLSEMEQQIRESRI 1482
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAfnrewpaETADLDADleslpeyLALLDRLEE-----DGLPEYEERFKELLN 841
|
250
....*....|....*.
gi 767956020 1483 SLEK-DIETLSELLAR 1497
Cdd:COG4913 842 ENSIeFVADLLSKLRR 857
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1312-1462 |
3.30e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1312 QEARAALTQASSSVQAATVTVMGARTLLADLEASAgfagmklqfprpKDQAALQRKADSVSDRLLADTRKKtKQAERMLG 1391
Cdd:pfam00529 61 DSAEAQLAKAQAQVARLQAELDRLQALESELAISR------------QDYDGATAQLRAAQAAVKAAQAQL-AQAQIDLA 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767956020 1392 NAAPLsssAKKKG--REAEVLAKDSAKLAKALLRERKQAHRRASR-LTSQTQATLQQASQQVLASEARRQELEE 1462
Cdd:pfam00529 128 RRRVL---APIGGisRESLVTAGALVAQAQANLLATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.68e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.68e-03
10 20 30
....*....|....*....|....*....|....*...
gi 767956020 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.10e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.10e-03
10 20
....*....|....*....|....*....
gi 767956020 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 ... |
1421-1498 |
4.23e-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: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1421 LLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEA--ERVGAGLSEMEQQIRESRIS-LEKDIETLSELLAR 1497
Cdd:TIGR02473 7 LLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQalEKVGAGTSALELSNYQRFIRqLDQRIQQQQQELAL 86
|
.
gi 767956020 1498 L 1498
Cdd:TIGR02473 87 L 87
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1513 |
5.03e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1053 LLGEAPRGDVYQ-GHHLLPGARE--AFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLA---DLEAVLESSE 1126
Cdd:COG3096 484 IAGEVERSQAWQtARELLRRYRSqqALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1127 EEILHAAAILASleipqegpsqptkwshlATEARALARSHRDTAtkiaatawRALLASNTSYALLWnllegRVAletqrd 1206
Cdd:COG3096 564 AQLEELEEQAAE-----------------AVEQRSELRQQLEQL--------RARIKELAARAPAW-----LAA------ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1207 ledryqevQAAQKALRTAVAEVLPEAESVLATVQQVGADtapylallaspgaLPQKSRAEDLGLKAK-ALEKTVASWQHM 1285
Cdd:COG3096 608 --------QDALERLREQSGEALADSQEVTAAMQQLLER-------------EREATVERDELAARKqALESQIERLSQP 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1286 A-TEAARTLQTAAQ------------ATLRQTEPLTKLHQEARAALTQASSSvqaatvtvmGARTLLADLEASagfagmk 1352
Cdd:COG3096 667 GgAEDPRLLALAERlggvllseiyddVTLEDAPYFSALYGPARHAIVVPDLS---------AVKEQLAGLEDC------- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1353 lqfprPKDQAALQRKADSVSDRLL-------ADTRKKTKQAER--------MLGNAAPlSSSAKKKGREAEVLAKDSAKL 1417
Cdd:COG3096 731 -----PEDLYLIEGDPDSFDDSVFdaeeledAVVVKLSDRQWRysrfpevpLFGRAAR-EKRLEELRAERDELAEQYAKA 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1418 AkALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQeLEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLAR 1497
Cdd:COG3096 805 S-FDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQR-RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQ 882
|
490
....*....|....*...
gi 767956020 1498 LGSLD--THQAPAQALNE 1513
Cdd:COG3096 883 ANLLAdeTLADRLEELRE 900
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1157-1581 |
5.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1157 TEARALARSHRDTATKIAAtaWRALLASNTSYA--LLWNLLEGRvaletQRDLEDRYQEVQAAQKALRTAVAEVLPEAES 1234
Cdd:COG4913 255 EPIRELAERYAAARERLAE--LEYLRAALRLWFaqRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1235 VLATVQQVGADtapylallaspgalpqksRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEA 1314
Cdd:COG4913 328 LEAQIRGNGGD------------------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1315 RAALTQASSSVQAATVTVMGARTLLADLEASAGfagmKLQfprpKDQAALQRKADSVSDRLLAdTRKKTKQA-------- 1386
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELR----ELE----AEIASLERRKSNIPARLLA-LRDALAEAlgldeael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1387 --------------------ERMLGNAApLS---------------SSAKKKGR-------------EAEVLAKDS--AK 1416
Cdd:COG4913 461 pfvgelievrpeeerwrgaiERVLGGFA-LTllvppehyaaalrwvNRLHLRGRlvyervrtglpdpERPRLDPDSlaGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1417 L----------AKALLRERK-----------QAHRRA---SRLTSQT-----------------------------QATL 1443
Cdd:COG4913 540 LdfkphpfrawLEAELGRRFdyvcvdspeelRRHPRAitrAGQVKGNgtrhekddrrrirsryvlgfdnraklaalEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1444 QQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRiSLEKDIETLSELLARLgsldthQAPAQALNETQWALERLRL 1523
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYS-WDEIDVASAEREIAEL------EAELERLDASSDDLAALEE 692
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767956020 1524 QLgspGSLQRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPENCASWQ 1581
Cdd:COG4913 693 QL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| TNFRSF5 |
cd13407 |
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 ... |
681-756 |
5.36e-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: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 681 GQFCESCAPGYKREMP-QGGPYASCVPCT-------------CNQHGTCDPNTG-------------ICVC--SHHTEGP 731
Cdd:cd13407 10 GRCCSLCPPGQKLVSDcTEATDTECLPCEegefqdtwnrerhCHQHRYCDPNLGlrvqtegtaetdtTCTCqeGQHCTSE 89
|
90 100 110
....*....|....*....|....*....|...
gi 767956020 732 SCERCL------PGFYGNPFAGQADD--CQPCP 756
Cdd:cd13407 90 ACETCAlhtsckPGFGVKQIATGVSDtiCEPCP 122
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1115-1335 |
8.75e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 40.38 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1115 LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNL 1194
Cdd:COG0515 262 AAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1195 LEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKA 1274
Cdd:COG0515 342 AAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALA 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767956020 1275 LEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGA 1335
Cdd:COG0515 422 AAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALALA 482
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1406-1497 |
9.60e-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: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956020 1406 EAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAER-VGAGLSEMEQQIRESRISL 1484
Cdd:COG0711 42 EAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKA-EAE----AEAERiIAQAEAEIEQERAKALAEL 116
|
90
....*....|...
gi 767956020 1485 EKDIETLSELLAR 1497
Cdd:COG0711 117 RAEVADLAVAIAE 129
|
|
| |
