|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.65e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
3.71e-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: 3.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 110611156 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.03e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.02 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 540 LTAPEKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaGHPREVELRFHLQETSED 615
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 110611156 616 VAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1515 |
7.47e-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: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1071 GAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1151 KWSHLATEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1291 RTLQTAAQATLRQ--TEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDR 1368
Cdd:COG1196 538 AALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1369 LLADTRKKTKQAERMLGN---AAPLSSSAKKKGREAEVL-----------AKDSAKLAKALLRERKQAHRRASRLTSQTQ 1434
Cdd:COG1196 618 LGDTLLGRTLVAARLEAAlrrAVTLAGRLREVTLEGEGGsaggsltggsrRELLAALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1435 ATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSE-LLARLGSLDTHQAPAQALNETQWALE 1513
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEeALEELPEPPDLEELERELERLEREIE 777
|
..
gi 110611156 1514 RL 1515
Cdd:COG1196 778 AL 779
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.25e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.25e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
1.69e-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: 1.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 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 |
4.18e-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: 4.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 110611156 542 APEKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgpQDAGHPRE---VELRFHLQE-TSE 614
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA------EGPPLPDElttVEVRFREENwQYY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 110611156 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 |
3.90e-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: 3.90e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 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 |
1.04e-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: 1.04e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110611156 706 PCTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAGQadDCQ 753
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
865-915 |
1.63e-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: 1.63e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110611156 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 |
3.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 3.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 110611156 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.81e-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: 5.81e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1516 |
1.73e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.00 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTL---QTAAQatlrqtepLTKLHQEARAALTQASSSVQAATvtvmgaRTL 1338
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKARTVaaeDTAAQ--------LAKAARTAEEVLTKASEDAKATT------RAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1339 LADLEgmklqfprpkdqaALQRKADSVSDRLLA---------------DT---RKKT----KQAERMLGNAAPLSSSAKK 1396
Cdd:NF041483 392 AEEAE-------------RIRREAEAEADRLRGeaadqaeqlkgaakdDTkeyRAKTvelqEEARRLRGEAEQLRAEAVA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1397 KG--------REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATLQQASqqvlaSEA 1449
Cdd:NF041483 459 EGerirgearREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETLERTR-----AEA 533
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1450 RRQELEEAERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWALERLR 1516
Cdd:NF041483 534 ERLRAEAEEQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAEAERIR 606
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.68e-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: 2.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.55e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.55e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
5.00e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 110611156 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
6.32e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 6.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110611156 430 CTCNPAGSLD-TCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPH 472
Cdd:smart00180 1 CDCDPGGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1520 |
2.40e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1276 EKtvaswQHMATEAARTLQTAAQATLRQTE---------------PLTKLH------QEARAALTQASSSVQAATVTvmg 1334
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAEeevdelksqladyqqALDVQQtraiqyQQAVQALERAKQLCGLPDLT--- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1335 artlLADLEGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAEV 1403
Cdd:PRK04863 437 ----ADNAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1404 LAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRES 1474
Cdd:PRK04863 504 RLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110611156 1475 RISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1520
Cdd:PRK04863 581 RMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
382-428 |
5.03e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 5.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 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 |
8.92e-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: 8.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1519 |
2.10e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATLR-----QTEPLTK-LHQEARAALTQASSSVQAATVTVmgaRTLLADLEg 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELRskreqEVTELKKaLEEETRSHEAQLQEMRQKHTQAL---EELTEQLE- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1345 mklQFPRPK------------DQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL 1411
Cdd:pfam01576 367 ---QAKRNKanlekakqalesENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1412 --AKALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDI 1482
Cdd:pfam01576 443 esVSSLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQL 519
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110611156 1483 ETLSELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1519
Cdd:pfam01576 520 STLQAQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-857 |
2.16e-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: 2.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 810 CQCSGNVDPNavGNCDPLSGHClRCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.71e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 2.71e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
4.32e-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: 4.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1567 |
5.78e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1083 LEGAVKAAREQLQRLNK-----GARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWSH 1154
Cdd:TIGR02168 300 LEQQKQILRERLANLERqleelEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEaELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1155 LATEARALARSHRDTATKIAAT------------AWRALLASNTSyALLWNLLEGRVAlETQRDLEDRYQEVQAAQKALR 1222
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEierlearlerleDRRERLQQEIE-ELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1223 TAVAEvLPEAESVLATVQQVGADTAPYLALLASPGALPQK--SRAEDLGLKAKALEK----------------TVASWQH 1284
Cdd:TIGR02168 458 RLEEA-LEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKnqsglsgilgvlseliSVDEGYE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1285 MATEAArtLQTAAQATLRQTEPLTKLhqeARAALTQASSsvqaatvtvmGARTLLAdLEGMKLQFPRPKDQAALQRKADS 1364
Cdd:TIGR02168 537 AAIEAA--LGGRLQAVVVENLNAAKK---AIAFLKQNEL----------GRVTFLP-LDSIKGTEIQGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1365 VSdrLLADTRKKTKQAER----MLG---------NAAPLSSSAKKKGR----EAEVLAKD-----SAKLAKALLRERKQA 1422
Cdd:TIGR02168 601 LG--VAKDLVKFDPKLRKalsyLLGgvlvvddldNALELAKKLRPGYRivtlDGDLVRPGgvitgGSAKTNSSILERRRE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1423 HRRASRLTSQTQATLQQASQQVLASEARRQELEEAER-VGAGLSEMEQQIRESRISL---EKDIETLSELLARLGSLDTH 1498
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTE 758
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110611156 1499 QAPAQALNETQWALERLRLQLGSPGSLQrklslleqesqqQELQIQGFESDLAEIRADKQNLEAILHSL 1567
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEE------------LEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
8.78e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 8.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 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 |
9.22e-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: 9.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 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 |
1.13e-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: 1.13e-07
10 20 30
....*....|....*....|....*....|....*....
gi 110611156 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1261-1507 |
2.92e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.60 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1261 QKSRAEDLGLKAKALEKtVASWQHMATEAARTLQTAAQ--ATLRQTEP---LTKLHQEARAALTqasssvqAATVTVMGA 1335
Cdd:NF041483 527 ERTRAEAERLRAEAEEQ-AEEVRAAAERAARELREETEraIAARQAEAaeeLTRLHTEAEERLT-------AAEEALADA 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1336 RTlladlegmklqfprpkDQAALQRKADSVSDRLLADT--RKKTKQ------AERMLGNAAPLSSSAKKKGR-------- 1399
Cdd:NF041483 599 RA----------------EAERIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLRTEAAADASAARAEGEnvavrlrs 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1400 ----EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEARRQELEEAERVGAGLSEMEQQIR 1472
Cdd:NF041483 663 eaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EAARRRREAEETLGSARAEADQERE 731
|
250 260 270
....*....|....*....|....*....|....*.
gi 110611156 1473 ESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1507
Cdd:NF041483 732 RAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.97e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.97e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110611156 810 CQCsgNVDPNAVGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGS 853
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1002 |
2.69e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.69e-06
10 20 30
....*....|....*....|....*....|....*....
gi 110611156 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1476 |
3.40e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRQtepltklHQEARA- 1316
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAART-------RADAREd 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1317 -------ALTQASSSVQAATVTvmgARTLLADLEGMKLQFPRPKDQAALQRKADSV--SDRLLADTrkkTKQAERMLGNA 1387
Cdd:NF041483 904 anrirsdAAAQADRLIGEATSE---AERLTAEARAEAERLRDEARAEAERVRADAAaqAEQLIAEA---TGEAERLRAEA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1388 APLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVLASEA 1449
Cdd:NF041483 978 AETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQLTAKA 1057
|
250 260 270
....*....|....*....|....*....|....*
gi 110611156 1450 RRQELE---EAER-----VGAGLSEMEQQIRESRI 1476
Cdd:NF041483 1058 QEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.29e-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: 7.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 110611156 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.90e-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: 4.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 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 |
2.35e-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: 2.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 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 |
4.46e-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: 4.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 110611156 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 ... |
1399-1491 |
2.95e-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: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1399 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1477
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 110611156 1478 LEKDIETLSELLAR 1491
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 |
3.09e-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: 3.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 110611156 755 CPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.63e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|....*...
gi 110611156 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.13e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.13e-03
10 20
....*....|....*....|....*....
gi 110611156 348 HGGRCHhCRDHTAGPHCERCQENFYHWDP 376
Cdd:smart00180 16 DTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1216-1485 |
4.87e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1216 AAQKALRTaVAEVLPEAESVLAtvqqvgADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQT 1295
Cdd:NF041483 911 AAAQADRL-IGEATSEAERLTA------EARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1296 AAQATLRQTEPLTKLHQEARAALTQASSSVQA-ATVTVMGAR---------------TLLADLEGMKLQFPRPKDQAALQ 1359
Cdd:NF041483 984 AQQHAERIRTEAERVKAEAAAEAERLRTEAREeADRTLDEARkdankrrseaaeqadTLITEAAAEADQLTAKAQEEALR 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1360 --RKADSVSDRLLADTRkktKQAERMLGNAAPLSSSAKKKGR-EAEVLAKDSAKLAKAL------LRER-----KQAHRR 1425
Cdd:NF041483 1064 ttTEAEAQADTMVGAAR---KEAERIVAEATVEGNSLVEKARtDADELLVGARRDATAIreraeeLRDRitgeiEELHER 1140
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611156 1426 ASRLTSQTQAT--------LQQASQQVLASEARRQELeeaervgagLSEMEQQIRESRISLEKDIETL 1485
Cdd:NF041483 1141 ARRESAEQMKSagercdalVKAAEEQLAEAEAKAKEL---------VSDANSEASKVRIAAVKKAEGL 1199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.65e-102 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 326.46 E-value: 2.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 35 CLPVFENAAFGRLAQASHTCG-SPPEDFCPHVGAAGaGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPSMAfgVQ 113
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEG-GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 114 YPtSVNITLRLGKAYEITYVRLKFHTSRPESFAIYKRSRADGPWEPYQFYSASCQKTYGRPEGQYLRPGEDErvAFCTSE 193
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
3.71e-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: 3.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 29 AGRPQRCLPVFENAAFGRLAQASHTCGSP-PEDFCPHVGAAGAGAHCQRCDAADPQRHHNASYLTDFHSQDESTWWQSPS 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 108 MAFGVQYptsVNITLRLGKAYEITYVRLKFHTSRPeSFAIYKRSRADGPWEPYQFYSASCQKTYGR-PEGQYLRPGEDEr 186
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 187 vAFCTSEFSDISPLSGGNVAFSTLEGRPSAYNFEESPGLQEWVTSTELLISLDRLNTFGDDIFKD-PKVLQSYYYAVSDF 265
Cdd:smart00136 156 -VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDI 234
|
....
