|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
24-296 |
2.39e-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: 303.13 E-value: 2.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 24 FTYSQVLTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGstqytplnsysyqddeqqkswsqyenpMVRGGHGCGH 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGE----PGPERYCKLVG---------------------------HTEQGKKCDY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 104 CNAGNE-NSHPAANMVDGNN----SWWMSPPLSRGLQhnEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERStDHGKT 178
Cdd:smart00136 50 CDARNPrRSHPAENLTDGNNpnnpTWWQSEPLSNGPQ--NVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 179 YQPWFNFAenaAECMRRFGMESLSPISE--DDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNV 256
Cdd:smart00136 126 WQPWQYFS---SDCRRTFGRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 808356960 257 RLRLLGTRTLQGHLMDMNewrdPTVTRRYFYAIKEIMIGG 296
Cdd:smart00136 203 RVRLTRLRTLGDELMDDR----PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
30-296 |
8.47e-75 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 249.42 E-value: 8.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 30 LTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGSTqytplnsysyqddeqqkswsqyenpmvrGGHGCGHCNAGNE 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGL----NGPERYCILSGLE----------------------------GGKKCFICDSRDP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 110 -NSHPAANMVDGNN----SWWMSPPLSrgLQHNEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERSTDHGKTYQPWFN 184
Cdd:pfam00055 49 hNSHPPSNLTDSNNgtneTWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 185 FAenaAECMRRFGM-ESLSPISEDDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNVRLRLLGT 263
Cdd:pfam00055 126 FA---SDCRRTFGRpSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRL 202
|
250 260 270
....*....|....*....|....*....|...
gi 808356960 264 RTLQghlmdMNEWRDPTVTRRYFYAIKEIMIGG 296
Cdd:pfam00055 203 HTLG-----DELLDDPSVLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2589-2730 |
2.76e-52 |
|
Laminin Domain II; 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: 368703 [Multi-domain] Cd Length: 138 Bit Score: 181.15 E-value: 2.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2589 SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKK 2668
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2669 LSSARSakvdSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAAHADI 2730
Cdd:pfam06009 81 LEVNSS----SLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1669-1793 |
2.04e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 146.64 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1669 SVYFNVPIEKK-DYTTSYGLKLTFKLSTVP-RGGRKSMNADadVRLTGANMTIEYWAsEQPTNPEEQFTVKCKLVPENFL 1746
Cdd:smart00281 4 PVYWVAPEQFLgDKVTSYGGKLRYTLSFDGrRGGTHVSAPD--VILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356960 1747 TAEGKTVTREELMKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEP 1793
Cdd:smart00281 81 YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3353-3510 |
7.08e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 140.63 E-value: 7.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3353 GFNFGSQQYSRIEydiLPEAIDKSGEFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSI 3431
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSFRTTSPNGLLLyAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356960 3432 IDGRWHTIKVSRRGKSAHLIVDDNSYEsEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLN 3510
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVV-ESGSPGGSALLNLDGPLYLGGLPEDL----KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2909-3057 |
3.06e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.71 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2909 VVSLDGEGYTSYKPSHwNPRKATKISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGqWITESSNYN 2986
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGsqNGGDFLALELEDGRLVLRYDLGSGSL-VLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356960 2987 DGKWHTVSIVREEKHVKIMIDGETeVLEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3057
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGER-VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVspGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
3378-3512 |
2.05e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.54 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3378 EFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSII-DGRWHTIKVSRRGKSAHLIVDDn 3455
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLnDGQWHRVAVERNGRSVTLSVDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 3456 SYESEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3512
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDL----KLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2932-3057 |
3.34e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2932 KISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGE 3009
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGskGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 808356960 3010 TEVlEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3057
Cdd:smart00282 81 NRV-SGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVtpGFRGCIRNLKV 129
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3383-3512 |
5.09e-31 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 119.83 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3383 IRPTSDNGIIFIATNKRTDHIAVMLEHGRVVFTYDTGSG-QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDnSYESEG 3461
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG-QTVVSS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 3462 AANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3512
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLL----LLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2704-2875 |
1.58e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 116.75 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2704 GAHFEKGSSLDLNIPQRVTRsaaHADISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAP 2783
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPNGLLLYAGSQ---------NGGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2784 AVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAETKSSVAggnksvLNLNqqiSRLFVGGVPTSARISKDLYNR 2863
Cdd:cd00110 69 LVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAL------LNLD---GPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 808356960 2864 DFVGDIESLKLH 2875
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2937-3059 |
3.89e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 114.44 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2937 FLTFSPHGLLFFVG-KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGETeVLEG 3015
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT-VVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 808356960 3016 DVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKLGS 3059
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVraGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3532-3682 |
8.06e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 108.66 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3532 GMYFGKDGGYAIVQKDyEVGLTFGLEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGgeELWHHPDieN 3608
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSG--SLVLSSK--T 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 3609 QYCDGQWQSFKISKKRNLLTVAVNGKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3682
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLnLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2729-2877 |
1.11e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2729 DISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAPAVVKLD-TPVNDGLWRRLNIERIGK 2807
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSK---------GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2808 TVSVTLSKPNSVETaetkssVAGGNKSVLNLNqqiSRLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2877
Cdd:smart00282 72 SVTLSVDGGNRVSG------ESPGGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3556-3682 |
4.12e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3556 LEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGGEELWHHPdieNQYCDGQWQSFKISKKRNLLTVAVN 3632
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgggDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 3633 GKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3682
Cdd:smart00282 79 GGNRVSGESPGGLTILnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1680-1806 |
7.99e-25 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 102.73 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1680 DYTTSYGLKLTFKLSTVPRGGRKSMNADADVRLTGANMTIEYWASEQPT-NPEEQFTVKCKLVPENFLTAEGKTVTREEL 1758
Cdd:pfam00052 11 NKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPpDPGQEQTYSVRLHEENWRDSDGAPVSREDF 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 808356960 1759 MKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEPNGVDSVikASSVE 1806
Cdd:pfam00052 91 MMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPP--ASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3560-3683 |
3.43e-24 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 100.57 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3560 MRPRMKNGILFSVGVL--EYITVEFVNGSIKTTVESGSGGEELWHHpdiENQYCDGQWQSFKISKKRNLLTVAVNGKAHL 3637
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgsDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356960 3638 KILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSFG 3683
Cdd:pfam02210 78 SSLPPGESLLLnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2289-2917 |
6.70e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK------- 2361
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkke 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2362 ESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAvttlNETR 2435
Cdd:PTZ00121 1375 EAKKKADaakkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKA----DEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2436 NDVAEALEA--AKKRVRRDEKSVDMQlvnAKAHELHlQATTLRQTFDNNKDNTDQAVEAANAfSNLTDTLKNAKaQIDNA 2513
Cdd:PTZ00121 1451 KKAEEAKKAeeAKKKAEEAKKADEAK---KKAEEAK-KADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAE-EAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2514 YEALSAEPAF-AESVQNARDKPFPDETKeKIDALSKtvSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNT 2592
Cdd:PTZ00121 1525 DEAKKAEEAKkADEAKKAEEKKKADELK-KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2593 LDSIDEKVQEV-----EKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELK 2667
Cdd:PTZ00121 1602 EEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2668 KLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAahadisfyfRTEQEHGIPLFFG 2747
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---------EEDKKKAEEAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2748 NEETAVGSRAVPTADYVAAEIEYGRPKIT---VDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAET 2824
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2825 KsSVAGGNKSVLNLNQQISRLFVGGVPTS-------ARISKDLYNR-DFVGDIESLKLHgEPIGLwNSREKGNTNVNGAQ 2896
Cdd:PTZ00121 1833 K-EVADSKNMQLEEADAFEKHKFNKNNENgedgnkeADFNKEKDLKeDDEEEIEEADEI-EKIDK-DDIEREIPNNNMAG 1909
|
650 660
....*....|....*....|.
gi 808356960 2897 KKPKITDNadelvvSLDGEGY 2917
Cdd:PTZ00121 1910 KNNDIIDD------KLDKDEY 1924
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2734-2877 |
3.53e-18 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 83.24 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2734 FRTEQEHGIPLFFGNEETavgsravptaDYVAAEIEYGRPKITVDLGDAPAVVK-LDTPVNDGLWRRLNIERIGKTVSVt 2812
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS----------DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTL- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2813 lskpnSVETAETKSSVAGGNKSVLNLNQQisrLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2877
Cdd:pfam02210 70 -----SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2317-2631 |
2.39e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKetfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQ--LTKVENLVAAITDDLE 2394
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEAAKGEFQKLNVAIGNITENLKDKREEMthavTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHElhlQATT 2474
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQLKEELKALREAL--DELRAELTLLNEEAAN---LRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2475 LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFP--DETKEKIDALSKTVSQ 2552
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2553 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKA 2628
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 808356960 2629 EEI 2631
Cdd:TIGR02168 982 KEL 984
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2415-2715 |
4.98e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2415 ENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvrRDEKsvdmqlvNAKAHELHLQATTLRQTFD--NNKdntdqavea 2492
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK--RDEL-------NAQVKELREEAQELREKRDelNEK--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2493 anaFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNARDKPFPDETKEKIDALSKTVsqdlkETEKL-----KKQLEQL 2567
Cdd:COG1340 73 ---VKELKEERDELNEKLNELREEL--DELRKELAELNKAGGSIDKLRKEIERLEWRQ-----QTEVLspeeeKELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2568 TELSEKLRKRKEAVKAGipKYSKNTLDSIDEKVQEVEKLKAEIDA---NIEETRAKISEIAGKAEEITEKANSAMEGIRL 2644
Cdd:COG1340 143 KELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2645 ARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQiKEMIAVARDAANRiklgahFEKGSSLDL 2715
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEK------LKKGEKLTT 284
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1426-1474 |
4.58e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.92 E-value: 4.58e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1426 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPECIKCQC 1474
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1425-1468 |
5.82e-14 |
|
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: 68.53 E-value: 5.82e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1425 SCDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPE 1468
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
564-612 |
8.30e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.15 E-value: 8.30e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYPNCKACAC 612
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1517-1567 |
1.00e-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: 67.76 E-value: 1.00e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 1517 CGCHPQGSEGGNlvCDPESGQCLCRESMGGRQCDRCLAGFYGFPHCYGCSC 1567
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1426-1469 |
1.29e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.29e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 1426 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYY--NFPEC 1469
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2193-2693 |
1.01e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2193 EITKMLNDEENSfgnvfgdAQDILTNSTQIQNKLvrtkthsqnsvssaKNITlngteFLQEvmkraqRARQSVRSLAE-I 2271
Cdd:pfam05483 230 EYKKEINDKEKQ-------VSLLLIQITEKENKM--------------KDLT-----FLLE------ESRDKANQLEEkT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2272 ALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQypekaQTVPGKLEEIQKKIQEETEKLDKQKEtfEAQKKRAE---- 2347
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-----KALEEDLQIATKTICQLTEEKEAQME--ELNKAKAAhsfv 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2348 --ELAAYLNSAQQLLKESKSKADKSNNIAKML--QLTKVENLVAAITD-------DLERVEAAKGEFQKL---NVAIGNI 2413
Cdd:pfam05483 351 vtEFEATTCSLEELLRTEQQRLEKNEDQLKIItmELQKKSSELEEMTKfknnkevELEELKKILAEDEKLldeKKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2414 TENLKDKREEMTHAVTTLNETRNDV---AEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK---DNTD 2487
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2488 QAVEAANAFSNLTDTLKNAK---AQIDNAYEAlsaEPAFAESVQNARD--KPFPDETKEKIDALSKTVSQDLKETEKLKK 2562
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEErmlKQIENLEEK---EMNLRDELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2563 QLEQLTELSEKLRKRKEavkagipkyskNTLDSIDEKVQEVEKLKAEIDA-----NIEETRA-----KISEIAGKAEEIT 2632
Cdd:pfam05483 588 QMKILENKCNNLKKQIE-----------NKNKNIEELHQENKALKKKGSAenkqlNAYEIKVnklelELASAKQKFEEII 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2633 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKvdsvsdkvsQIKEMIAV 2693
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH---------KIAEMVAL 708
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
756-806 |
2.58e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.91 E-value: 2.58e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 756 CDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRLNSYNQMGC 806
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-658 |
3.85e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.53 E-value: 3.85e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCRGCEC 658
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
564-605 |
3.99e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 3.99e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
609-657 |
8.72e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.72e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 609 ACACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCR-GCE 657
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
656-703 |
1.20e-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: 61.99 E-value: 1.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 656 CECLLSGAKGQTCDSN-GQCYCKGNFEGERCDRCKPNFYNFPICEECNC 703
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
755-807 |
1.20e-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: 61.99 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808356960 755 SCDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRlNSYNQMGCE 807
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1517-1560 |
1.38e-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: 61.99 E-value: 1.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1517 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYGFP 1560
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
756-799 |
2.36e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 756 CDCNVNGTISglNTCDLKTGQCMCKKNADGRRCDQCADGFYRLN 799
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
519-564 |
2.50e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFC 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
564-605 |
2.53e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1517-1562 |
9.09e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.09e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 1517 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYG--FPHC 1562
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2048-2092 |
9.36e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 2048 CHCGTA-AFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHGC 2092
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2494-2702 |
1.20e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2494 NAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTEL 2570
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL--EEVLREINEISSelpELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2571 SEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKlkaeidaNIEETRAKISEIAGKAEEITEKANSAMEGIRlarrnsv 2650
Cdd:PRK03918 240 IEELEKELESLEG--------SKRKLEEKIRELEE-------RIEELKKEIEELEEKVKELKELKEKAEEYIK------- 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2651 qLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:PRK03918 298 -LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2095-2140 |
2.07e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.07e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGC 2140
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
519-566 |
2.72e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.72e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFCNC 566
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
471-520 |
4.75e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.36 E-value: 4.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 471 PCECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTAGCVECV 520
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-656 |
5.13e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 5.13e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPdCRGC 656
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| CBM6-CBM35-CBM36_like |
cd02795 |
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ... |
855-988 |
5.56e-10 |
|
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.