gi 110611156 266 SVGG 269
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
540-671 |
3.03e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.02 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 540 LTAPEKFLGDQRFSYGQPLILTFRVP--PGDSPLPV--QLRLEGTGLALSLRHSSLSGPQDaGHPREVELRFHLQETSED 615
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 110611156 616 VAPPLPPFHFQRLLANLTSLRLRVSPGPSPAGpVFLTEVRLTSARPG-LSPPASWVE 671
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQ-VSLSNVSLDSAVPGgSGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1515 |
7.47e-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: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1071 GAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIpQEGPSQpT 1150
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1151 KWSHLATEARALARSHRDTATKIAA----------------TAWRALLASNTSYALLwnLLEGRVALETQRDLEDRYQEV 1214
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEEleeaeeallerlerleEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1215 QAAQKALRTAVAEVLPEAESVLATVQ-QVGADTAPYLALL---ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAA 1290
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLeELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1291 RTLQTAAQATLRQ--TEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDR 1368
Cdd:COG1196 538 AALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1369 LLADTRKKTKQAERMLGN---AAPLSSSAKKKGREAEVL-----------AKDSAKLAKALLRERKQAHRRASRLTSQTQ 1434
Cdd:COG1196 618 LGDTLLGRTLVAARLEAAlrrAVTLAGRLREVTLEGEGGsaggsltggsrRELLAALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1435 ATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSE-LLARLGSLDTHQAPAQALNETQWALE 1513
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEeALEELPEPPDLEELERELERLEREIE 777
|
..
gi 110611156 1514 RL 1515
Cdd:COG1196 778 AL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1072-1493 |
1.22e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1072 AREAFLEQMMSLEGAVKAAREQLQRLNKGARcAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQptk 1151
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE--- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1152 wsHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQevQAAQKALRTAVAEVLPE 1231
Cdd:COG1196 446 --EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE--GFLEGVKAALLLAGLRG 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1232 AESVLATVQQVGAdtAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKL- 1310
Cdd:COG1196 522 LAGAVAVLIGVEA--AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGa 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1311 HQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRpkdqaALQRKADSVSDRLLADTRKKTKQAERMLGNAAPL 1390
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV-----TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1391 SSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQ 1470
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
410 420
....*....|....*....|....*.
gi 110611156 1471 IRE---SRISLEKDIETLSELLARLG 1493
Cdd:COG1196 755 ELPeppDLEELERELERLEREIEALG 780
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-962 |
1.25e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.25e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
1.69e-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: 1.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 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 |
4.18e-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: 4.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 110611156 542 APEKFLGDQRFSYGQPLILTFRVPPGDSPLPVQ---LRLEGTGLALSLRHsslsgpQDAGHPRE---VELRFHLQE-TSE 614
Cdd:smart00281 9 APEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapdVILEGNGLRISHPA------EGPPLPDElttVEVRFREENwQYY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 110611156 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 |
3.90e-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: 3.90e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 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 |
1.04e-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: 1.04e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110611156 706 PCTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAGQadDCQ 753
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
865-915 |
1.63e-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: 1.63e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 110611156 865 PCSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQP-GRGCR 915
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1073-1519 |
1.64e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1073 REAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkw 1152
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1153 shlaTEARALARSHRDTATKIAATAwRALLASNTSYALLWNLLEgrVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEA 1232
Cdd:COG1196 323 ----EELAELEEELEELEEELEELE-EELEEAEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1233 ESVLATVQQVGADTAPYLALLASpgALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQ 1312
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER--LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1313 EARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSS 1392
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1393 SAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQA------TLQQASQQVLASEARRQELEEAERVGAGLSE 1466
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavdLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1467 MEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQL 1519
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1075-1567 |
2.42e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1075 AFLEQMmsLEGAVKAAREQLQRLNKgarcaqagsQKTCTQLADLEAVlessEEEIlhaaailasleipQEGPSQPTKWSH 1154
Cdd:COG4717 41 AFIRAM--LLERLEKEADELFKPQG---------RKPELNLKELKEL----EEEL-------------KEAEEKEEEYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1155 LATEARALARSHRDTATKIAAtaWRALLASNTSYALLWNLLEGRVALETQ-RDLEDRYQEVQAAQKALRTAVAEvLPEAE 1233
Cdd:COG4717 93 LQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEE-LEELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1234 SVLATVQQVgADTAPYLALLASPGALPQ-KSRAEDLGLKAKALEKTVASWQhMATEAARTLQTAAQATLRQTEPLTKLHQ 1312
Cdd:COG4717 170 AELAELQEE-LEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQ-EELEELEEELEQLENELEAAALEERLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1313 E--------ARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRpKDQAALQRKADSVsdrLLADTRKKTKQAErml 1384
Cdd:COG4717 248 ArlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA-REKASLGKEAEEL---QALPALEELEEEE--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1385 gnaapLSSSAKKKGREAEvLAKDSAKLAKALLRERKQAHRRASRLTSQ-TQATLQQASQQVLAS---------EARRQEL 1454
Cdd:COG4717 321 -----LEELLAALGLPPD-LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEagvedeeelRAALEQA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1455 EEAERVGAGLSEMEQQIRESRISLEKDIETLS--ELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQRKlsll 1532
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELE------EELEELEEELEELREELAE---LEAE---- 461
|
490 500 510
....*....|....*....|....*....|....*..
gi 110611156 1533 eqesqqqelqIQGFESD--LAEIRADKQNLEAILHSL 1567
Cdd:COG4717 462 ----------LEQLEEDgeLAELLQELEELKAELREL 488
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
866-914 |
3.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 3.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 110611156 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQ--PGRGC 914
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
429-477 |
5.81e-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: 5.81e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 429 PCTCNPAGSL-DTCDPRSGRCPCKENVEGNLCDRCRPGTFNLqPHNPAGC 477
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1198-1516 |
1.73e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.00 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1198 RVALETQRDLEDRYQEvqaAQKALRTAVAE---VLPEAESVlATVQQVGADTA---------PYLALL---ASPGALPQK 1262
Cdd:NF041483 254 RQAAELSRAAEQRMQE---AEEALREARAEaekVVAEAKEA-AAKQLASAESAneqrtrtakEEIARLvgeATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1263 SRAEDLGLKAKA-LEKTVASwqhmATEAARTL---QTAAQatlrqtepLTKLHQEARAALTQASSSVQAATvtvmgaRTL 1338
Cdd:NF041483 330 AEAEQALADARAeAEKLVAE----AAEKARTVaaeDTAAQ--------LAKAARTAEEVLTKASEDAKATT------RAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1339 LADLEgmklqfprpkdqaALQRKADSVSDRLLA---------------DT---RKKT----KQAERMLGNAAPLSSSAKK 1396
Cdd:NF041483 392 AEEAE-------------RIRREAEAEADRLRGeaadqaeqlkgaakdDTkeyRAKTvelqEEARRLRGEAEQLRAEAVA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1397 KG--------REAEVLAKDSAKLAKALL-------------------RERKQAHRRASRLTSQTQATLQQASqqvlaSEA 1449
Cdd:NF041483 459 EGerirgearREAVQQIEEAARTAEELLtkakadadelrstataeseRVRTEAIERATTLRRQAEETLERTR-----AEA 533
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1450 RRQELEEAERVGAGLSEMEQQIRESRISLEKDIET----LSELLARL--GSLDTHQAPAQALNETQWALERLR 1516
Cdd:NF041483 534 ERLRAEAEEQAEEVRAAAERAARELREETERAIAArqaeAAEELTRLhtEAEERLTAAEEALADARAEAERIR 606
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-752 |
2.68e-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: 2.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPfAGQADDC 752
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
866-914 |
3.55e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.55e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 866 CSCHPQGSVSEQmpCDPVTGQCSCLPHVTARDCSRCYPGFFDLQPGrGC 914
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-747 |
5.00e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 110611156 707 CTCNQHGT----CDPNTGICVCSHHTEGPSCERCLPGFYGNPFAG 747
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
430-472 |
6.32e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 6.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110611156 430 CTCNPAGSLD-TCDPRSGRCPCKENVEGNLCDRCRPGTFNLQPH 472
Cdd:smart00180 1 CDCDPGGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1195-1521 |
2.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1195 LEGRVA-LETQRDLEDRYQEVQAAQKALrtavaevlpEAESVLATVQQVGADtapyLALLaspgalpqKSRAEDLGLKAK 1273
Cdd:COG1196 198 LERQLEpLERQAEKAERYRELKEELKEL---------EAELLLLKLRELEAE----LEEL--------EAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1274 ALEKTVAswqhmATEAARTLQTAAQATLRQTEpltklhQEARAALTQASSSVQAATVTVMGARTLLADLEgmklqfprpK 1353
Cdd:COG1196 257 ELEAELA-----ELEAELEELRLELEELELEL------EEAQAEEYELLAELARLEQDIARLEERRRELE---------E 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1354 DQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQT 1433
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1434 QATLQQAS-QQVLASEARRQELEEAERVG--AGLSEMEQQIRESRISLEKDIETLSELLARL-GSLDTHQAPAQALNETQ 1509
Cdd:COG1196 397 ELAAQLEElEEAEEALLERLERLEEELEEleEALAELEEEEEEEEEALEEAAEEEAELEEEEeALLELLAELLEEAALLE 476
|
330
....*....|..