Pssm-ID: 271143 Cd Length: 124 Bit Score: 59.89 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 855 QYEAEDAHTEDQKPVRFA---VDPEQFADFSWRGYAVFSPiqdkilidVDITKATVYRLLFRYRNPTSVPV-TATVTINP 930
Cdd:cd02795 1 RIEAEDATLTGGTAVSTAagaSGGGYVIGFSSGGDSVTFT--------VTVPKAGTYRLAVRYASPNGNGSrSVSLDGNG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 931 RFTHTHDVEQTGkatFAPGDLPAMKEITVDgkpfvlNPGKWSLAISTKQ---RLFLDYVVV 988
Cdd:cd02795 73 KLVGTITVPSTG---GWDTWGTASVSVNLP------DAGGHTLKIVGTGdngGANIDYVVV 124
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
656-696 |
8.71e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFP 696
Cdd:cd00055 2 CDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2048-2091 |
8.97e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 808356960 2048 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHG 2091
Cdd:cd00055 2 CDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1840-1883 |
1.23e-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: 56.21 E-value: 1.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 1840 PCECNGHSA---TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1883
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
808-854 |
1.91e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.91e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 808 SCHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHYFPTLWHN 854
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
656-701 |
2.06e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFPiCEEC 701
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1841-1888 |
3.58e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 3.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 1841 CECNGH---SATCDPDTGICtDCEHNTNGDHCEFCNEGHYGNAtNGSPYDC 1888
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2259-2769 |
3.69e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2259 QRARQSVRSLAEIALAIGSSSKAV--NVDPRLLKEAE---ETLMTLEAASADQYPEKAQTVPGKLEEiqkkiqEETEKLD 2333
Cdd:NF041483 629 AQAEQEAERLRTEAAADASAARAEgeNVAVRLRSEAAaeaERLKSEAQESADRVRAEAAAAAERVGT------EAAEALA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2334 KQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAITDdleRVEAAKGEFQKLnvaignI 2413
Cdd:NF041483 703 AAQE--EAARRRRE--------AEETLGSARAEADQERERAR----EQSEELLASARK---RVEEAQAEAQRL------V 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2414 TEnlKDKR--EEMTHAVTTLNETRNDVA--------------EALEAAKKRVRRdEKSVDMQLVNAKAHelhlqATTLRQ 2477
Cdd:NF041483 760 EE--ADRRatELVSAAEQTAQQVRDSVAglqeqaeeeiaglrSAAEHAAERTRT-EAQEEADRVRSDAY-----AERERA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2478 TFDNNK--DNTDQAVEAANAFSNLT-------------DTLKNAKAQIDNAYEAL-SAEPAFAESVQNARDkpfpDETKE 2541
Cdd:NF041483 832 SEDANRlrREAQEETEAAKALAERTvseaiaeaerlrsDASEYAQRVRTEASDTLaSAEQDAARTRADARE----DANRI 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALSKT---VSQDLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAgipkyskntldsidEKVQEVEKLKAEIDANIEET 2617
Cdd:NF041483 908 RSDAAAQAdrlIGEATSEAERLTAEARAEAErLRDEARAEAERVRA--------------DAAAQAEQLIAEATGEAERL 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2618 RAKISEIAGKAEEITE---------KANSAMEGIRL-------------------ARRNSVQLNKLAPVIVSKFEELKKL 2669
Cdd:NF041483 974 RAEAAETVGSAQQHAErirteaervKAEAAAEAERLrteareeadrtldearkdaNKRRSEAAEQADTLITEAAAEADQL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2670 -SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEkGSSLdlnipqrVTRSAAHADisfyfrteqehgiPLFFG- 2747
Cdd:NF041483 1054 tAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVE-GNSL-------VEKARTDAD-------------ELLVGa 1112
|
570 580
....*....|....*....|...
gi 808356960 2748 -NEETAVGSRAVPTADYVAAEIE 2769
Cdd:NF041483 1113 rRDATAIRERAEELRDRITGEIE 1135
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2001-2045 |
3.74e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 2001 CECSQCGS--QYCDNKSGGCECKINVEGDSCDRCKPDHWGFSkCQGC 2045
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2095-2141 |
4.55e-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: 54.67 E-value: 4.55e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPT--YGCR 2141
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1565-1613 |
4.90e-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: 54.67 E-value: 4.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLSAENPLGC 1613
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
472-516 |
5.22e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTA-GC 516
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPpGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
519-559 |
5.62e-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: 54.28 E-value: 5.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGD 559
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1947-1998 |
1.24e-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: 53.51 E-value: 1.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 1947 PCQCNGNNNLtdSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVTAKNC 1998
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2048-2097 |
1.56e-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: 53.13 E-value: 1.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2048 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYgeHGCDKCDC 2097
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL--PSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2537-2669 |
1.75e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLR-KRKEAVKagipkyskntldSIDEKVQEVEKLKAEIDANIE 2615
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNA------------QVKELREEAQELREKRDELNE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2616 etraKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2669
Cdd:COG1340 72 ----KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL 121
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2000-2046 |
1.85e-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: 53.13 E-value: 1.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2000 SCECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGF-SKCQGCQ 2046
Cdd:cd00055 1 PCDCNGHGSLsgQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1565-1614 |
3.04e-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: 52.36 E-value: 3.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLsAENPLGCV 1614
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
427-474 |
3.72e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 427 CDCDPD-KHTGACAEETGKCECLPRFVGEDCDQCASGYYDAPKCKPCEC 474
Cdd:pfam00053 1 CDCNPHgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2095-2143 |
4.35e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 4.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGCRRC 2143
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2319-2705 |
7.20e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2319 EEIQKKIQEETEkLDKQKETFEAQKKR----AEELAAYLNS-AQQLLKESKSKADKSnniakmlqltkvenLVAAitddl 2393
Cdd:NF041483 124 EAVQRRQQLDQE-LAERRQTVESHVNEnvawAEQLRARTESqARRLLDESRAEAEQA--------------LAAA----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2394 eRVEAAKgefqklnvaignITEnlkDKREEMThavttlNETRNDVAEAlEAAKKRVRRDEKsvdmQLVNA---KAHELHL 2470
Cdd:NF041483 184 -RAEAER------------LAE---EARQRLG------SEAESARAEA-EAILRRARKDAE----RLLNAastQAQEATD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2471 QATTLRQTFDNNKDNT-DQAVEAANA----FSNLTDTLKNAKAQIDN----AYEALSAEPAFAESVQNARDKpfpdETKE 2541
Cdd:NF041483 237 HAEQLRSSTAAESDQArRQAAELSRAaeqrMQEAEEALREARAEAEKvvaeAKEAAAKQLASAESANEQRTR----TAKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALsktVSQDLKETEKLKKQLEQL------------TELSEKLR-KRKEAVKAGIPKYSKNTLD-----SIDEK---- 2599
Cdd:NF041483 313 EIARL---VGEATKEAEALKAEAEQAladaraeaeklvAEAAEKARtVAAEDTAAQLAKAARTAEEvltkaSEDAKattr 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2600 --VQEVEKLKAEIDANIEETRAKISEIA----GKAEEITE----KANSAMEGIRLARRNSVQLNKLApviVSKFEELKkl 2669
Cdd:NF041483 390 aaAEEAERIRREAEAEADRLRGEAADQAeqlkGAAKDDTKeyraKTVELQEEARRLRGEAEQLRAEA---VAEGERIR-- 464
|
410 420 430
....*....|....*....|....*....|....*.
gi 808356960 2670 SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGA 2705
Cdd:NF041483 465 GEARREAVQQIEEAARTAEELLTKAKADADELRSTA 500
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1891-1945 |
8.22e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 8.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 1891 CACPFAPTNNfaKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHPQISGESC 1945
Cdd:pfam00053 1 CDCNPHGSLS--DTCD-PETGQ---CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
472-509 |
8.30e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 8.30e-08
10 20 30
....*....|....*....|....*....|....*...