gi 110611156 1510 WALERLRLQLGS 1521
Cdd:COG1196 477 AALAELLEELAE 488
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1200-1520 |
2.40e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1200 ALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQvgaDTAPYLALLASPGALPQK-SRA-EDLGLKAKAL 1275
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELaeLNEAESDLEQDYQ---AASDHLNLVQTALRQQEKiERYqADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1276 EKtvaswQHMATEAARTLQTAAQATLRQTE---------------PLTKLH------QEARAALTQASSSVQAATVTvmg 1334
Cdd:PRK04863 365 EE-----QNEVVEEADEQQEENEARAEAAEeevdelksqladyqqALDVQQtraiqyQQAVQALERAKQLCGLPDLT--- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1335 artlLADLEGMklqfprpkdQAALQRKADSVSDRLLADTRK----------KTKQAERMLGNAAPLS-SSAKKKGREAEV 1403
Cdd:PRK04863 437 ----ADNAEDW---------LEEFQAKEQEATEELLSLEQKlsvaqaahsqFEQAYQLVRKIAGEVSrSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1404 LAKDSAKLAKAL---------LRERKQAHRRASRLTSQTQatlQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRES 1474
Cdd:PRK04863 504 RLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110611156 1475 RISLEKDIETLSELLARLgsldTHQAPA-QALNEtqwALERLRLQLG 1520
Cdd:PRK04863 581 RMALRQQLEQLQARIQRL----AARAPAwLAAQD---ALARLREQSG 620
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1198-1522 |
3.21e-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: 61.89 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1198 RVALETQRDLEDRYQEVQAAQKALRTAVAEV--LPEAESVLATVQQVGADtapYLALLASPGALPQK--SRAEDLGLKAK 1273
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELeeLSARESDLEQDYQAASD---HLNLVQTALRQQEKieRYQEDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1274 ALEKtvaswQHMATEAARTLQTAAQATLRQTE---------------PLTKLH------QEARAALTQASSSVQAATVTV 1332
Cdd:COG3096 362 RLEE-----QEEVVEEAAEQLAEAEARLEAAEeevdslksqladyqqALDVQQtraiqyQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1333 MGARTLladlegmklqfprpkdQAALQRKADSVSDRLLadtrkktkQAERMLGnaapLSSSAKKKGREA---------EV 1403
Cdd:COG3096 437 ENAEDY----------------LAAFRAKEQQATEEVL--------ELEQKLS----VADAARRQFEKAyelvckiagEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1404 LAKDSAKLAKALLRE----RKQAHRRAS----------RLTSQTQAT------LQQASQQVLASEARRQELEEAERVGAG 1463
Cdd:COG3096 489 ERSQAWQTARELLRRyrsqQALAQRLQQlraqlaeleqRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 110611156 1464 LSEMEQQIRESRISLEKdieTLSELLARLGSLdTHQAPaqALNETQWALERLRLQLGSP 1522
Cdd:COG3096 569 LEEQAAEAVEQRSELRQ---QLEQLRARIKEL-AARAP--AWLAAQDALERLREQSGEA 621
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
382-428 |
5.03e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 5.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 382 PCDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSE--GGCR 428
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1072-1521 |
6.15e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 60.69 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1072 AREAFLEQMMSLEGAVKAAREQLQRLnkgARCAQAGSQKtctqLADLEAVLESSEEEILHAAAILASLEIPQEgpsqptK 1151
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARL---DELEALIDQW----LAELEQVIALRRAGGLEAALALVRSGEGKA------L 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1152 WSHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPE 1231
Cdd:COG5278 151 MDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1232 AESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLH 1311
Cdd:COG5278 231 ALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1312 QEARAALTQASSSVQAATVT--VMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAP 1389
Cdd:COG5278 311 AAAAAAAAAAAAAALAALLAlaLATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVEL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1390 LSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQ 1469
Cdd:COG5278 391 EVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAA 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 110611156 1470 QIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGS 1521
Cdd:COG5278 471 VAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
810-857 |
8.92e-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: 8.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 810 CQCSGNVDPNavGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1202-1519 |
2.10e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1202 ETQRDLEDRYQEVQAAQKAL------RTAVAEVLPEAESVLATVQQvgaDtapylalLASPGAlpQKSRAE----DLGLK 1271
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQE---D-------LESERA--ARNKAEkqrrDLGEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1272 AKALEktvaswqhmaTEAARTLQ-TAAQATLR-----QTEPLTK-LHQEARAALTQASSSVQAATVTVmgaRTLLADLEg 1344
Cdd:pfam01576 301 LEALK----------TELEDTLDtTAAQQELRskreqEVTELKKaLEEETRSHEAQLQEMRQKHTQAL---EELTEQLE- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1345 mklQFPRPK------------DQAALQRKADSVSDRLlADTRKKTKQAERMLGN-AAPLSSSAKKKGREAEVLAKDSAKL 1411
Cdd:pfam01576 367 ---QAKRNKanlekakqalesENAELQAELRTLQQAK-QDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1412 --AKALLRERK----QAHRRASRLTSQ---TQATLQQASQQVLASEARRQELEEaERvgAGLSEMEQQIRESRISLEKDI 1482
Cdd:pfam01576 443 esVSSLLNEAEgkniKLSKDVSSLESQlqdTQELLQEETRQKLNLSTRLRQLED-ER--NSLQEQLEEEEEAKRNVERQL 519
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110611156 1483 ETLSELLARLG-SLDTHQAPAQALNET----QWALERLRLQL 1519
Cdd:pfam01576 520 STLQAQLSDMKkKLEEDAGTLEALEEGkkrlQRELEALTQQL 561
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-857 |
2.16e-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: 2.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 810 CQCSGNVDPNavGNCDPLSGHClRCLHNTTGDHCEHCQEGFYGSALAP 857
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
383-427 |
2.71e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 2.71e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110611156 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 |
4.32e-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: 4.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 383 CDCQSAGSLHLQCD-DTGTCACKPTVTGWKCDRCLPGFHSLSEGGCRPC 430
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1567 |
5.78e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1083 LEGAVKAAREQLQRLNK-----GARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLE-IPQEGPSQPTKWSH 1154
Cdd:TIGR02168 300 LEQQKQILRERLANLERqleelEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEaELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1155 LATEARALARSHRDTATKIAAT------------AWRALLASNTSyALLWNLLEGRVAlETQRDLEDRYQEVQAAQKALR 1222
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEierlearlerleDRRERLQQEIE-ELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1223 TAVAEvLPEAESVLATVQQVGADTAPYLALLASPGALPQK--SRAEDLGLKAKALEK----------------TVASWQH 1284
Cdd:TIGR02168 458 RLEEA-LEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKnqsglsgilgvlseliSVDEGYE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1285 MATEAArtLQTAAQATLRQTEPLTKLhqeARAALTQASSsvqaatvtvmGARTLLAdLEGMKLQFPRPKDQAALQRKADS 1364
Cdd:TIGR02168 537 AAIEAA--LGGRLQAVVVENLNAAKK---AIAFLKQNEL----------GRVTFLP-LDSIKGTEIQGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1365 VSdrLLADTRKKTKQAER----MLG---------NAAPLSSSAKKKGR----EAEVLAKD-----SAKLAKALLRERKQA 1422
Cdd:TIGR02168 601 LG--VAKDLVKFDPKLRKalsyLLGgvlvvddldNALELAKKLRPGYRivtlDGDLVRPGgvitgGSAKTNSSILERRRE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1423 HRRASRLTSQTQATLQQASQQVLASEARRQELEEAER-VGAGLSEMEQQIRESRISL---EKDIETLSELLARLGSLDTH 1498
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTE 758
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110611156 1499 QAPAQALNETQWALERLRLQLGSPGSLQrklslleqesqqQELQIQGFESDLAEIRADKQNLEAILHSL 1567
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEE------------LEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1073-1492 |
6.48e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1073 REAFLEQMMSLEGAVKAAREQLQRLNKgarcAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKW 1152
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1153 SHLATEARALARSHRDTATKIAATAWRALLASNTSYALlwNLLEGRVALETQRDLED---RYQEVQAAQKALRTAVAEV- 1228
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEAq 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1229 --LPEAESVLATVQQVGADTAPY---------------LALLASPGALPQKSRAED-------LGLKAKALEKTVASWQH 1284
Cdd:COG4717 220 eeLEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIagvlflvLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1285 MATEAARTLQTAAQATLRQTEpLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQF---PRPKDQAALQRK 1361
Cdd:COG4717 300 LGKEAEELQALPALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1362 ADSVSD----------RLLADTRKKTKQAERMLGNAAPlsssakkkGREAEVLAKDSAKLAKALLRERKQAHRRASRLT- 1430
Cdd:COG4717 379 AGVEDEeelraaleqaEEYQELKEELEELEEQLEELLG--------ELEELLEALDEEELEEELEELEEELEELEEELEe 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1431 -SQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLekdiETLSELLARL 1492
Cdd:COG4717 451 lREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL----ELLEEAREEY 509
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
964-1011 |
8.78e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 8.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110611156 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 |
9.22e-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: 9.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110611156 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 |
1.13e-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: 1.13e-07
10 20 30
....*....|....*....|....*....|....*....
gi 110611156 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1261-1507 |
2.92e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.60 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1261 QKSRAEDLGLKAKALEKtVASWQHMATEAARTLQTAAQ--ATLRQTEP---LTKLHQEARAALTqasssvqAATVTVMGA 1335
Cdd:NF041483 527 ERTRAEAERLRAEAEEQ-AEEVRAAAERAARELREETEraIAARQAEAaeeLTRLHTEAEERLT-------AAEEALADA 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1336 RTlladlegmklqfprpkDQAALQRKADSVSDRLLADT--RKKTKQ------AERMLGNAAPLSSSAKKKGR-------- 1399
Cdd:NF041483 599 RA----------------EAERIRREAAEETERLRTEAaeRIRTLQaqaeqeAERLRTEAAADASAARAEGEnvavrlrs 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1400 ----EAEVL---AKDSAKlakallRERKQAHRRASRLTSQTQATLQQASQqvlasEARRQELEEAERVGAGLSEMEQQIR 1472
Cdd:NF041483 663 eaaaEAERLkseAQESAD------RVRAEAAAAAERVGTEAAEALAAAQE-----EAARRRREAEETLGSARAEADQERE 731
|
250 260 270
....*....|....*....|....*....|....*.
gi 110611156 1473 ESRislekdiETLSELLARL-GSLDTHQAPAQALNE 1507
Cdd:NF041483 732 RAR-------EQSEELLASArKRVEEAQAEAQRLVE 760
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1193-1569 |
5.64e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1193 NLLEGRVAlETQRDLEdRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADtapyLALLASPGALPQKSR---AEDLG 1269
Cdd:PRK02224 209 NGLESELA-ELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELETLEAE----IEDLRETIAETEREReelAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1270 LKAKALEKTVASWQHMATEAARTlQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEG--MKL 1347
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEEraEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1348 QFPRPKDQAALQRKADSVSDR--LLADTRKKTKQAERMLGNAAplsssakkkgreaevLAKDSAKLAKALLRERKQAHRr 1425
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRreEIEELEEEIEELRERFGDAP---------------VDLGNAEDFLEELREERDELR- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1426 aSRLTSqTQATLQQASQQVlaSEARR-----------QELEEAERVgAGLSEMEQQ----------IRESRISLEKDI-- 1482
Cdd:PRK02224 426 -EREAE-LEATLRTARERV--EEAEAlleagkcpecgQPVEGSPHV-ETIEEDRERveeleaeledLEEEVEEVEERLer 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1483 -ETLSELLARLGSLDTHQAPAQAL--------NETQWALERLRLQ---LGSPGSLQRKL-SLLEQESQQQELQIQGFESD 1549
Cdd:PRK02224 501 aEDLVEAEDRIERLEERREDLEELiaerretiEEKRERAEELRERaaeLEAEAEEKREAaAEAEEEAEEAREEVAELNSK 580
|
410 420
....*....|....*....|
gi 110611156 1550 LAEIRADKQNLEAILHSLPE 1569
Cdd:PRK02224 581 LAELKERIESLERIRTLLAA 600
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
810-853 |
7.97e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.97e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110611156 810 CQCsgNVDPNAVGNCDPLSGHCLrCLHNTTGDHCEHCQEGFYGS 853
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1086-1516 |
1.00e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1086 AVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlaTEARALARS 1165
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE----------------EEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1166 HRDTATKI-AATAWRALLASNTsyallwNLLEGRVA-LETQ-RDLEDRYQEVQAAQKA---------------------L 1221
Cdd:PRK02224 400 FGDAPVDLgNAEDFLEELREER------DELREREAeLEATlRTARERVEEAEALLEAgkcpecgqpvegsphvetieeD 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1222 RTAVAEVLPEAESVLATVQQVGA--DTAPYLALLASpgalpqksRAEDLGLKAKALEKTVAswQHMATEAARTLQTAaqa 1299
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEErlERAEDLVEAED--------RIERLEERREDLEELIA--ERRETIEEKRERAE--- 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1300 TLR-QTEPLTKLHQEARAALTQASSSVQAATVTVmgartllADLEGmklqfprpkDQAALQRKADSVSD--RLLADTRKK 1376
Cdd:PRK02224 541 ELReRAAELEAEAEEKREAAAEAEEEAEEAREEV-------AELNS---------KLAELKERIESLERirTLLAAIADA 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1377 TKQAERMlgnaaplsssAKKKGREAEVLAKDSAKLAKalLRERKQahrrasrltsQTQATLQQAsqqvlASEARRQELEE 1456
Cdd:PRK02224 605 EDEIERL----------REKREALAELNDERRERLAE--KRERKR----------ELEAEFDEA-----RIEEAREDKER 657
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110611156 1457 AERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSL-DTHqapaQALNETQWALERLR 1516
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELrERR----EALENRVEALEALY 714
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1114-1520 |
1.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1114 QLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwshlatEARALARSHRDTATKIAATAWRALLASNTSYAllwn 1193
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELE-----------------AELEELRLELEELELELEEAQAEEYELLAELA---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1194 LLEGRVALETQR--DLEDRYQEVQAAQKALRTAVAevlpEAESVLATVQQVGADTAPYLALLAspgalpqkSRAEDLGLK 1271
Cdd:COG1196 299 RLEQDIARLEERrrELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAE--------AELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1272 AKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSsvqaatvtvmgARTLLADLEgmklqfpr 1351
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----------LEEELEELE-------- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1352 pKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRE--RKQAHRRASRL 1429
Cdd:COG1196 428 -EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1430 TSQTQATLQQASQ----QVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETL-SELLARLGSL-DTHQAPAQ 1503
Cdd:COG1196 507 LEGVKAALLLAGLrglaGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLpLDKIRARA 586
|
410
....*....|....*..
gi 110611156 1504 ALNETQWALERLRLQLG 1520
Cdd:COG1196 587 ALAAALARGAIGAAVDL 603
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1078-1328 |
1.81e-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: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1078 EQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEipqegpsqptkwSHLAT 1157
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR------------EELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1158 EARALARSHRDTatkiaaTAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLA 1237
Cdd:COG3883 91 RARALYRSGGSV------SYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1238 TVQQVGADTApylALLASpgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAA 1317
Cdd:COG3883 165 ELEAAKAELE---AQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|.
gi 110611156 1318 LTQASSSVQAA 1328
Cdd:COG3883 237 AAAAAAAASAA 247
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1070-1527 |
2.08e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 52.94 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1070 PGAREAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAgsqktCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQP 1149
Cdd:COG3899 721 YAEALRYLERALELLPPDPEEEYRLALLLELAEALYL-----AGRFEEAEALLERALAARALAALAALRHGNPPASARAY 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1150 TKWSHLAT----EARALARSHRDTATKIAATAWRALLASNTSYALLWN------LLEGRVALETQRDLEDRYQEVQAAQK 1219
Cdd:COG3899 796 ANLGLLLLgdyeEAYEFGELALALAERLGDRRLEARALFNLGFILHWLgplreaLELLREALEAGLETGDAALALLALAA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1220 ALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQA 1299
Cdd:COG3899 876 AAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALA 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1300 TLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQ 1379
Cdd:COG3899 956 AALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAA 1035
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1380 AERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAER 1459
Cdd:COG3899 1036 LLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALA 1115
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611156 1460 VGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1527
Cdd:COG3899 1116 LAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALL 1183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1485 |
2.28e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1199 VALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADtapyLALLASPGALPQKSRAEDLGLKAKALEKT 1278
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1279 VASWQHMATeaartLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAAL 1358
Cdd:TIGR02168 778 AEAEAEIEE-----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1359 QRKADSVS-DRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLtSQTQATL 1437
Cdd:TIGR02168 853 DIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRL 931
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1438 QQASQQVL-----ASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETL 1485
Cdd:TIGR02168 932 EGLEVRIDnlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1070-1570 |
2.51e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1070 PGAREAFLEQMMSLeGAVKAAREQLQRLNKGARCAQAGSQktcTQLADLEAVLESSEEEILHAAaiLASLEipQEGPSQP 1149
Cdd:PRK02224 148 PSDRQDMIDDLLQL-GKLEEYRERASDARLGVERVLSDQR---GSLDQLKAQIEEKEEKDLHER--LNGLE--SELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1150 TKWSHLaTEARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRD-LEDRYQEVQAAQKALRTAVAEV 1228
Cdd:PRK02224 220 EEIERY-EEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREeLAEEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1229 L-------PEAESVLATVQQVGADTAPYLALL--ASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQA 1299
Cdd:PRK02224 299 LaeaglddADAEAVEARREELEDRDEELRDRLeeCRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1300 TLRQTEPLTKLHQEARAAltqaSSSVQAATVTVMGARTLLADLEGMK--LQFPRPKDQAALQRKADSVSD--RLLA---- 1371
Cdd:PRK02224 379 VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREERdeLREREAELEATLRTARERVEEaeALLEagkc 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1372 -----------------DTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKalLRERKQAhrrASRLTSQTQ 1434
Cdd:PRK02224 455 pecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER--LEERRED---LEELIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1435 ATLQQASQQVLASEARRQELE-EAERVGAGLSEMEQQIRESRI---SLEKDIETLSELLARLGSLDTHQAPAQALNEtqw 1510
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERIRTLLAAIADAED--- 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611156 1511 ALERLRLQLGSPGSL--QRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPEN 1570
Cdd:PRK02224 607 EIERLREKREALAELndERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEK 668
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
965-1002 |
2.69e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.69e-06
10 20 30
....*....|....*....|....*....|....*....