gi 808356960 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGY 509
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
427-467 |
9.47e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 427 CDCDPDKH-TGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
809-847 |
9.75e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.75e-08
10 20 30
....*....|....*....|....*....|....*....
gi 808356960 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1472-1515 |
1.02e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.82 E-value: 1.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDPLI-GCQ 1515
Cdd:cd00055 2 CDCNghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1472-1510 |
1.17e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.17e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDP 1510
Cdd:smart00180 1 CDCDpggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-467 |
1.66e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 1.66e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 427 CDCDPD-KHTGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:cd00055 2 CDCNGHgSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1472-1514 |
2.04e-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: 50.04 E-value: 2.04e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGY--DPLIGC 1514
Cdd:pfam00053 1 CDCNphgsLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1565-1613 |
2.52e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDlsaENPLGC 1613
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1891-1938 |
2.55e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 1891 CACPfaPTNNFAKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHP 1938
Cdd:smart00180 1 CDCD--PGGSASGTCD-PDTGQ---CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2541-2709 |
8.62e-07 |
|
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: 55.46 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2541 EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAK 2620
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2621 ISEIAGKAEEITEKANSAMEGIRLARRN-----SVQLNKLAPVIVSKFEELKKLsSARSAKVDSVSDKVSQIKEMI--AV 2693
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigelEAEIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEELerEI 345
|
170
....*....|....*.
gi 808356960 2694 ARDAANRIKLGAHFEK 2709
Cdd:TIGR02169 346 EEERKRRDKLTEEYAE 361
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1890-1945 |
1.10e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 1890 ACACPFAPTNNFakSCDVseegQLLQCNCKPGYTGDRCDRCASGFFGHPqISGESC 1945
Cdd:cd00055 1 PCDCNGHGSLSG--QCDP----GTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
701-753 |
1.24e-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: 47.73 E-value: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEDGC 753
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPET-GQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2001-2048 |
1.56e-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: 47.35 E-value: 1.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2001 CECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGFSKCQGcQGC 2048
Cdd:pfam00053 1 CDCNPHGSLsdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP-QGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1841-1883 |
1.56e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 1841 CECN--GHSA-TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1883
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1948-1991 |
3.20e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 3.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1948 CQCNGNNNLTDSrsCHPNSGDCyLCEQNTDGRHCESCAAWFYGD 1991
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
297-345 |
3.20e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 3.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 297 RCVCNGHA---VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQA 345
Cdd:cd00055 1 PCDCNGHGslsGQCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
809-847 |
3.76e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 3.76e-06
10 20 30
....*....|....*....|....*....|....*....
gi 808356960 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
701-754 |
4.01e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 4.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEdGCR 754
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGT-GQ-CECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2211-2584 |
9.34e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2211 DAQDILTNSTQIQNKLVRTKTHSQNSVSSAknITLNGTEFLQEVMKRAQRARQSVRSLAE--IALAIGSSSkavnvdpRL 2288
Cdd:NF041483 903 DANRIRSDAAAQADRLIGEATSEAERLTAE--ARAEAERLRDEARAEAERVRADAAAQAEqlIAEATGEAE-------RL 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLmtleaASADQYPEKAQTVPGKL--------EEIQKKIQEETEK-LDKQKEtfEAQKKRAE--ELAAYLNS-- 2355
Cdd:NF041483 974 RAEAAETV-----GSAQQHAERIRTEAERVkaeaaaeaERLRTEAREEADRtLDEARK--DANKRRSEaaEQADTLITea 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2356 ---AQQLLKESKSKADKSNNIAKMLQLTKV-------ENLVA-AITDDLERVEAAKGEFQKLNV-------AIGNITENL 2417
Cdd:NF041483 1047 aaeADQLTAKAQEEALRTTTEAEAQADTMVgaarkeaERIVAeATVEGNSLVEKARTDADELLVgarrdatAIRERAEEL 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2418 kdkREEMTHAVTTLNE-TRNDVAEALEAAKKRVRRDEKSVDMQLVNA--KAHEL----HLQATTLRQTfdnnkdntdqAV 2490
Cdd:NF041483 1127 ---RDRITGEIEELHErARRESAEQMKSAGERCDALVKAAEEQLAEAeaKAKELvsdaNSEASKVRIA----------AV 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2491 EAANAFsnltdtLKNA---KAQIDNAYEALSAEpAFAESVQNArdkpfpDETKEKIDALSKTvSQDLK-ETEKLKKQLEQ 2566
Cdd:NF041483 1194 KKAEGL------LKEAeqkKAELVREAEKIKAE-AEAEAKRTV------EEGKRELDVLVRR-REDINaEISRVQDVLEA 1259
|
410
....*....|....*....
gi 808356960 2567 LTEL-SEKLRKRKEAVKAG 2584
Cdd:NF041483 1260 LESFeAPSGGGKGNGVKAG 1278
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1948-1994 |
2.36e-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: 44.27 E-value: 2.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 1948 CQCNGNNnlTDSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVT 1994
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2510-2635 |
2.87e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.93 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2510 IDNAYEALSAepaFAESVQNARDKPFPDET-----------KEKIDALSKTVSQDLKE-TEKLKKQLEQ----LTELSEK 2573
Cdd:cd13769 7 IQKAQEAINN---LAQQVQKQLGLQNPEEVvntlkeqsdnfANNLQEVSSSLKEEAKKkQGEVEEAWNEfktkLSETVPE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2574 LRKRKEAVKAgipkySKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2635
Cdd:cd13769 84 LRKSLPVEEK-----AQELQAKLQSGLQtlvtESQKLAKAISENSQKAQEELQKATKQAYDIAVEA 144
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
701-749 |
1.74e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHH 749
Cdd:smart00180 1 CDCDPGGSASG--TCDPDT-GQ-CECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2282-2389 |
3.46e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 43.34 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2282 VNVDpRLLKEAEETlmtlEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKKRAEELAAYLNSAQQL 2359
Cdd:smart00935 4 VDVQ-KILQESPAG----KAAQK-QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseAAREKKEKELQKKVQEFQRK 77
|
90 100 110
....*....|....*....|....*....|..
gi 808356960 2360 LKESKSKADKSNN--IAKMLQltKVENLVAAI 2389
Cdd:smart00935 78 QQKLQQDLQKRQQeeLQKILD--KINKAIKEV 107
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2504-2709 |
1.01e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2504 KNAKAQIDNAYEALSAEpafAESVQNARDKPFPDETKEKI----DALSKTVSQDLKETEKLKKQL----EQLTELSEKLR 2575
Cdd:cd22656 83 QNAGGTIDSYYAEILEL---IDDLADATDDEELEEAKKTIkallDDLLKEAKKYQDKAAKVVDKLtdfeNQTEKDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2576 KRKEAVKAGIPKYSK-NTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQL-N 2653
Cdd:cd22656 160 TLEKALKDLLTDEGGaIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLlA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2654 KLAPVIVSkFEELKKLSSARSAKVDSVSDKVSQIkemiavARDAANRIKLGAHFEK 2709
Cdd:cd22656 240 LIGPAIPA-LEKLQGAWQAIATDLDSLKDLLEDD------ISKIPAAILAKLELEK 288
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
298-344 |
1.69e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 298 CVCN--GHA-VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQ 344
Cdd:smart00180 1 CDCDpgGSAsGTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
24-296 |
2.39e-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: 303.13 E-value: 2.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 24 FTYSQVLTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGstqytplnsysyqddeqqkswsqyenpMVRGGHGCGH 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGE----PGPERYCKLVG---------------------------HTEQGKKCDY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 104 CNAGNE-NSHPAANMVDGNN----SWWMSPPLSRGLQhnEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERStDHGKT 178
Cdd:smart00136 50 CDARNPrRSHPAENLTDGNNpnnpTWWQSEPLSNGPQ--NVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 179 YQPWFNFAenaAECMRRFGMESLSPISE--DDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNV 256
Cdd:smart00136 126 WQPWQYFS---SDCRRTFGRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 808356960 257 RLRLLGTRTLQGHLMDMNewrdPTVTRRYFYAIKEIMIGG 296
Cdd:smart00136 203 RVRLTRLRTLGDELMDDR----PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
30-296 |
8.47e-75 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 249.42 E-value: 8.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 30 LTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGSTqytplnsysyqddeqqkswsqyenpmvrGGHGCGHCNAGNE 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGL----NGPERYCILSGLE----------------------------GGKKCFICDSRDP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 110 -NSHPAANMVDGNN----SWWMSPPLSrgLQHNEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERSTDHGKTYQPWFN 184
Cdd:pfam00055 49 hNSHPPSNLTDSNNgtneTWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 185 FAenaAECMRRFGM-ESLSPISEDDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNVRLRLLGT 263
Cdd:pfam00055 126 FA---SDCRRTFGRpSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRL 202
|
250 260 270
....*....|....*....|....*....|...