gi 110611156 965 CRCSPLGAASAQCH-ENGTCVCRPGFEGYKCDRCHDNFF 1002
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1073-1553 |
2.92e-06 |
|
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: 52.06 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1073 REAFLEQMMSLEgavkAAREQLQRLNKGARCAQAGSQKTCTQLADLEAV---LESSEEEILHAAAILASLEIPQEGPSQP 1149
Cdd:pfam07111 86 RETSLQQKMRLE----AQAMELDALAVAEKAGQAEAEGLRAALAGAEMVrknLEEGSQRELEEIQRLHQEQLSSLTQAHE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1150 TKWSHLATEARALARSHRDTATKIAATAWRALLASNTSyallwNLLEGRVAlETQRDLEDRYQEVQAaqkaLRTAVAEVL 1229
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEA-----ELLRKQLS-KTQEELEAQVTLVES----LRKYVGEQV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1230 P----------EAESVLATVQQVGADTApylallaspgalpqksraeDLGLKAKALEKTVASWQHMateaartLQTAAQA 1299
Cdd:pfam07111 232 PpevhsqtwelERQELLDTMQHLQEDRA-------------------DLQATVELLQVRVQSLTHM-------LALQEEE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1300 TLRQTEPLTKLHQE----ARAALTQASSSVQAATVTVMGARTLLAD-LEGMKLQFPRPKDQAALQRKADSVSDRLLADTR 1374
Cdd:pfam07111 286 LTRKIQPSDSLEPEfpkkCRSLLNRWREKVFALMVQLKAQDLEHRDsVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1375 KKTkQAERMLGNAAPLSSSAKKKGREAEVLAKDSAK-----LAKALLRERKQAHRRASRLtSQTQATLQQASQQV----- 1444
Cdd:pfam07111 366 AEV-EVERMSAKGLQMELSRAQEARRRQQQQTASAEeqlkfVVNAMSSTQIWLETTMTRV-EQAVARIPSLSNRLsyavr 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1445 ------------LASEARRQEL----EEAERVGAGLSEMEQQIRESRISLEKDIETLSELLA-------------RLGSL 1495
Cdd:pfam07111 444 kvhtikglmarkVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQqevgrareqgeaeRQQLS 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611156 1496 DTHQAPAQALNETQWALERLRLQL-----GSPGSLQRKLSLLEQESQQQELQIQGFESDLAEI 1553
Cdd:pfam07111 524 EVAQQLEQELQRAQESLASVGQQLevarqGQQESTEEAASLRQELTQQQEIYGQALQEKVAEV 586
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1476 |
3.40e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1254 ASPGALPQKSRAEDLGLKAKAL-EKTVAS---------------WQHMATEAARTLQTAAQATLRQtepltklHQEARA- 1316
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaERTVSEaiaeaerlrsdaseyAQRVRTEASDTLASAEQDAART-------RADAREd 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1317 -------ALTQASSSVQAATVTvmgARTLLADLEGMKLQFPRPKDQAALQRKADSV--SDRLLADTrkkTKQAERMLGNA 1387
Cdd:NF041483 904 anrirsdAAAQADRLIGEATSE---AERLTAEARAEAERLRDEARAEAERVRADAAaqAEQLIAEA---TGEAERLRAEA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1388 APLSSSAKKKGR----EAEVLAKDSAKLAKALLRE------------RKQAHRRASRLTSQ--TQATLQQASQQVLASEA 1449
Cdd:NF041483 978 AETVGSAQQHAErirtEAERVKAEAAAEAERLRTEareeadrtldeaRKDANKRRSEAAEQadTLITEAAAEADQLTAKA 1057
|
250 260 270
....*....|....*....|....*....|....*
gi 110611156 1450 RRQELE---EAER-----VGAGLSEMEQQIRESRI 1476
Cdd:NF041483 1058 QEEALRtttEAEAqadtmVGAARKEAERIVAEATV 1092
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1564 |
6.55e-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: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1078 EQMMSLEGAVKAAREQLQRLNkgARCAQAGSQKTCTQ--LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHL 1155
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLN--NEIERLEARLERLEdrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1156 ATEARALARshrdtATKIAATAWRALLASNTSYALLWNLLEGRVALetQRDLEDRYQEVQAAQKA--------------- 1220
Cdd:TIGR02168 457 ERLEEALEE-----LREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLKNqsglsgilgvlseli 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1221 -----LRTAVAEVLPE---------AESVLATVQ---QVGADTAPYLALLASPGALPQKSRAE-------------DLGL 1270
Cdd:TIGR02168 530 svdegYEAAIEAALGGrlqavvvenLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREilkniegflgvakDLVK 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1271 KAKALEKTVASW-------------QHMA-----------------------------TEAARTLQTAAQATLRQT-EPL 1307
Cdd:TIGR02168 610 FDPKLRKALSYLlggvlvvddldnaLELAkklrpgyrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKiEEL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1308 TKLHQEARAALTQASSSVQAATVTVMGARTLLADLE----GMKLQFPR-PKDQAALQRKADSVSDRLLADTRKKTKQAER 1382
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1383 MLGNAAPLSSSAKKKGREAEVL--AKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEE-AER 1459
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqIEE 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1460 VGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDthqapaQALNETQWALERLRLQLGSpgsLQRKLSLLEQESQQQ 1539
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLE------EALALLRSELEELSEELRE---LESKRSELRRELEEL 920
|
570 580
....*....|....*....|....*
gi 110611156 1540 ELQIQGFESDLAEIRADKQNLEAIL 1564
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1489 |
6.66e-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: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1083 LEGAVKAAREQLQRLNKGARCAQagsqktctQLADLEAvlessEEEILHAAAILASLEipqegpSQPTKWSHLATEARAL 1162
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAE--------RYKELKA-----ELRELELALLVLRLE------ELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1163 ARSHRDTATKIAAtawrallasntsYALLWNLLEGRValetqRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQV 1242
Cdd:TIGR02168 252 EEELEELTAELQE------------LEEKLEELRLEV-----SELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1243 GADTAPYLALLASpgalpQKSRAEDLGLKAKALEKTVASWQ---HMATEAARTLQTAAQATLRQTEPLTKLHQEARAALT 1319
Cdd:TIGR02168 315 ERQLEELEAQLEE-----LESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1320 QASSSVQAATVTVMGARTLLADLEGMKlqfprpkdqaalqrkadsvsDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGR 1399
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRR--------------------ERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1400 EAEVLAKDSAKLAKALLRERKQAHRRASRltsQTQATLQQASQQVLASEARRQELEeaervgaGLSEMEQQIRESRISLE 1479
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALD---AAERELAQLQARLDSLERLQENLE-------GFSEGVKALLKNQSGLS 519
|
410
....*....|
gi 110611156 1480 KDIETLSELL 1489
Cdd:TIGR02168 520 GILGVLSELI 529
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1309-1524 |
6.83e-06 |
|
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: 50.80 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1309 KLHQEARAA--LTQASSSVQAAtvtVMGARTllaDLEGMKLQFPRPKDQA-ALQRKADSVSDRL------LADTRkktkQ 1379
Cdd:pfam05701 273 KLKEEADGEgnEKKTSTSIQAA---LASAKK---ELEEVKANIEKAKDEVnCLRVAAASLRSELekekaeLASLR----Q 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1380 AERMlgnaaplsSSAKKKGREAEvLAKDSAKLAKALLRErKQAHRRASRLTSQTQATLQQASQQVLASEARRQEL----E 1455
Cdd:pfam05701 343 REGM--------ASIAVSSLEAE-LNRTKSEIALVQAKE-KEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELrkakE 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110611156 1456 EAERVGAGLSEMEQQIRESRisleKDIE--TLSELLARlgsldthqAPAQALNETQWAlERLRLQLGSPGS 1524
Cdd:pfam05701 413 EAEQAKAAASTVESRLEAVL----KEIEaaKASEKLAL--------AAIKALQESESS-AESTNQEDSPRG 470
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-312 |
7.29e-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: 7.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 110611156 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFFQDRP 312
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1078-1492 |
9.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1078 EQMMSLEGAVKAAREQLQRLNkgARCAQAGSQktctQLADLE---AVLESSEEEILHAAAILASL--EIPQEGPSQPTKW 1152
Cdd:COG4913 309 AELERLEARLDALREELDELE--AQIRGNGGD----RLEQLEreiERLERELEERERRRARLEALlaALGLPLPASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1153 SHLATEARALARSHRDTATKIAATAWRALLAsntsyalLWNLLEGRVALETQRD-LEDR---Y-QEVQAAQKALRTA--- 1224
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAA-------LRDLRRELRELEAEIAsLERRksnIpARLLALRDALAEAlgl 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1225 -------VAE---VLPE-------AESVLAT-----------------------------VQQVGADTAPYLALLASPGA 1258
Cdd:COG4913 456 deaelpfVGElieVRPEeerwrgaIERVLGGfaltllvppehyaaalrwvnrlhlrgrlvYERVRTGLPDPERPRLDPDS 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1259 LPQKsraedlgLKAKA------LEKTVAS-WQHMATEAARTLQTAAQA-------------------------------T 1300
Cdd:COG4913 536 LAGK-------LDFKPhpfrawLEAELGRrFDYVCVDSPEELRRHPRAitragqvkgngtrhekddrrrirsryvlgfdN 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1301 LRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRL--LADTRKKTK 1378
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerLDASSDDLA 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1379 QAERMLgnaaplsSSAKKKGREAEvlakdsAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEaE 1458
Cdd:COG4913 689 ALEEQL-------EELEAELEELE------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-R 754
|
490 500 510
....*....|....*....|....*....|....
gi 110611156 1459 RVGAGLSEMEQQIREsriSLEKDIETLSELLARL 1492
Cdd:COG4913 755 FAAALGDAVERELRE---NLEERIDALRARLNRA 785
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1399-1573 |
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 110611156 1399 REAEVLAKDSAKLAKALLrERKQAHRRASRLTSQtqatLQQASQQVlasEARRQELEEAERvgaGLSEMEQQIRESRISL 1478
Cdd:COG4372 21 KTGILIAALSEQLRKALF-ELDKLQEELEQLREE----LEQAREEL---EQLEEELEQARS---ELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1479 EKDIETLSELLARLGSLDTHQAPAQA-LNETQWALERLRLQLgspGSLQRKLSLLEQESQQQELQIQGFESDLAEIRADK 1557
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEeLEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170
....*....|....*.
gi 110611156 1558 QNLEAILHSLPENCAS 1573
Cdd:COG4372 167 AALEQELQALSEAEAE 182
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1515 |
2.39e-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: 48.61 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1250 LALLASPGALPQKSRAEDLGLKAKALEKTVAswqhmateaartlqtAAQATLRQTEpltKLHQEARAALTQASSSVQAAT 1329
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIA---------------ELEKELAALK---KEEKALLKQLAALERRIAALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1330 VTVMGARTLLADLEgmklqfprpKDQAALQRKADSVSDRLladtRKKTKQAERMLGNAAPLSssakKKGREAEVLAKDSA 1409
Cdd:COG4942 69 RRIRALEQELAALE---------AELAELEKEIAELRAEL----EAQKEELAELLRALYRLG----RQPPLALLLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1410 KlakallrerkQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELL 1489
Cdd:COG4942 132 L----------DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
250 260
....*....|....*....|....*..