gi 808356960 264 RTLQghlmdMNEWRDPTVTRRYFYAIKEIMIGG 296
Cdd:pfam00055 203 HTLG-----DELLDDPSVLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2589-2730 |
2.76e-52 |
|
Laminin Domain II; 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: 368703 [Multi-domain] Cd Length: 138 Bit Score: 181.15 E-value: 2.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2589 SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKK 2668
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2669 LSSARSakvdSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAAHADI 2730
Cdd:pfam06009 81 LEVNSS----SLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1669-1793 |
2.04e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 146.64 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1669 SVYFNVPIEKK-DYTTSYGLKLTFKLSTVP-RGGRKSMNADadVRLTGANMTIEYWAsEQPTNPEEQFTVKCKLVPENFL 1746
Cdd:smart00281 4 PVYWVAPEQFLgDKVTSYGGKLRYTLSFDGrRGGTHVSAPD--VILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356960 1747 TAEGKTVTREELMKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEP 1793
Cdd:smart00281 81 YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3353-3510 |
7.08e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 140.63 E-value: 7.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3353 GFNFGSQQYSRIEydiLPEAIDKSGEFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSI 3431
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSFRTTSPNGLLLyAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356960 3432 IDGRWHTIKVSRRGKSAHLIVDDNSYEsEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLN 3510
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVV-ESGSPGGSALLNLDGPLYLGGLPEDL----KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2909-3057 |
3.06e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.71 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2909 VVSLDGEGYTSYKPSHwNPRKATKISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGqWITESSNYN 2986
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGsqNGGDFLALELEDGRLVLRYDLGSGSL-VLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356960 2987 DGKWHTVSIVREEKHVKIMIDGETeVLEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3057
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGER-VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVspGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
3378-3512 |
2.05e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.54 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3378 EFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSII-DGRWHTIKVSRRGKSAHLIVDDn 3455
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLnDGQWHRVAVERNGRSVTLSVDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 3456 SYESEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3512
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDL----KLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2932-3057 |
3.34e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2932 KISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGE 3009
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGskGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 808356960 3010 TEVlEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3057
Cdd:smart00282 81 NRV-SGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVtpGFRGCIRNLKV 129
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3383-3512 |
5.09e-31 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 119.83 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3383 IRPTSDNGIIFIATNKRTDHIAVMLEHGRVVFTYDTGSG-QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDnSYESEG 3461
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG-QTVVSS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 3462 AANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3512
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLL----LLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2704-2875 |
1.58e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 116.75 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2704 GAHFEKGSSLDLNIPQRVTRsaaHADISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAP 2783
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPNGLLLYAGSQ---------NGGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2784 AVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAETKSSVAggnksvLNLNqqiSRLFVGGVPTSARISKDLYNR 2863
Cdd:cd00110 69 LVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAL------LNLD---GPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 808356960 2864 DFVGDIESLKLH 2875
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2937-3059 |
3.89e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 114.44 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2937 FLTFSPHGLLFFVG-KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGETeVLEG 3015
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT-VVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 808356960 3016 DVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKLGS 3059
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVraGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3532-3682 |
8.06e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 108.66 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3532 GMYFGKDGGYAIVQKDyEVGLTFGLEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGgeELWHHPDieN 3608
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSG--SLVLSSK--T 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 3609 QYCDGQWQSFKISKKRNLLTVAVNGKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3682
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLnLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2729-2877 |
1.11e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2729 DISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAPAVVKLD-TPVNDGLWRRLNIERIGK 2807
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSK---------GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2808 TVSVTLSKPNSVETaetkssVAGGNKSVLNLNqqiSRLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2877
Cdd:smart00282 72 SVTLSVDGGNRVSG------ESPGGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3556-3682 |
4.12e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3556 LEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGGEELWHHPdieNQYCDGQWQSFKISKKRNLLTVAVN 3632
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgggDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 3633 GKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3682
Cdd:smart00282 79 GGNRVSGESPGGLTILnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1680-1806 |
7.99e-25 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 102.73 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1680 DYTTSYGLKLTFKLSTVPRGGRKSMNADADVRLTGANMTIEYWASEQPT-NPEEQFTVKCKLVPENFLTAEGKTVTREEL 1758
Cdd:pfam00052 11 NKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPpDPGQEQTYSVRLHEENWRDSDGAPVSREDF 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 808356960 1759 MKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEPNGVDSVikASSVE 1806
Cdd:pfam00052 91 MMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPP--ASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3560-3683 |
3.43e-24 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 100.57 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3560 MRPRMKNGILFSVGVL--EYITVEFVNGSIKTTVESGSGGEELWHHpdiENQYCDGQWQSFKISKKRNLLTVAVNGKAHL 3637
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgsDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 808356960 3638 KILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSFG 3683
Cdd:pfam02210 78 SSLPPGESLLLnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2937-3063 |
1.50e-23 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.93 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2937 FLTFSPHGLLFFVGK--DKDFMALELSDGGVKLSVDLGSGVGQwITESSNYNDGKWHTVSIVREEKHVKIMIDGETEVLE 3014
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGRLEVSYDLGSGAAV-VRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 3015 GDVPGKDSEMSVTEFLYIGGTPSGLSVR--TTIVP-LRGCIKSVKLGSDNVD 3063
Cdd:pfam00054 80 ESPLGATTDLDVDGPLYVGGLPSLGVKKrrLAISPsFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3383-3515 |
1.87e-23 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.54 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3383 IRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDN---SYE 3458
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEarpTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 3459 SEGAANQNEDLIEtqpPFYVGGVPADLAGfARNLVVGVRsqFSGCIKDFKLNGKSLD 3515
Cdd:pfam00054 81 SPLGATTDLDVDG---PLYVGGLPSLGVK-KRRLAISPS--FDGCIRDVIVNGKPLD 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2289-2917 |
6.70e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK------- 2361
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkke 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2362 ESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAvttlNETR 2435
Cdd:PTZ00121 1375 EAKKKADaakkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKA----DEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2436 NDVAEALEA--AKKRVRRDEKSVDMQlvnAKAHELHlQATTLRQTFDNNKDNTDQAVEAANAfSNLTDTLKNAKaQIDNA 2513
Cdd:PTZ00121 1451 KKAEEAKKAeeAKKKAEEAKKADEAK---KKAEEAK-KADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAE-EAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2514 YEALSAEPAF-AESVQNARDKPFPDETKeKIDALSKtvSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNT 2592
Cdd:PTZ00121 1525 DEAKKAEEAKkADEAKKAEEKKKADELK-KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2593 LDSIDEKVQEV-----EKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELK 2667
Cdd:PTZ00121 1602 EEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2668 KLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAahadisfyfRTEQEHGIPLFFG 2747
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---------EEDKKKAEEAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2748 NEETAVGSRAVPTADYVAAEIEYGRPKIT---VDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAET 2824
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2825 KsSVAGGNKSVLNLNQQISRLFVGGVPTS-------ARISKDLYNR-DFVGDIESLKLHgEPIGLwNSREKGNTNVNGAQ 2896
Cdd:PTZ00121 1833 K-EVADSKNMQLEEADAFEKHKFNKNNENgedgnkeADFNKEKDLKeDDEEEIEEADEI-EKIDK-DDIEREIPNNNMAG 1909
|
650 660
....*....|....*....|.
gi 808356960 2897 KKPKITDNadelvvSLDGEGY 2917
Cdd:PTZ00121 1910 KNNDIIDD------KLDKDEY 1924
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2252-2709 |
2.08e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2252 QEVMKRAQRARQSvrslAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPgKLEEIQKKIQEETEK 2331
Cdd:PTZ00121 1332 DAAKKKAEEAKKA----AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2332 LDKQKETfEAQKKRAEEL---AAYLNSAQQLLK--ESKSKADKSNNIAKmlQLTKVENLVAAITddlervEAAKGEFQKL 2406
Cdd:PTZ00121 1407 ADELKKA-AAAKKKADEAkkkAEEKKKADEAKKkaEEAKKADEAKKKAE--EAKKAEEAKKKAE------EAKKADEAKK 1477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2407 NVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHlQATTLRQTFDNNKDNT 2486
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2487 DQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQnardKPFPDETKEKIDALSK-----TVSQDLKETEKLK 2561
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM----KLYEEEKKMKAEEAKKaeeakIKAEELKKAEEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2562 KQLEQLTELSEKLRKRKEAVKagipkyskntldsideKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEG 2641
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELK----------------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 2642 IRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEK 2709
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2734-2877 |
3.53e-18 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 83.24 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2734 FRTEQEHGIPLFFGNEETavgsravptaDYVAAEIEYGRPKITVDLGDAPAVVK-LDTPVNDGLWRRLNIERIGKTVSVt 2812
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS----------DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTL- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2813 lskpnSVETAETKSSVAGGNKSVLNLNQQisrLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2877
Cdd:pfam02210 70 -----SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2168-2695 |
1.28e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2168 IANISSATIVgARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSsakniTLNG 2247
Cdd:PRK02224 196 IEEKEEKDLH-ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE-----TIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2248 TEFLQEVMKRAQRARQSVRSlaeialaigssskavnvdpRLLKEAEETLMTLEAASADqypekAQTVPGKLEEIQKKIQE 2327
Cdd:PRK02224 270 TEREREELAEEVRDLRERLE-------------------ELEEERDDLLAEAGLDDAD-----AEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2328 ETEKLDKQKETFEAQKKRAEELAAylnSAQQLLKESKSKADKSNNIAKMLQLTK--VENLVAAITDDLERVEAAKGEFQK 2405
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE---DADDLEERAEELREEAAELESELEEAReaVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2406 LNVAIGN-------ITENLKDKREEMTHAVTTLNETRNDVAEA---LEAAK-------------------KRVRRDE--- 2453
Cdd:PRK02224 403 APVDLGNaedfleeLREERDELREREAELEATLRTARERVEEAealLEAGKcpecgqpvegsphvetieeDRERVEElea 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2454 ---------KSVDMQLVNAK-AHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNayEALSAEPAF 2523
Cdd:PRK02224 483 eledleeevEEVEERLERAEdLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA--EAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2524 AESVQNArdkpfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTELS---EKLRKRKEAvKAGIPKYSKNTLDSID 2597
Cdd:PRK02224 561 AEAEEEA------EEAREEVAELNSklaELKERIESLERIRTLLAAIADAEdeiERLREKREA-LAELNDERRERLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2598 EKVQEvekLKAEID-ANIEETRAK-------ISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLApvivskfEELKKL 2669
Cdd:PRK02224 634 ERKRE---LEAEFDeARIEEAREDkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELR-------ERREAL 703
|
570 580
....*....|....*....|....*.
gi 808356960 2670 sSARSAKVDSVSDKVSQIKEMIAVAR 2695
Cdd:PRK02224 704 -ENRVEALEALYDEAEELESMYGDLR 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2317-2631 |
2.39e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKetfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQ--LTKVENLVAAITDDLE 2394
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEAAKGEFQKLNVAIGNITENLKDKREEMthavTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHElhlQATT 2474
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQLKEELKALREAL--DELRAELTLLNEEAAN---LRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2475 LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFP--DETKEKIDALSKTVSQ 2552
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2553 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKA 2628
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 808356960 2629 EEI 2631
Cdd:TIGR02168 982 KEL 984
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2415-2715 |
4.98e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2415 ENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvrRDEKsvdmqlvNAKAHELHLQATTLRQTFD--NNKdntdqavea 2492
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK--RDEL-------NAQVKELREEAQELREKRDelNEK--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2493 anaFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNARDKPFPDETKEKIDALSKTVsqdlkETEKL-----KKQLEQL 2567
Cdd:COG1340 73 ---VKELKEERDELNEKLNELREEL--DELRKELAELNKAGGSIDKLRKEIERLEWRQ-----QTEVLspeeeKELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2568 TELSEKLRKRKEAVKAGipKYSKNTLDSIDEKVQEVEKLKAEIDA---NIEETRAKISEIAGKAEEITEKANSAMEGIRL 2644
Cdd:COG1340 143 KELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2645 ARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQiKEMIAVARDAANRiklgahFEKGSSLDL 2715
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEK------LKKGEKLTT 284
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2317-2702 |
7.28e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.61 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQLLKE-----------SKSKADKSNNIAKM-LQLTKVE 2383
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkYNDLKKQkeelenelnllEKEKLNIQKNIDKIkNKLLKLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2384 ----NLVAAITD---------DLER--------VEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDvaeaL 2442
Cdd:TIGR04523 201 lllsNLKKKIQKnkslesqisELKKqnnqlkdnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----L 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2443 EAAKKRVrrDEKSVDMQLVNAKAHELhlqattlrqtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSaepa 2522
Cdd:TIGR04523 277 EQNNKKI--KELEKQLNQLKSEISDL------------NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2523 faesvqnardkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIP--KYSKNTLDS----- 2595
Cdd:TIGR04523 339 ---------------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlESQINDLESkiqnq 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2596 ------IDEKVQEVEKLKAEIDANIEETRAKI----SEIAGKAEEITEKANSAMEgirLARRNSVQLNKLapvivSKFE- 2664
Cdd:TIGR04523 404 eklnqqKDEQIKKLQQEKELLEKEIERLKETIiknnSEIKDLTNQDSVKELIIKN---LDNTRESLETQL-----KVLSr 475
|
410 420 430
....*....|....*....|....*....|....*...
gi 808356960 2665 ELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2185-2709 |
2.00e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.06 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2185 KKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVM--------K 2256
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseisdlnnQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2257 RAQRARQSVRS--------LAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEA--ASADQYPEKAQTvpgKLEEIQKKIQ 2326
Cdd:TIGR04523 304 KEQDWNKELKSelknqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESenSEKQRELEEKQN---EIEKLKKENQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2327 ---EETEKLDKQKETFEAQKKRAEELAaylnsaQQLLKESKSKADKSNNIAKMLQLTKVENLVAAIT-DDLERVEAAKGe 2402
Cdd:TIGR04523 381 sykQEIKNLESQINDLESKIQNQEKLN------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKE- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2403 fqklnvaigNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMqlvnakaheLHLQATTLRQTFDNN 2482
Cdd:TIGR04523 454 ---------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK---------LNEEKKELEEKVKDL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2483 KDNTDQaveaanaFSNLTDTLKNAKAQIDNayealsaepafaesvqnardkpfpdETKEKIDALSKtvsqdlKETEKLKK 2562
Cdd:TIGR04523 516 TKKISS-------LKEKIEKLESEKKEKES-------------------------KISDLEDELNK------DDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2563 QLE-QLTELSEKLRKRKEAVKAgipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEItEKANSAMEG 2641
Cdd:TIGR04523 558 NLEkEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA-KKENEKLSS 631
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 2642 IRLARRNSvqLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANriKLGAHFEK 2709
Cdd:TIGR04523 632 IIKNIKSK--KNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK--ELSLHYKK 695
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2182-2652 |
3.00e-14 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 79.23 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2182 ARNKKEFNDINEITKMLNDEENSFGNV-FGDAQDILTNSTQIQNKLvrtkthsqnsvssaKNITLNGTEFLQEvmkraqr 2260
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGEVeTGIIKDIFGKLTQELNQN--------------LKKLEIFGLTLGL------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2261 aRQSVRSLAEIALAIGSSSKAVNVDPRL-----LKEAEETLMTLEAA-----SADQYPEKAQTVPGKLEEIQKKIQE-ET 2329
Cdd:COG5185 189 -LKGISELKKAEPSGTVNSIKESETGNLgsestLLEKAKEIINIEEAlkgfqDPESELEDLAQTSDKLEKLVEQNTDlRL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2330 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlqltkvenlvaaiTDDLERVEAAKGEFQKLNVA 2409
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA-----------------TESLEEQLAAAEAEQELEES 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2410 IGNITENLKDKREEmthavttLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNnkDNTDQA 2489
Cdd:COG5185 331 KRETETGIQNLTAE-------IEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE--IPQNQR 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2490 VEAANAFSNLTDTLKNAKAQIDN----------AYEALSAEPAFAESVQNARDKPFPDETKEKID-ALSKTVSQDLKETE 2558
Cdd:COG5185 402 GYAQEILATLEDTLKAADRQIEElqrqieqatsSNEEVSKLLNELISELNKVMREADEESQSRLEeAYDEINRSVRSKKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2559 KLKKQLEQlteLSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANiEETRAKISEIAGKAEEITEKANSA 2638
Cdd:COG5185 482 DLNEELTQ---IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRAR-GYAHILALENLIPASELIQASNAK 557
|
490
....*....|....
gi 808356960 2639 MEGIRLARRNSVQL 2652
Cdd:COG5185 558 TDGQAANLRTAVID 571
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1426-1474 |
4.58e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.92 E-value: 4.58e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1426 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPECIKCQC 1474
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1425-1468 |
5.82e-14 |
|
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: 68.53 E-value: 5.82e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1425 SCDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPE 1468
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
564-612 |
8.30e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.15 E-value: 8.30e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYPNCKACAC 612
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1517-1567 |
1.00e-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: 67.76 E-value: 1.00e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 1517 CGCHPQGSEGGNlvCDPESGQCLCRESMGGRQCDRCLAGFYGFPHCYGCSC 1567
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2249-2692 |
1.06e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2249 EFLQEVMKRAQRARQSVRS--------LAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEE 2320
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAelqeleekLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2321 IQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQlTKVENLVAAITDDLERVEAAK 2400
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2401 GEFQK-------LNVAIGNITENLKDKREEMTHA--------VTTLNETRNDVAEALEA-----AKKRVRRDEKSVDMQL 2460
Cdd:TIGR02168 400 NEIERlearlerLEDRRERLQQEIEELLKKLEEAelkelqaeLEELEEELEELQEELERleealEELREELEEAEQALDA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2461 VNAKAHELHLQATTLRQTFDNNKDNTD---QAVEAANAFSNLTDTLKNaKAQIDNAYEAlSAEPAFAESVQNA--RDKpf 2535
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILGVLSE-LISVDEGYEA-AIEAALGGRLQAVvvENL-- 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2536 pDETKEKIDALSKT--------VSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGiPKYSK--NTL-------DSIDE 2598
Cdd:TIGR02168 556 -NAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD-PKLRKalSYLlggvlvvDDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2599 KVQEVEKLKA------------------------------EIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRN 2648
Cdd:TIGR02168 634 ALELAKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 808356960 2649 SVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIA 2692
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1426-1469 |
1.29e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.29e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 1426 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYY--NFPEC 1469
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2309-2596 |
1.29e-13 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 74.56 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2309 EKAQTVPGKLEEIQKKIQE---ETEKLDKQKETFEAQ-KKRAEELAAYLNSAQQL---LKESKSKADKSNNIAKMLQLTK 2381
Cdd:COG1340 1 SKTDELSSSLEELEEKIEElreEIEELKEKRDELNEElKELAEKRDELNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2382 vENLVAAITDDLERVEAAKGEFQKLNVAIGNItENLKDK--REEMTH--AVTTLNETR------NDVAEALEAAKKRVRR 2451
Cdd:COG1340 81 -DELNEKLNELREELDELRKELAELNKAGGSI-DKLRKEieRLEWRQqtEVLSPEEEKelvekiKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2452 DEKSVDMQlvnAKAHELHLQATTLRQtfdnnkdntdQAVEAANAFSNLTDTLKNAKAQIDNAYEalSAEPAFAEsVQNAR 2531
Cdd:COG1340 159 NEKLKELR---AELKELRKEAEEIHK----------KIKELAEEAQELHEEMIELYKEADELRK--EADELHKE-IVEAQ 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2532 DKpfPDETKEKIDALSKTVSQDLKETEKLKKQLE--QLTELSEKLRKRKEAVKAGIPKYSKNTLDSI 2596
Cdd:COG1340 223 EK--ADELHEEIIELQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKKGEKLTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2317-2618 |
2.40e-13 |
|
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: 77.03 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQE--------ETEKLDKQKETFEAQ-----------KKRAEELAAYLNSAQQLLKE-----SKSKADKSNN 2372
Cdd:TIGR02169 212 RYQALLKEKREyegyellkEKEALERQKEAIERQlasleeeleklTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2373 I-AKMLQLT-KVENLVAAITDDLERVEAAKGEFQKLNVAIgnitENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvr 2450
Cdd:TIGR02169 292 VkEKIGELEaEIASLERSIAEKERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2451 rdeksvdMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNA 2530
Cdd:TIGR02169 366 -------LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2531 rdkpFPDETKEKIDalsktvsqdlkETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSkntlDSIDEKVQEVEKLKAEI 2610
Cdd:TIGR02169 439 ----LEEEKEDKAL-----------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE----KELSKLQRELAEAEAQA 499
|
....*...
gi 808356960 2611 DANIEETR 2618
Cdd:TIGR02169 500 RASEERVR 507
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2289-2640 |
4.10e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKAD 2368
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2369 KSNNiakmlQLTKVENLVAAITDDLERVEAakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEaLEAAKKR 2448
Cdd:COG4372 98 QAQE-----ELESLQEEAEELQEELEELQK---ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-LQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2449 VRRDEKSVDMQLVNAKAHELHLQAttlRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKaqIDNAYEALSAEPAFAESVQ 2528
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEA---NRNAEKEEELAEAEKLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2529 NARDKPFPDETKEKIDALSKTVsQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKA 2608
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELEL-AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350
....*....|....*....|....*....|..
gi 808356960 2609 EIDANIEETRAKISEIAGKAEEITEKANSAME 2640
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2289-2666 |
5.95e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASaDQYPEKAQTVP---GKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELA---AYLNSAQQLLKE 2362
Cdd:PRK03918 288 LKEKAEEYIKLSEFY-EEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2363 SKSKADKSNNIAKMLQLTKVENLVAaitdDLERVEAAKGEFQKlnvAIGNITE---NLKDKREEMTHAVTTL-------- 2431
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEK----ELEELEKAKEEIEE---EISKITArigELKKEIKELKKAIEELkkakgkcp 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2432 ----------------------NETRNDVAEaLEAAKKRVRRDEKSVDMQLvnAKAHELhlqaTTLRQTFDN-------- 2481
Cdd:PRK03918 440 vcgrelteehrkelleeytaelKRIEKELKE-IEEKERKLRKELRELEKVL--KKESEL----IKLKELAEQlkeleekl 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2482 NKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALS------------------AEPAFAESVQNARDKPFP--DETKE 2541
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleelkkklaelekkldeLEEELAELLKELEELGFEsvEELEE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALS---------KTVSQDLKETEK--------LKKQLEQLTELS---EKLRKRKEAVKAgipKYSKNT--------- 2592
Cdd:PRK03918 593 RLKELEpfyneylelKDAEKELEREEKelkkleeeLDKAFEELAETEkrlEELRKELEELEK---KYSEEEyeelreeyl 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2593 -----LDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIT--EKANSAMEGIR---LARRNSVQLNKLAPV--IV 2660
Cdd:PRK03918 670 elsreLAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELRekvKKYKALLKERALSKVgeIA 749
|
....*..