gi 110611156 1490 ARL-GSLDTHQAPAQALNETQWALERL 1515
Cdd:COG4942 202 ARLeKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1283-1495 |
2.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1283 QHMAT-EAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQ-AATVTVMGARTLLADLEgmklqfprpKDQAALQR 1360
Cdd:COG4913 232 EHFDDlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLE---------AELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1361 KADSVSDRL--LADTRKKTKQAERMLGNAAplsssAKKKGREAEVLAKDSAKLAKALlRERKQAHRRASRLTSQTQATLQ 1438
Cdd:COG4913 303 ELARLEAELerLEARLDALREELDELEAQI-----RGNGGDRLEQLEREIERLEREL-EERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110611156 1439 qASQQVLAsEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSL 1495
Cdd:COG4913 377 -ASAEEFA-ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-383 |
4.90e-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: 4.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 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 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1073 REAFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLADLEAVLESSEEEI---LHAAAILASLEIPQE--GPS 1147
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRALYRLGRQPPLALllSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1148 QPTKWSHLATEARALARSHRDTATKIAATawRALLASNtsyallwnllegRVALETQRD-LEDRYQEVQAAQKALRTAVA 1226
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAAL------------RAELEAERAeLEALLAELEEERAALEALKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611156 1227 evlpEAESVLATVQQVGADtapylallaspgalpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLR 1302
Cdd:COG4942 196 ----ERQKLLARLEKELAE---------------LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1225-1476 |
5.81e-05 |
|
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: 47.15 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1225 VAEVLPEAESVLATVQQVGADT------APYLALLASPGALPQKSRAEDLGLKAKALEKTVASwqhmatEAARTLQT--- 1295
Cdd:TIGR02794 24 YHSVKPEPGGGAEIIQAVLVDPgavaqqANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA------EQARQKELeqr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1296 -AAQATLRQTEP-----LTKLHQEARAALTQASSSVQAATVTvmGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRL 1369
Cdd:TIGR02794 98 aAAEKAAKQAEQaakqaEEKQKQAEEAKAKQAAEAKAKAEAE--AERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1370 LADTRKKT---KQAERmlGNAAPLSSSAKKKgreAEVLAKDSAKLAKAlLRERKQAHRRASRLTSQTQATLQQASQQVLA 1446
Cdd:TIGR02794 176 EAEAKAKAeaeAKAKA--EEAKAKAEAAKAK---AAAEAAAKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
250 260 270
....*....|....*....|....*....|
gi 110611156 1447 SEARRQELEEAERVGAGlseMEQQIRESRI 1476
Cdd:TIGR02794 250 GGARGAAAGSEVDKYAA---IIQQAIQQNL 276
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1392-1492 |
7.36e-05 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 44.22 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1392 SSAKKKGREAEvlakdsaKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLA---SEARRQeLEEAERvgaglsEME 1468
Cdd:PRK07353 46 AEAKERLAEAE-------KLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAeaqAEAQAS-KEKARR------EIE 111
|
90 100
....*....|....*....|....*
gi 110611156 1469 QQIRESRISLEKDIETLSEL-LARL 1492
Cdd:PRK07353 112 QQKQAALAQLEQQVDALSRQiLEKL 136
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1265-1512 |
8.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1265 AEDLGLKAKALEKTVASWQHMATEAARTLQTAAQA--TLRQTEPLTKLHQEARAA---LTQASSSVQAATVTVMGARTLL 1339
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAAleEFRQKNGLVDLSEEAKLLlqqLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1340 ADLEGmklqfprpKDQAALQRKADSVSDRLLADTRKKTKQAERmlgnaaplsssakkkgREAEVLAKDSAK--LAKALLR 1417
Cdd:COG3206 243 AALRA--------QLGSGPDALPELLQSPVIQQLRAQLAELEA----------------ELAELSARYTPNhpDVIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1418 ERKQAHRRasrLTSQTQATLQQASQQVLASEARRQEL----EEAERVGAGLSEMEQQIREsrisLEKDIETLSE----LL 1489
Cdd:COG3206 299 QIAALRAQ---LQQEAQRILASLEAELEALQAREASLqaqlAQLEARLAELPELEAELRR----LEREVEVARElyesLL 371
|
250 260
....*....|....*....|...
gi 110611156 1490 ARLGSLDThqapAQALNETQWAL 1512
Cdd:COG3206 372 QRLEEARL----AEALTVGNVRV 390
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1392-1490 |
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 110611156 1392 SSAKKKGREAEVLAKDsaklAKALLrerKQAHRRASRLTSQTQAtlqQASQQVlaSEARRQELEEAER-VGAGLSEMEQQ 1470
Cdd:PRK05759 45 AAAERAKKELELAQAK----YEAQL---AEARAEAAEIIEQAKK---RAAQII--EEAKAEAEAEAARiKAQAQAEIEQE 112
|
90 100
....*....|....*....|
gi 110611156 1471 IRESRISLEKDIETLSELLA 1490
Cdd:PRK05759 113 RKRAREELRKQVADLAVAGA 132
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1157-1575 |
1.37e-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: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1157 TEARALARSHRDTATKIAAtaWRALLASNTSYA--LLWNLLEGRvaletQRDLEDRYQEVQAAQKALRTAVAEVLPEAES 1234
Cdd:COG4913 255 EPIRELAERYAAARERLAE--LEYLRAALRLWFaqRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1235 VLATVQQVGADtapylallaspgalpqksRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEA 1314
Cdd:COG4913 328 LEAQIRGNGGD------------------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1315 RAALTQASSSVQAATVTVMGARTLLADLEGMK--LQfprpKDQAALQRKADSVSDRLLAdTRKKTKQA------------ 1380
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELreLE----AEIASLERRKSNIPARLLA-LRDALAEAlgldeaelpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1381 ----------------ERMLGNAApLS---------------SSAKKKGR-------------EAEVLAKDS--AKL--- 1411
Cdd:COG4913 465 elievrpeeerwrgaiERVLGGFA-LTllvppehyaaalrwvNRLHLRGRlvyervrtglpdpERPRLDPDSlaGKLdfk 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1412 -------AKALLRERK-----------QAHRRA---SRLTSQTQATLQ------QASQQVLASEARRQ------ELEEAE 1458
Cdd:COG4913 544 phpfrawLEAELGRRFdyvcvdspeelRRHPRAitrAGQVKGNGTRHEkddrrrIRSRYVLGFDNRAKlaaleaELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1459 RVgagLSEMEQQIREsrisLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERL-----RLQLGSPG---------S 1524
Cdd:COG4913 624 EE---LAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELeaeleRLDASSDDlaaleeqleE 696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 110611156 1525 LQRKLSLLEQESQQQELQIQGFESDLAEIRADKQNLEAILHSLPENCASWQ 1575
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1194-1486 |
1.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1194 LLEGRVALETQRDLEDRYQEVQAAQKA-LRTAVAEVLpEAESVLATVQQvGADTAPYLALlaspgalpQKSRAEDLGLKA 1272
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEArAEAAEEEVD-ELKSQLADYQQ-ALDVQQTRAI--------QYQQAVQALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1273 KAL----EKTVASWQHMATEAARTLQTAAQAtLRQTEPLTKLHQEARAALTQASSSVQAATVTV------MGARTLLAD- 1341
Cdd:PRK04863 427 KQLcglpDLTADNAEDWLEEFQAKEQEATEE-LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRl 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1342 ---------LEGMKLQFPRPKDQAALQRKADsvsdRLLADTRKktkQAERMLGNAAPLSSSAKKKGREAEVL---AKDSA 1409
Cdd:PRK04863 506 reqrhlaeqLQQLRMRLSELEQRLRQQQRAE----RLLAEFCK---RLGKNLDDEDELEQLQEELEARLESLsesVSEAR 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1410 KLAKALLRERKQAHRRASRLTSQT------QATLQQASQQVLASEARRQELEE-----AERVGAgLSEMEQQIRESRISL 1478
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARApawlaaQDALARLREQSGEEFEDSQDVTEymqqlLERERE-LTVERDELAARKQAL 657
|
....*...
gi 110611156 1479 EKDIETLS 1486
Cdd:PRK04863 658 DEEIERLS 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1068-1399 |
1.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1068 LLPGAREAFLEQMMSLEGAVKAAREQLQRLNKGArcaqagsQKTCTQLADLEAVLESSEEEIlhaaailasleipqegps 1147
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALERRI------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1148 qptkwshlateaRALARSHRDTATKIAAtawrallasntsyallwnlLEGRVAletqrDLEDRYQEVQAAQKALRTAVAE 1227
Cdd:COG4942 65 ------------AALARRIRALEQELAA-------------------LEAELA-----ELEKEIAELRAELEAQKEELAE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1228 VLPEAesvlatvQQVGAdtAPYLALLASPGALPQKSR-AEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEP 1306
Cdd:COG4942 109 LLRAL-------YRLGR--QPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1307 LTKLhQEARAALTQASSSVQAatvtvmgartLLADLEGMKlqfprPKDQAALQRKADSVSDrlLADTRKKTKQAERMLGN 1386
Cdd:COG4942 180 LAEL-EEERAALEALKAERQK----------LLARLEKEL-----AELAAELAELQQEAEE--LEALIARLEAEAAAAAE 241
|
330
....*....|...