gi 808356960 2661 SK-FEEL 2666
Cdd:PRK03918 750 SEiFEEL 756
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2193-2693 |
1.01e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2193 EITKMLNDEENSfgnvfgdAQDILTNSTQIQNKLvrtkthsqnsvssaKNITlngteFLQEvmkraqRARQSVRSLAE-I 2271
Cdd:pfam05483 230 EYKKEINDKEKQ-------VSLLLIQITEKENKM--------------KDLT-----FLLE------ESRDKANQLEEkT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2272 ALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQypekaQTVPGKLEEIQKKIQEETEKLDKQKEtfEAQKKRAE---- 2347
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-----KALEEDLQIATKTICQLTEEKEAQME--ELNKAKAAhsfv 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2348 --ELAAYLNSAQQLLKESKSKADKSNNIAKML--QLTKVENLVAAITD-------DLERVEAAKGEFQKL---NVAIGNI 2413
Cdd:pfam05483 351 vtEFEATTCSLEELLRTEQQRLEKNEDQLKIItmELQKKSSELEEMTKfknnkevELEELKKILAEDEKLldeKKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2414 TENLKDKREEMTHAVTTLNETRNDV---AEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK---DNTD 2487
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2488 QAVEAANAFSNLTDTLKNAK---AQIDNAYEAlsaEPAFAESVQNARD--KPFPDETKEKIDALSKTVSQDLKETEKLKK 2562
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEErmlKQIENLEEK---EMNLRDELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2563 QLEQLTELSEKLRKRKEavkagipkyskNTLDSIDEKVQEVEKLKAEIDA-----NIEETRA-----KISEIAGKAEEIT 2632
Cdd:pfam05483 588 QMKILENKCNNLKKQIE-----------NKNKNIEELHQENKALKKKGSAenkqlNAYEIKVnklelELASAKQKFEEII 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2633 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKvdsvsdkvsQIKEMIAV 2693
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH---------KIAEMVAL 708
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
756-806 |
2.58e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.91 E-value: 2.58e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 756 CDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRLNSYNQMGC 806
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2734-2880 |
2.72e-12 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 66.57 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2734 FRTEQEHGIPLFFGNeetavgsraVPTADYVAAEIEYGRPKITVDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTL 2813
Cdd:pfam00054 1 FRTTEPSGLLLYNGT---------QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 2814 SKpNSVETAETKSsvagGNKSVLNLNQQisrLFVGGVPTSARISKDL-YNRDFVGDIESLKLHGEPIG 2880
Cdd:pfam00054 72 DG-EARPTGESPL----GATTDLDVDGP---LYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2293-2845 |
3.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2293 EETLMTLEAASADqypekaqtvpgkLEEIQKKIQEetekLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNN 2372
Cdd:COG1196 175 EEAERKLEATEEN------------LERLEDILGE----LERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2373 iakmLQLTKVENLVAAITDDLERVEAakgEFQKLNVAIgnitENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRD 2452
Cdd:COG1196 239 ----AELEELEAELEELEAELEELEA---ELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2453 EKsvdmQLVNAKAHELHLQATTLRQTFDNNKDNTDQAvEAANAFSNLTDTLKNAKAQIDNAYEALSAEpafaesvQNARd 2532
Cdd:COG1196 308 EE----RRRELEERLEELEEELAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEA-------EAEL- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2533 kpfpDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKLKAEIDA 2612
Cdd:COG1196 375 ----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE--------ELEELEEALAELEEEEEEEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2613 NIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSdKVSQIKEMIA 2692
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2693 VARDAANRIKLGAHFEK--GSSLDLNIPQRVTRSAAHADISFYFRTEQEHGIPLFFgnEETAVGSRAVPTADYVAAEIEY 2770
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGA 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2771 GRPKITVDLGDAPAVVKLDtpVNDGLWRRLNIERI--GKTVSVTLSKPNSVETAETKSSVAGGNKSVLNLNQQISRL 2845
Cdd:COG1196 600 AVDLVASDLREADARYYVL--GDTLLGRTLVAARLeaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2316-2688 |
3.77e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2316 GKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKmlQLTKVENLVAAIT---DD 2392
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK--RLSRLEEEINGIEeriKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2393 LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRN-----------DVAEALEAAKKrvRRDEKSVDMQLV 2461
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeKLEKELEELEK--AKEEIEEEISKI 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2462 NAKAHELHLQATTLRQTFDN-----------NKDNTDQavEAANAFSNLTDTLKNA---KAQIDNAYEALSAEPAFAESV 2527
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEElkkakgkcpvcGRELTEE--HRKELLEEYTAELKRIekeLKEIEEKERKLRKELRELEKV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2528 QNARDKPFP-DETKEKIDAL-SKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYS--KNTLDSIDEKVQEV 2603
Cdd:PRK03918 489 LKKESELIKlKELAEQLKELeEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2604 EKLKAEID--------ANIEETRAKISEIagkaEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLssarSA 2675
Cdd:PRK03918 569 EEELAELLkeleelgfESVEELEERLKEL----EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET----EK 640
|
410
....*....|...
gi 808356960 2676 KVDSVSDKVSQIK 2688
Cdd:PRK03918 641 RLEELRKELEELE 653
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-658 |
3.85e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.53 E-value: 3.85e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCRGCEC 658
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
564-605 |
3.99e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 3.99e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2155-2697 |
5.99e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2155 DNLELEIDVLGTAIANI-SSATIVGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNS-------------- 2219
Cdd:TIGR02168 312 ANLERQLEELEAQLEELeSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskvaql 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2220 ----TQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEvMKRAQRARQSvRSLAEIALAIGSSSKAVNVDPRLLKEAEET 2295
Cdd:TIGR02168 392 elqiASLNNEIERLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQ-AELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2296 LMTLEAAsADQYPEKAQTVPGKLEEIQKkIQEETEKLDkqkETFEAQKKRAEELAAYLNSAQQLLK-ESKSKADKSNNIA 2374
Cdd:TIGR02168 470 LEEAEQA-LDAAERELAQLQARLDSLER-LQENLEGFS---EGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAALG 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2375 KMLQLTKVENLVAAIT--DDLERVEAAKGEFQKLNVAIGN-ITENLKDKREEMTHAVTTLNETR---------------- 2435
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllgg 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2436 ----NDVAEALEAAKKrVRRDEKSV--DMQLVNA------KAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTL 2503
Cdd:TIGR02168 625 vlvvDDLDNALELAKK-LRPGYRIVtlDGDLVRPggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2504 KNAKAQIDNAYEALSAEPAFAESVQNARDKPFPDETKEkIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKA 2583
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2584 GIpkyskntlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANS-----AMEGIRL------ARRNSVQL 2652
Cdd:TIGR02168 783 EI--------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerriAATERRLedleeqIEELSEDI 854
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 808356960 2653 NKLAPVIvskfEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA 2697
Cdd:TIGR02168 855 ESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSE 895
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
609-657 |
8.72e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.72e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 609 ACACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCR-GCE 657
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
656-703 |
1.20e-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: 61.99 E-value: 1.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 656 CECLLSGAKGQTCDSN-GQCYCKGNFEGERCDRCKPNFYNFPICEECNC 703
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
755-807 |
1.20e-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: 61.99 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808356960 755 SCDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRlNSYNQMGCE 807
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1517-1560 |
1.38e-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: 61.99 E-value: 1.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1517 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYGFP 1560
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2317-2647 |
1.41e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQ---EETEKLDKQKETFEAQKKRAE-ELAAYLNSAQQLLKESKSKADKSNNIAKMLQltKVENLVAAITDD 2392
Cdd:PRK03918 166 NLGEVIKEIKrriERLEKFIKRTENIEELIKEKEkELEEVLREINEISSELPELREELEKLEKEVK--ELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2393 LERVEAAKGEFQKLNVAIGNITENLKDKREEMthavttlnetrndvaEALEAAKKRVRRDEKSvdmqlvnAKAHElhlqa 2472
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEI---------------EELEEKVKELKELKEK-------AEEYI----- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2473 tTLRQTFDNNKDNTdQAVEaaNAFSNLTDTLKNAKAQIDNAyealsaepafaesvqnardkpfpDETKEKIDALSKTVSQ 2552
Cdd:PRK03918 297 -KLSEFYEEYLDEL-REIE--KRLSRLEEEINGIEERIKEL-----------------------EEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2553 DLKETEKLKKQLEQLTELSEKLrKRKEAVKAgipKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIt 2632
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKK-EELERLKK---RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL- 424
|
330
....*....|....*
gi 808356960 2633 ekaNSAMEGIRLARR 2647
Cdd:PRK03918 425 ---KKAIEELKKAKG 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2288-2685 |
1.67e-11 |
|
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: 70.86 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2288 LLKEAEETLMTLE--AASADQYPE-KAQtvpgkLEEIQK-----KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQL 2359
Cdd:TIGR02168 194 ILNELERQLKSLErqAEKAERYKElKAE-----LRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2360 LKEskskadksnniaKMLQLTKVEnlvaaitddlERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNEtrndVA 2439
Cdd:TIGR02168 269 LEE------------LRLEVSELE----------EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----LE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2440 EALEAAKKrvRRDEKSVDMQLVNAKAHELhlqattlrqtfdnnkdnTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALsa 2519
Cdd:TIGR02168 323 AQLEELES--KLDELAEELAELEEKLEEL-----------------KEELESLEAELEELEAELEELESRLEELEEQL-- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2520 epafaESVQNARdkpfpDETKEKIDALSKTVSQdlketekLKKQLEQLTELSEKLRKRKEAVKagiPKYSKNTLDSIDEK 2599
Cdd:TIGR02168 382 -----ETLRSKV-----AQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELL---KKLEEAELKELQAE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2600 VQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGI-----RLARRNSVQLNKLapvivSKFEELKKL---SS 2671
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLE-----GFSEGVKALlknQS 516
|
410
....*....|....
gi 808356960 2672 ARSAKVDSVSDKVS 2685
Cdd:TIGR02168 517 GLSGILGVLSELIS 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2322-2702 |
2.08e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2322 QKKIQEETEKLDKQKETFEAQKK----RAEElaaylnsaQQLLKESKSKAD---KSNNIAKMLQLTKVENlvAAITDDLE 2394
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKtetgKAEE--------ARKAEEAKKKAEdarKAEEARKAEDARKAEE--ARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEAAKGEFQKLNVAIGNITENLKdKREEMTHA--VTTLNETRN-DVAEALEAAKK--------RVRRDEKSVDMQLVNa 2463
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEDAK-KAEAARKAeeVRKAEELRKaEDARKAEAARKaeeerkaeEARKAEDAKKAEAVK- 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2464 KAHELHLQATTLRQTFD--NNKDNTDQAVEAANAFSNLTDTLKNAKA----QIDNAYEALSAEPAF-AESVQNARDKPFP 2536
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEerNNEEIRKFEEARMAHFARRQAAIKAEEArkadELKKAEEKKKADEAKkAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTldSIDEKVQEVEKLKAEIDANIEE 2616
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2617 TRAKISEIAGKAEEITEKANSaMEGIRLARRNSVQLNKLAPViVSKFEELKKlsSARSAKvdsvsdKVSQIKEMIAVARD 2696
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE-KKKADEAKK--KAEEAK------KADEAKKKAEEAKK 1458
|
....*.
gi 808356960 2697 AANRIK 2702
Cdd:PTZ00121 1459 AEEAKK 1464
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
756-799 |
2.36e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 756 CDCNVNGTISglNTCDLKTGQCMCKKNADGRRCDQCADGFYRLN 799
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
519-564 |
2.50e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFC 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
564-605 |
2.53e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2309-2696 |
2.56e-11 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 69.60 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2309 EKAQTVPGKLEEIQKKIQEETEKldkqKETFEAQKKRAEELAAYLNSAQQ-LLKESKSKADKSNNI----AKMLQLTKVE 2383
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLEI----FGLTLGLLKGISELKKAEPSGTVnSIKESETGNLGSESTllekAKEIINIEEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2384 NLV-AAITDDLERVEAAKGEFQKLNVAIGNI-TENLKDKREEMTHavttLNETRNDVAEALEAAKKRVRRDEKSVDMQLV 2461
Cdd:COG5185 235 LKGfQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKR----LNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2462 NAKAHELhLQATTLRQTFDNNKDNTDQAVEaanafsNLTDTLKNAKAQIDNAYEALSAEpafAESVQNARDKPfpdETKE 2541
Cdd:COG5185 311 TESLEEQ-LAAAEAEQELEESKRETETGIQ------NLTAEIEQGQESLTENLEAIKEE---IENIVGEVELS---KSSE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALSKTVsqdlketEKLKKQLEQLtelseklrkrkeavkagipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKI 2621
Cdd:COG5185 378 ELDSFKDTI-------ESTKESLDEI---------------------PQNQRGYAQEILATLEDTLKAADRQIEELQRQI 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2622 SEIAGKAEEITEKANSAMEGIRLARRnSVQLNKLAPVIvskfEELKKLSSARSAKVDSVSDKVSQIKEMIAVARD 2696
Cdd:COG5185 430 EQATSSNEEVSKLLNELISELNKVMR-EADEESQSRLE----EAYDEINRSVRSKKEDLNEELTQIESRVSTLKA 499
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2309-2679 |
2.96e-11 |
|
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: 69.82 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2309 EKAQTVPGKLEEIQKKIQ---EE----TEKLDKQKETF-EAQKKRA---------EELAAYLNS--------AQQLLKES 2363
Cdd:pfam01576 19 ERQQKAESELKELEKKHQqlcEEknalQEQLQAETELCaEAEEMRArlaarkqelEEILHELESrleeeeerSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2364 K----------SKADKSNNIAKMLQLTKV--ENLVAAITDDLERVEAAKGEFQK----LNVAIGNITENLKDKREEmtha 2427
Cdd:pfam01576 99 KkmqqhiqdleEQLDEEEAARQKLQLEKVttEAKIKKLEEDILLLEDQNSKLSKerklLEERISEFTSNLAEEEEK---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2428 VTTLNETRNDVAEALEAAKKRVRRDEKSvDMQLVNAK------AHELHLQATTLRQTFDN------NKDNTDQAV----- 2490
Cdd:pfam01576 175 AKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKrklegeSTDLQEQIAELQAQIAElraqlaKKEEELQAAlarle 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2491 EAANAFSNLTDTLKNAKAQIDNAYEALSAEPAfaesvqnARDKpfpdETKEKidalsktvsQDL-KETEKLKKQLEQL-- 2567
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERA-------ARNK----AEKQR---------RDLgEELEALKTELEDTld 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2568 -TELSEKLRKRKEavkagipkyskntldsidekvQEVEKLKAEIDaniEETRAKISEIAgkaeEITEKANSAM----EGI 2642
Cdd:pfam01576 314 tTAAQQELRSKRE---------------------QEVTELKKALE---EETRSHEAQLQ----EMRQKHTQALeeltEQL 365
|
410 420 430
....*....|....*....|....*....|....*...
gi 808356960 2643 RLARRNSVQLNKLAPVIVSKFEELKK-LSSARSAKVDS 2679
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAeLRTLQQAKQDS 403
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2251-2708 |
3.00e-11 |
|
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: 69.29 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2251 LQEvMKRAQRARQSVRSLAEIALAIGSSSKAVNvDPRLLKEAEETL---MTLEAASADQYPEKAQTVPGKLEEIQKKIQE 2327
Cdd:pfam05701 107 VEE-MEQGIADEASVAAKAQLEVAKARHAAAVA-ELKSVKEELESLrkeYASLVSERDIAIKRAEEAVSASKEIEKTVEE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2328 ETEKLDKQKETFEAQKkraeelAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVE------NLVAAitDDLE-RVEAAK 2400
Cdd:pfam05701 185 LTIELIATKESLESAH------AAHLEAEEHRIGAALAREQDKLNWEKELKQAEEElqrlnqQLLSA--KDLKsKLETAS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2401 GEFQKLNVAIGNITENlkdKREEMTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHELHLQATTLRQTFD 2480
Cdd:pfam05701 257 ALLLDLKAELAAYMES---KLKEEADGEGNEKKTSTSIQAALASAKKEL--EEVKANIEKAKDEVNCLRVAAASLRSELE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2481 NNKDNTD----QAVEAANAFSNLTDTLKNAKAQIdnayealsaepafaESVQnARDKpfpdETKEKIDALSKTVSQDLKE 2556
Cdd:pfam05701 332 KEKAELAslrqREGMASIAVSSLEAELNRTKSEI--------------ALVQ-AKEK----EAREKMVELPKQLQQAAQE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2557 TEKLKKqLEQLTElsEKLRKRKEavKAGIPKYSKNTLDSIDEKVQ-EVEKLKAE-------IDANIE-ETRAKISEIAGK 2627
Cdd:pfam05701 393 AEEAKS-LAQAAR--EELRKAKE--EAEQAKAAASTVESRLEAVLkEIEAAKASeklalaaIKALQEsESSAESTNQEDS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2628 AEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKlSSARS-AKVDSVSDKVSQIKEMIAVARDAANRI---KL 2703
Cdd:pfam05701 468 PRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKE-SELRSlEKLEEVNREMEERKEALKIALEKAEKAkegKL 546
|
....*
gi 808356960 2704 GAHFE 2708
Cdd:pfam05701 547 AAEQE 551
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2160-2616 |
4.38e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2160 EIDVLGTAIANISsATIVGARLARN--KKEFNDINEITKMLNDEENSF--GNVFGDA--------QDILTNS-TQIQNKL 2226
Cdd:PRK02224 252 ELETLEAEIEDLR-ETIAETEREREelAEEVRDLRERLEELEEERDDLlaEAGLDDAdaeavearREELEDRdEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2227 VRTKTHSQNSVSSAKNITLNGTEfLQEvmkRAQRARQSVRSL-AEIALAigssskAVNVDPR--LLKEAEETLMTLEAAS 2303
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADD-LEE---RAEELREEAAELeSELEEA------REAVEDRreEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2304 ADqypekAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELaayLNSAQQLLKESK---------------SKAD 2368
Cdd:PRK02224 401 GD-----APVDLGNAEDFLEELREERDELREREAELEATLRTARER---VEEAEALLEAGKcpecgqpvegsphveTIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2369 KSNNIAKM-LQLTKVENLVAAITDDLERVEAAK---GEFQKLNVAIGNITENLKDKREemthavtTLNETRndvaeaLEA 2444
Cdd:PRK02224 473 DRERVEELeAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRE-------TIEEKR------ERA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2445 AKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQ---TFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSA-- 2519
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAla 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2520 --------------------EPAFAES-VQNARDK-----PFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTElsek 2573
Cdd:PRK02224 620 elnderrerlaekrerkrelEAEFDEArIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE---- 695
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 808356960 2574 LRKRKEAVKAgipkySKNTLDSIDEKVQEVE----KLKAEIDA-NIEE 2616
Cdd:PRK02224 696 LRERREALEN-----RVEALEALYDEAEELEsmygDLRAELRQrNVET 738
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2156-2624 |
4.95e-11 |
|
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: 69.43 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2156 NLELEIDVLGTAIANISSATIVGARLaRNKKEfNDINEITKMLNDEENSFgnvfgdaqdiltnSTQIQNklVRTKtHSQn 2235
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQEL-RSKRE-QEVTELKKALEEETRSH-------------EAQLQE--MRQK-HTQ- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2236 svssaknitlnGTEFLQEVMKRAQRARQSvrsLAEIALAIGSSSKAVNVDPRLL-----------KEAEETLMTLEAASA 2304
Cdd:pfam01576 357 -----------ALEELTEQLEQAKRNKAN---LEKAKQALESENAELQAELRTLqqakqdsehkrKKLEGQLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2305 DQYPEKAQtvpgkLEEIQKKIQEETEKLDKQKETFEAQ----KKRAEELAAYLNSAQQLLKESKSKadKSNNIAKMLQLt 2380
Cdd:pfam01576 423 ESERQRAE-----LAEKLSKLQSELESVSSLLNEAEGKniklSKDVSSLESQLQDTQELLQEETRQ--KLNLSTRLRQL- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2381 kvENLVAAITDDLERVEAAKGEFQK----LNVAIgnitENLKDKREEMTHAVttlnetrndvaEALEAAKKRVRRDEKSV 2456
Cdd:pfam01576 495 --EDERNSLQEQLEEEEEAKRNVERqlstLQAQL----SDMKKKLEEDAGTL-----------EALEEGKKRLQRELEAL 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2457 DMQLVN--AKAHELHLQATTLRQTFDN---NKDNTDQAVEA----ANAFSNLTDTLKNAKAQidNAYEALSAEpafAEsv 2527
Cdd:pfam01576 558 TQQLEEkaAAYDKLEKTKNRLQQELDDllvDLDHQRQLVSNlekkQKKFDQMLAEEKAISAR--YAEERDRAE---AE-- 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2528 qnARDKpfpdETKekidALSktvsqdlketekLKKQLEQLTELSEKLRKRKEAVKAGIPKY--SKntlDSIDEKVQEVEK 2605
Cdd:pfam01576 631 --AREK----ETR----ALS------------LARALEEALEAKEELERTNKQLRAEMEDLvsSK---DDVGKNVHELER 685
|
490
....*....|....*....
gi 808356960 2606 LKAEIDANIEETRAKISEI 2624
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEEL 704
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1517-1562 |
9.09e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.09e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 1517 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYG--FPHC 1562
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2048-2092 |
9.36e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 2048 CHCGTA-AFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHGC 2092
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2494-2702 |
1.20e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2494 NAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTEL 2570
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL--EEVLREINEISSelpELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2571 SEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKlkaeidaNIEETRAKISEIAGKAEEITEKANSAMEGIRlarrnsv 2650
Cdd:PRK03918 240 IEELEKELESLEG--------SKRKLEEKIRELEE-------RIEELKKEIEELEEKVKELKELKEKAEEYIK------- 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2651 qLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:PRK03918 298 -LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2209-2702 |
1.25e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2209 FGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSvrsLAEIALAIGSSSKAVNVDPRL 2288
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYpEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKAD 2368
Cdd:TIGR02168 360 LEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2369 KSN--NIAKML-----QLTKVENLVAAITDDLERVE----AAKGEFQKLNVAIgNITENLKDKREEMTHAVTTLNETRND 2437
Cdd:TIGR02168 439 QAEleELEEELeelqeELERLEEALEELREELEEAEqaldAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2438 VAEALEAAKKRVRRDEK-----------SVDMQLVN-----AKAHELHLQATTLRQTF---DNNKDNTDQA--------- 2489
Cdd:TIGR02168 518 LSGILGVLSELISVDEGyeaaieaalggRLQAVVVEnlnaaKKAIAFLKQNELGRVTFlplDSIKGTEIQGndreilkni 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2490 ----------VEAANAFSNL----------TDTLKNAKAQIDNAYE----------------ALSAEPAFAESVQNARDK 2533
Cdd:TIGR02168 598 egflgvakdlVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPgyrivtldgdlvrpggVITGGSAKTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2534 PFpDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpKYSKNTLDSIDEKVQEVEKLKAEIDAN 2613
Cdd:TIGR02168 678 EI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2614 IEETRAKISEIAGKAEEITEKANSAMEGI-----RLARRNSvQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIK 2688
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIeeleaQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
570
....*....|....