gi 110611156 1387 AAPLSSSAKKKGR 1399
Cdd:COG4942 242 RTPAAGFAALKGK 254
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
754-802 |
2.35e-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: 2.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110611156 754 PCPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPLGLFG 802
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1089-1493 |
2.37e-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: 46.12 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1089 AAREQLQRLNKGARCAQAGSQKT---CTQLADLEAVLESSEE---EILHAAAILASLEIPQEGpsqptKWSHLATEARAL 1162
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLkerEQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCG-----SCIHPNPARQDI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1163 ARSHRDTA--TKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDryQEVQA-AQKalRTAVAEVLPeaesvlaTV 1239
Cdd:TIGR00618 521 DNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ--QSFSIlTQC--DNRSKEDIP-------NL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1240 QQVGADTAPYLallaspgalPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQatlRQTEPLTKLHQEArAALT 1319
Cdd:TIGR00618 590 QNITVRLQDLT---------EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQ-LTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1320 QASSSVQAATVTVMGARTLLA-DLEGMKLQfpRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKG 1398
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASrQLALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1399 REAEVLAKDSAKLAKALLRERKQAHRRASrltsqtqatlQQASQQVLASEARRQELEEAERvgaglsEMEQQIREsrisL 1478
Cdd:TIGR00618 735 AAREDALNQSLKELMHQARTVLKARTEAH----------FNNNEEVTAALQTGAELSHLAA------EIQFFNRL----R 794
|
410
....*....|....*
gi 110611156 1479 EKDIETLSELLARLG 1493
Cdd:TIGR00618 795 EEDTHLLKTLEAEIG 809
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1368-1522 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1368 RLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS 1447
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110611156 1448 EARRQELEEAERVGAGLSEMEQQIRESRIS-LEKDIETLSELLaRLGSLDTHQAPAQA-LNETQWALERLRLQLGSP 1522
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEI-RSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSP 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1156-1502 |
4.03e-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: 45.06 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1156 ATEARALARSHRDTATKIAATAWRALLASNTSyallwnlLEGRVA-LE-----TQRDLEDRYQEVQAAQKALRTAVAEVL 1229
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALERQKEA-------IERQLAsLEeelekLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1230 PEAESVLATVQQVGADTAPYLALLASPGALpQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAqatlRQTEPLTK 1309
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER----KRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1310 LHQEARAALTQASSSVQAATVTVMGARTLLADLEgmklqfprpKDQAALQRKADSV---SDRLLADTRKKTKQAERMlgn 1386
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYR---------EKLEKLKREINELkreLDRLQEELQRLSEELADL--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1387 aaplssSAKKKGREAEVLAKDSAKLAKALlrERKQAHRRASrltsQTQATLQQASQQVLASEAR-----------RQELE 1455
Cdd:TIGR02169 426 ------NAAIAGIEAKINELEEEKEDKAL--EIKKQEWKLE----QLAADLSKYEQELYDLKEEydrvekelsklQRELA 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110611156 1456 EAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPA 1502
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-377 |
4.46e-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: 4.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 110611156 326 PCNCSGR---SEECTFdrelfrstgHGGRCHhCRDHTAGPHCERCQENFYHWDPR 377
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1286-1514 |
5.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1286 ATEAARTLQTAAQATLRQTEPLTKLhQEARAALTQASSSVQAATVTVMGARTLLADLEgmklqfprpKDQAALQRKADSV 1365
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKEL-SELQAELEAAQAELDALQAELEELNEEYNELQ---------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1366 SDRLlADTRKKTKQAERMLGNAAplsSSAKKKGREA---EVLAkDSAKLAKALlrerkqahRRA---SRLTSQTQATLQQ 1439
Cdd:COG3883 71 QAEI-AEAEAEIEERREELGERA---RALYRSGGSVsylDVLL-GSESFSDFL--------DRLsalSKIADADADLLEE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611156 1440 ASQQVLASEARRQELEEAErvgAGLSEMEQQIRESRISLEKDIETLSELLARLGS-LDTHQAPAQALNETQWALER 1514
Cdd:COG3883 138 LKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQEALLAQLSAeEAAAEAQLAELEAELAAAEA 210
|
|
| TNFRSF6B |
cd10575 |
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ... |
684-777 |
5.77e-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: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 684 CEsCAPGYKREMPqggpyascvpcTCNQHGTCDPNTGICVCSHHTEGPSCERCLPGFYgNPFAGQADDCQP-CPCPGQSA 762
Cdd:cd10575 80 CE-CKPGYYMEHG-----------FCLRHSSCPPGEGVIKLGTPYSDTQCEPCPPGFF-SASSSSTEPCQPhTNCTQGGL 146
|
90
....*....|....*..
gi 110611156 763 CTTIP--ESREVVCTHC 777
Cdd:cd10575 147 ETNVPgnDYHDTLCTSC 163
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1202-1528 |
6.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1202 ETQRDLEDRYQEVQAAQKALRtavaevlpEAESVLATVQQvgadtapylallaspgalpqksraedlglKAKALEKTVAS 1281
Cdd:COG4372 63 QLEEELEQARSELEQLEEELE--------ELNEQLQAAQA-----------------------------ELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1282 wqhmATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGmKLQFPRPKDQAALQRK 1361
Cdd:COG4372 106 ----LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-ELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1362 ADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRR-ASRLTSQTQATLQQA 1440
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELeEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1441 SQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLG 1520
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
....*...
gi 110611156 1521 SPGSLQRK 1528
Cdd:COG4372 341 DLLQLLLV 348
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1287-1528 |
8.33e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1287 TEAARTLQTAAQATLRQTEPLTKLHQEARAaltQASSSVQAATVTVMG--------ARTLLADLE--GMKLQFPRPKDQA 1356
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQ---KAKEEAEEERLAELEakrqaeeeAREAKAEAEqrAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1357 ALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQAT 1436
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1437 LQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQALNETQWALERLR 1516
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250
....*....|..
gi 110611156 1517 LQLGSPGSLQRK 1528
Cdd:COG3064 241 EEAALGGAEEAA 252
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1312-1456 |
1.14e-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: 42.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1312 QEARAALTQASSSVQAATVTVMGARTLLADLEGMKlqfprpKDQAALQRKADSVSDRLLADTRKKtKQAERMLGNAAPLs 1391
Cdd:pfam00529 61 DSAEAQLAKAQAQVARLQAELDRLQALESELAISR------QDYDGATAQLRAAQAAVKAAQAQL-AQAQIDLARRRVL- 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611156 1392 ssAKKKG--REAEVLAKDSAKLAKALLRERKQAHRRASR-LTSQTQATLQQASQQVLASEARRQELEE 1456
Cdd:pfam00529 133 --APIGGisRESLVTAGALVAQAQANLLATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1198-1514 |
1.47e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1198 RVALETQR-DLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTApylALLASPGALPQKSR--AEDL-GLKAK 1273
Cdd:pfam07888 68 REQWERQRrELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRelEEDIkTLTQR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1274 ALEKTV-----------ASWQHMATEAAR-TLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVmgarTLLAD 1341
Cdd:pfam07888 145 VLERETelermkerakkAGAQRKEEEAERkQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI----TTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1342 LEGMKLQfpRPKDQAALQRKADSVSDRLLADTRKKTkqaerMLGnaAPLSSSAKKKGR-EAEV------LAKDSAKLAKA 1414
Cdd:pfam07888 221 KLTTAHR--KEAENEALLEELRSLQERLNASERKVE-----GLG--EELSSMAAQRDRtQAELhqarlqAAQLTLQLADA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1415 LLRERK-QAHRRASRLTSQTQAT-----LQQASQQVLASEARRQElEEAERVGAGLsEMEQQIRESRISLEKDIETLSEL 1488
Cdd:pfam07888 292 SLALREgRARWAQERETLQQSAEadkdrIEKLSAELQRLEERLQE-ERMEREKLEV-ELGREKDCNRVQLSESRRELQEL 369
|
330 340 350
....*....|....*....|....*....|
gi 110611156 1489 LARLGSL----DTHQAPAQALNETQWALER 1514
Cdd:pfam07888 370 KASLRVAqkekEQLQAEKQELLEYIRQLEQ 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1562 |
1.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1383 MLGNAAPLSSSAKKKGREAEvLAKDSAKLaKALLRERKQAHRRASRLTSQtqatLQQASQQVLASEARRQELE-EAERVG 1461
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAE-LEQLQQEI-AELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEqELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1462 AGLSEMEQQIREsrisLEKDIETLSELLARlgsldthQAPAQALNETQWALERLrLQLGSPGSLQRKLSLLEQESQQQEL 1541
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAE-------LLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180
....*....|....*....|.
gi 110611156 1542 QIQGFESDLAEIRADKQNLEA 1562
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 ... |
1399-1483 |
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 110611156 1399 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAS---EARRQELEEAERVGAGLSEMEQQIRE-- 1473
Cdd:pfam00430 40 AEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAaeaEAERIIEQAAAEIEQEKDRALAELRQqv 119
|
90
....*....|...
gi 110611156 1474 ---SRISLEKDIE 1483
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 ... |
1391-1518 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1391 SSSAKKKGREAEVLAKDSAKlaKALLRERKQAHRRASRLTSQT-----------------QATLQQASQQVLASEARRQE 1453
Cdd:pfam01576 128 TTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSNLaeeeekakslsklknkhEAMISDLEERLKKEEKGRQE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1454 LEEAERVGAG--------LSEMEQQIRESRISLEKDIETLSELLARLGSLDTHQAPAQA--------LNETQWALERLRL 1517
Cdd:pfam01576 206 LEKAKRKLEGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaqISELQEDLESERA 285
|
.
gi 110611156 1518 Q 1518
Cdd:pfam01576 286 A 286
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1519 |
2.01e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1053 LLGEAPRGDVYQ-GHHLLPGARE--AFLEQMMSLEGAVKAAREQLQRLNKGARCAQAGSQKTCTQLA---DLEAVLESSE 1126
Cdd:COG3096 484 IAGEVERSQAWQtARELLRRYRSqqALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1127 EEILHAAAILASleipqegpsqptkwshlATEARALARSHRD-TATKIA-----ATAWRAL------LASNTSYAL---- 1190
Cdd:COG3096 564 AQLEELEEQAAE-----------------AVEQRSELRQQLEqLRARIKelaarAPAWLAAqdalerLREQSGEALadsq 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1191 -----LWNLLEGRVALETQRDledryqEVQAAQKALRTAVAEVL----PEAESVLATVQQVGA------------DTAPY 1249
Cdd:COG3096 627 evtaaMQQLLEREREATVERD------ELAARKQALESQIERLSqpggAEDPRLLALAERLGGvllseiyddvtlEDAPY 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1250 LALLASPGA----LPQKSRA-----------EDLGL-------------KAKALEKTV---------------------- 1279
Cdd:COG3096 701 FSALYGPARhaivVPDLSAVkeqlagledcpEDLYLiegdpdsfddsvfDAEELEDAVvvklsdrqwrysrfpevplfgr 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1280 -ASWQHMAT---EAARTLQTAAQATLRQTEpLTKLHQ-------------------EARAALTQASSSVQAAtvtvmgar 1336
Cdd:COG3096 781 aAREKRLEElraERDELAEQYAKASFDVQK-LQRLHQafsqfvgghlavafapdpeAELAALRQRRSELERE-------- 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1337 tlLADLEGMKLQFPRPKDQA-----ALQRKADSVSdrLLADT--RKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKdsa 1409
Cdd:COG3096 852 --LAQHRAQEQQLRQQLDQLkeqlqLLNKLLPQAN--LLADEtlADRLEELREELDAAQEAQAFIQQHGKALAQLEP--- 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1410 kLAkALLRERKQAHRRASRLTSQTQATLQQASQQVLASE---ARRQEL--EEAERVGAGLSEM-----------EQQIRE 1473
Cdd:COG3096 925 -LV-AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevvQRRPHFsyEDAVGLLGENSDLneklrarleqaEEARRE 1002
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 110611156 1474 SRISLEKDIETLSELLARLGSLDT-HQAPAQALNETQWALERLRLQL 1519
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKSsRDAKQQTLQELEQELEELGVQA 1049
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1193-1493 |
2.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1193 NLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVlpeaeSVLATVQQVGADtapYLALLASPGALpqksRAEDLGLKA 1272
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI-----ELLEPIRELAER---YAAARERLAEL----EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1273 KALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVqaatvtvmGARtlLADLEgmklqfprp 1352
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------GDR--LEQLE--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1353 KDQAALQRKADSVSDRlladtRKKTKQAERMLGNAAPLSssakkkgreaevlakdsaklAKALLRERKQAHRRASRLTSQ 1432
Cdd:COG4913 345 REIERLERELEERERR-----RARLEALLAALGLPLPAS--------------------AEEFAALRAEAAALLEALEEE 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110611156 1433 T---QATLQQASQQVLASEARRQELeEAErvgagLSEMEQqiRESRISlEKDIETLSELLARLG 1493
Cdd:COG4913 400 LealEEALAEAEAALRDLRRELREL-EAE-----IASLER--RKSNIP-ARLLALRDALAEALG 454
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1399-1491 |
2.95e-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: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1399 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAERVGA-GLSEMEQQIRESRIS 1477
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-EAK----EEAERILEqAKAEIEQEKEKALAE 114
|
90
....*....|....
gi 110611156 1478 LEKDIETLSELLAR 1491
Cdd:cd06503 115 LRKEVADLAVEAAE 128
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1401-1524 |
3.03e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1401 AEVLAKdsaklAKALLRERKQAHRRASRLTSQTQATLQQASQQvLASEA--RRQELEEAervgagLSEMEQQIRESRISL 1478
Cdd:COG1842 47 AQVIAN-----QKRLERQLEELEAEAEKWEEKARLALEKGRED-LAREAleRKAELEAQ------AEALEAQLAQLEEQV 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 110611156 1479 EKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGS 1524
Cdd:COG1842 115 EKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1159-1527 |
3.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.31 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1159 ARALARSHRDTATKIAATAWRALLASNTSYALLWNLLEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLAT 1238
Cdd:COG3903 569 ERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAA 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1239 VQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAAL 1318
Cdd:COG3903 649 AAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALL 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1319 TQASSSVQAATVTVmGARTLLADLEGMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAkkkG 1398
Cdd:COG3903 729 AAAAAAALAAAAAA-AALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAA---A 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1399 REAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEAERVGAGLSEMEQQIRESRISL 1478
Cdd:COG3903 805 AAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAAL 884
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 110611156 1479 EKDIETLSELLARLGSLDTHQAPAQALNETQWALERLRLQLGSPGSLQR 1527
Cdd:COG3903 885 LAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
755-807 |
3.09e-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: 3.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 110611156 755 CPCPGQSACTTIPESREVVCtHCPPGQRGRRCEVCDDGFFGDPlglFGHPQPC 807
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-308 |
3.63e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|....*...
gi 110611156 271 CKCNGHASECGPDVAGQLACRCQHNTTGTDCERCLPFF 308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1203-1419 |
3.77e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 41.54 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1203 TQRDLEDRYQEVQAAQKALR-------------TAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLG 1269
Cdd:COG0515 247 LAKDPEERYQSAAELAAALRavlrslaaaaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1270 LKAKALEKTVASWQHMATEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATVTVMGARTLLADLEGMKLQF 1349
Cdd:COG0515 327 AAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1350 PRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLGNAAPLSSSAKKKGREAEVLAKDSAKLAKALLRER 1419
Cdd:COG0515 407 AAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAA 476
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
348-376 |
4.13e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 4.13e-03
10 20
....*....|....*....|....*....
gi 110611156 348 HGGRCHhCRDHTAGPHCERCQENFYHWDP 376
Cdd:smart00180 16 DTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1261-1509 |
4.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1261 QKSRAEDLGLKAKALEKTVASwqhmaTEAARTLQTAAQATLRQTEPLTKLHQEARAALTQASSSVQAATvtvmgartlla 1340
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAAL-----SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1341 dlegmklqfprpKDQAALQRKADSVSDRLLADTRKKTKQAERMlgnaaplsssaKKKGREAEVLAKDSAKLAKallrERK 1420
Cdd:COG4372 73 ------------SELEQLEEELEELNEQLQAAQAELAQAQEEL-----------ESLQEEAEELQEELEELQK----ERQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1421 QAHRRASRLTSQtQATLQQASQQvlaseaRRQELEEAERvgaGLSEMEQQIRESRISLEK-DIETLSELLARLGSLDTHQ 1499
Cdd:COG4372 126 DLEQQRKQLEAQ-IAELQSEIAE------REEELKELEE---QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRN 195
|
250
....*....|
gi 110611156 1500 APAQALNETQ 1509
Cdd:COG4372 196 AEKEEELAEA 205
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
1415-1492 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1415 LLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEEA--ERVGAGLSEMEQQIRESRIS-LEKDIETLSELLAR 1491
Cdd:TIGR02473 7 LLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQalEKVGAGTSALELSNYQRFIRqLDQRIQQQQQELAL 86
|
.
gi 110611156 1492 L 1492
Cdd:TIGR02473 87 L 87
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1216-1485 |
4.87e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1216 AAQKALRTaVAEVLPEAESVLAtvqqvgADTAPYLALLASPGALPQKSRAEDLGLKAKALEKTVASWQHMATEAARTLQT 1295
Cdd:NF041483 911 AAAQADRL-IGEATSEAERLTA------EARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1296 AAQATLRQTEPLTKLHQEARAALTQASSSVQA-ATVTVMGAR---------------TLLADLEGMKLQFPRPKDQAALQ 1359
Cdd:NF041483 984 AQQHAERIRTEAERVKAEAAAEAERLRTEAREeADRTLDEARkdankrrseaaeqadTLITEAAAEADQLTAKAQEEALR 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1360 --RKADSVSDRLLADTRkktKQAERMLGNAAPLSSSAKKKGR-EAEVLAKDSAKLAKAL------LRER-----KQAHRR 1425
Cdd:NF041483 1064 ttTEAEAQADTMVGAAR---KEAERIVAEATVEGNSLVEKARtDADELLVGARRDATAIreraeeLRDRitgeiEELHER 1140
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611156 1426 ASRLTSQTQAT--------LQQASQQVLASEARRQELeeaervgagLSEMEQQIRESRISLEKDIETL 1485
Cdd:NF041483 1141 ARRESAEQMKSagercdalVKAAEEQLAEAEAKAKEL---------VSDANSEASKVRIAAVKKAEGL 1199
|
|
| TNFRSF5 |
cd13407 |
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 ... |
681-756 |
5.49e-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: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 681 GQFCESCAPGYKREMP-QGGPYASCVPCT-------------CNQHGTCDPNTG-------------ICVC--SHHTEGP 731
Cdd:cd13407 10 GRCCSLCPPGQKLVSDcTEATDTECLPCEegefqdtwnrerhCHQHRYCDPNLGlrvqtegtaetdtTCTCqeGQHCTSE 89
|
90 100 110
....*....|....*....|....*....|...
gi 110611156 732 SCERCL------PGFYGNPFAGQADD--CQPCP 756
Cdd:cd13407 90 ACETCAlhtsckPGFGVKQIATGVSDtiCEPCP 122
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1072-1516 |
6.96e-03 |
|
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: 41.11 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1072 AREAFlEQMMSLEGAVKAAREQLQRLNKgarCAQAGSQKTCTQLADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTK 1151
Cdd:TIGR00618 182 ALMEF-AKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1152 WSHLATEARALARSHRdtaTKIAATAwrallasntsyallwnllEGRVALETQRDLEdRYQEVQAAqkalrtaVAEVLPE 1231
Cdd:TIGR00618 258 KQQLLKQLRARIEELR---AQEAVLE------------------ETQERINRARKAA-PLAAHIKA-------VTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1232 AESVLATVQQVGADTA----PYLALLASPGALPQKSRAEDLGLKAkalEKTVASWQHmaTEAARTLQTAAQATLRQtePL 1307
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAkllmKRAAHVKQQSSIEEQRRLLQTLHSQ---EIHIRDAHE--VATSIREISCQQHTLTQ--HI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1308 TKLHQEARAALTQASSSVQaatvtvmgartlladlegMKLQFPRPKDQAALQRKADSVSDRLLADTRKKTKQAERMLgna 1387
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCK------------------ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA--- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1388 aplsssAKKKGREAEVLakDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLASEARRQELEE----------- 1456
Cdd:TIGR00618 441 ------ELCAAAITCTA--QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEepcplcgscih 512
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611156 1457 --AERVGAGLSEME----QQIRESRISLEKDIET----LSELLARLGSL--------DTHQAPAQALNETQWALERLR 1516
Cdd:TIGR00618 513 pnPARQDIDNPGPLtrrmQRGEQTYAQLETSEEDvyhqLTSERKQRASLkeqmqeiqQSFSILTQCDNRSKEDIPNLQ 590
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
1115-1335 |
8.72e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 40.38 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1115 LADLEAVLESSEEEILHAAAILASLEIPQEGPSQPTKWSHLATEARALARSHRDTATKIAATAWRALLASNTSYALLWNL 1194
Cdd:COG0515 262 AAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1195 LEGRVALETQRDLEDRYQEVQAAQKALRTAVAEVLPEAESVLATVQQVGADTAPYLALLASPGALPQKSRAEDLGLKAKA 1274
Cdd:COG0515 342 AAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALA 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110611156 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 ... |
1400-1491 |
9.57e-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: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611156 1400 EAEVLAKDSAKLAKALLRERKQAHRRASRLTSQTQATLQQASQQVLAsEARrqelEEAER-VGAGLSEMEQQIRESRISL 1478
Cdd:COG0711 42 EAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKA-EAE----AEAERiIAQAEAEIEQERAKALAEL 116
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90
....*....|...
gi 110611156 1479 EKDIETLSELLAR 1491
Cdd:COG0711 117 RAEVADLAVAIAE 129
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