gi 808356960 2689 EMIAVARDAANRIK 2702
Cdd:TIGR02168 835 ATERRLEDLEEQIE 848
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2289-2702 |
1.52e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 67.93 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAaSADQYPEKAQTVPGKLEEiqKKIQEETEKlDKQKETFEAQKKRAEELaayLNSAQQLLKESKSKAD 2368
Cdd:PTZ00440 1079 IKLLEEKVEALLK-KIDENKNKLIEIKNKSHE--HVVNADKEK-NKQTEHYNKKKKSLEKI---YKQMEKTLKELENMNL 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2369 ---KSNNIAKM-LQLTK--VENLVAAITDDLERveaAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETR-NDVAEA 2441
Cdd:PTZ00440 1152 ediTLNEVNEIeIEYERilIDHIVEQINNEAKK---SKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAyYDKATA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2442 LEAakkrvrrdeksvdmqlvnaKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNL------TDTLKNAKAQIDNAYE 2515
Cdd:PTZ00440 1229 SYE-------------------NIEELTTEAKGLKGEANRSTNVDELKEIKLQVFSYLqqvikeNNKMENALHEIKNMYE 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2516 ALsaepafaesvqnardkpfpdeTKEKIDALSKTVSQDLKETE----KLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKN 2591
Cdd:PTZ00440 1290 FL---------------------ISIDSEKILKEILNSTKKAEefsnDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGS 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2592 TLD-SIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARrnsvqlnklapvIVSKFEELKKlS 2670
Cdd:PTZ00440 1349 LEDkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKID------------FLNKHEAIEP-S 1415
|
410 420 430
....*....|....*....|....*....|..
gi 808356960 2671 SARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:PTZ00440 1416 NSKEVNIIKITDNINKCKQYSNEAMETENKAD 1447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2341-2586 |
1.73e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2341 AQKKRAEELAAYLNSAQQLLKESKSKADKsnniakmlQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDK 2420
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2421 REEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVdmqLVNAK-AHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNL 2499
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL---LLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2500 TDTLKNAKAQIDNAYEALSAEPAFAESVQNARdkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKE 2579
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER--------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*..
gi 808356960 2580 AVKAGIP 2586
Cdd:COG4942 238 AAAERTP 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2095-2140 |
2.07e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.07e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGC 2140
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2287-2689 |
2.11e-10 |
|
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: 67.12 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2287 RLLKEaEETLMTLEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKEsksk 2366
Cdd:pfam01576 195 RLKKE-EKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE---- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2367 adksnniakmlqltkVENLVAAITDDL--ERVEAAKGEFQKlnvaignitenlKDKREEMTHAVTTLNETRNDVAEALEA 2444
Cdd:pfam01576 269 ---------------LEAQISELQEDLesERAARNKAEKQR------------RDLGEELEALKTELEDTLDTTAAQQEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2445 AKKR---VRRDEKSVDMQlvnAKAHELHLQATTLRQTfdnnkdntdQAVEaanAFSNLTDTLKNAKAQIDNAYEALSAEP 2521
Cdd:pfam01576 322 RSKReqeVTELKKALEEE---TRSHEAQLQEMRQKHT---------QALE---ELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2522 AfaesvqnardkpfpdETKEKIdalsKTVSQDLKETEKLKKQLE-QLTELSEKL----RKRKEAVKagipKYSK--NTLD 2594
Cdd:pfam01576 387 A---------------ELQAEL----RTLQQAKQDSEHKRKKLEgQLQELQARLseseRQRAELAE----KLSKlqSELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2595 SIDEKVQEVEK--LKAEIDANI-------------EETRAKISeIAGKAEEITEKANSAMEgiRL-----ARRNsvqLNK 2654
Cdd:pfam01576 444 SVSSLLNEAEGknIKLSKDVSSlesqlqdtqellqEETRQKLN-LSTRLRQLEDERNSLQE--QLeeeeeAKRN---VER 517
|
410 420 430
....*....|....*....|....*....|....*
gi 808356960 2655 LAPVIVSKFEELKKlssarsaKVDSVSDKVSQIKE 2689
Cdd:pfam01576 518 QLSTLQAQLSDMKK-------KLEEDAGTLEALEE 545
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2155-2603 |
2.19e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2155 DNLELEIDVLGTAIANISsativgARLARNKKEFNDINEITKMLNDEEnsfgnvfgdaQDILTNSTQIQNKLVRtkthsq 2234
Cdd:TIGR02168 680 EELEEKIEELEEKIAELE------KALAELRKELEELEEELEQLRKEL----------EELSRQISALRKDLAR------ 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2235 nsvssaknitlngteFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTV 2314
Cdd:TIGR02168 738 ---------------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2315 PGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQllkeskSKADKSNNIAKM-LQLTKVENLVAAITDDL 2393
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE------QIEELSEDIESLaAEIEELEELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2394 ERVEAAKGEFQklnvaignitENLKDKREEMTHAVTTLNETRNDVAEALEaakkrvrrdeksvDMQLVNAKAHELHLQAT 2473
Cdd:TIGR02168 876 EALLNERASLE----------EALALLRSELEELSEELRELESKRSELRR-------------ELEELREKLAQLELRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2474 TLRQTFDNNKDntdqaveaanAFSNLtdtlknakaQIDNAYEALSAEPAFAESVQNARDKpfPDETKEKIDALSK---TV 2550
Cdd:TIGR02168 933 GLEVRIDNLQE----------RLSEE---------YSLTLEEAEALENKIEDDEEEARRR--LKRLENKIKELGPvnlAA 991
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2551 SQDLKETEK----LKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEV 2603
Cdd:TIGR02168 992 IEEYEELKErydfLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
519-566 |
2.72e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.72e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFCNC 566
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2317-2643 |
3.00e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADksnniakmlqLTKVENLVAAITDDLERV 2396
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID----------VASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2397 EAAKGEFQKLnvaigniTENLKDKREEMTHAVTTLNETRNDVAEaLEAAKKRVRRDEKSVDMQLVNAKAhelhLQATTLR 2476
Cdd:COG4913 681 DASSDDLAAL-------EEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAED----LARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2477 QTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNardkpFPDETKEKIDALSktvsqDLKE 2556
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL--ERAMRAFNRE-----WPAETADLDADLE-----SLPE 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2557 TEKLKKQLEQ--LTELSEKLRKRKEavkagipkysKNTldsidekVQEVEKLKAEIDANIEETRAKISEIagkaeeitek 2634
Cdd:COG4913 817 YLALLDRLEEdgLPEYEERFKELLN----------ENS-------IEFVADLLSKLRRAIREIKERIDPL---------- 869
|
....*....
gi 808356960 2635 aNSAMEGIR 2643
Cdd:COG4913 870 -NDSLKRIP 877
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2293-2633 |
3.08e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.79 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2293 EETLMTLEAAsaDQYPEKAQTVPGKLEEIQKKIQEETEKL----DKQKETFEAQKKRAEELAAYLNSAQQLLKE------ 2362
Cdd:pfam12128 460 PELLLQLENF--DERIERAREEQEAANAEVERLQSELRQArkrrDQASEALRQASRRLEERQSALDELELQLFPqagtll 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2363 ---SKSKADKSNNIAKML---QLTKvenlvaaiTD-DLERVEAAKGefQKLNVaiGNITENLKDKREEMTHAVT-TLNET 2434
Cdd:pfam12128 538 hflRKEAPDWEQSIGKVIspeLLHR--------TDlDPEVWDGSVG--GELNL--YGVKLDLKRIDVPEWAASEeELRER 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2435 RNDVAEALEAAKKRVRRDEKSvdMQLVNAKAHELHLQATTLRQTFDNNKDNTDQaveaanafsnLTDTLKNAKAQIDnay 2514
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQ--LVQANGELEKASREETFARTALKNARLDLRR----------LFDEKQSEKDKKN--- 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2515 EALSAEPAFAESVQNARD----------KPFPDETKEKIDALSKTVSQDLKETEKLKKqlEQLTELSEKLRKRKEAVKA- 2583
Cdd:pfam12128 671 KALAERKDSANERLNSLEaqlkqldkkhQAWLEEQKEQKREARTEKQAYWQVVEGALD--AQLALLKAAIAARRSGAKAe 748
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2584 --GIPKYSKNTLDSIDEKVQEVEKLKAEidanIEETRAKISEIAGKAEEITE 2633
Cdd:pfam12128 749 lkALETWYKRDLASLGVDPDVIAKLKRE----IRTLERKIERIAVRRQEVLR 796
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3566-3683 |
3.79e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 60.41 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3566 NGILFSVGV---LEYITVEFVNGSIKTTVESGSGGEELWHHPDIenqyCDGQWQSFKISKKRNLLTVAVNGKAHLKI--L 3640
Cdd:pfam00054 7 SGLLLYNGTqteRDFLALELRDGRLEVSYDLGSGAAVVRSGDKL----NDGKWHSVELERNGRSGTLSVDGEARPTGesP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 808356960 3641 KKAKTDVLTKDPLYFGGLPEGVTNKGIKTN-KPFVGCIRFVSFG 3683
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2325-2702 |
4.10e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2325 IQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQL--LKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKG 2401
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEkRQQLerLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2402 EFQKLNVAIGNITENLKDKREEMthavttlnetrNDVAEALEAAKKRVRrDEKSVDMQLVNAKAHELHLQATTLRQTFDN 2481
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRL-----------EEIEQLLEELNKKIK-DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2482 NKDNTDQAVEaanafsnltdTLKNAKAQIDNayealsaepafaesvqnardkpfpdeTKEKIDALSKtvsqdlkETEKLK 2561
Cdd:TIGR02169 313 KERELEDAEE----------RLAKLEAEIDK--------------------------LLAEIEELER-------EIEEER 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2562 KQLEQLTELSEKLRKRKEavkagipkyskntldsidEKVQEVEklkaEIDANIEETRAKISEIAGKAEEITEKANSAMEG 2641
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELE------------------DLRAELE----EVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 2642 IR----LARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSD---KVSQIKEMIAVARDAANRIK 2702
Cdd:TIGR02169 408 LDrlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewKLEQLAADLSKYEQELYDLK 475
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
471-520 |
4.75e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.36 E-value: 4.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 471 PCECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTAGCVECV 520
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2253-2687 |
5.03e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.02 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2253 EVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLE---AASADQYPEKAQTVPGKL----EEIQKKi 2325
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNGELsaadAAVAKD- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2326 QEETEKLDKQKETFeaQKKRAEELAAYLNSAQQ-------LLKESKSKADKSNNIAK---MLQLTKVENLVAAITDDLER 2395
Cdd:pfam12128 321 RSELEALEDQHGAF--LDADIETAAADQEQLPSwqselenLEERLKALTGKHQDVTAkynRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2396 VEAAKGEFQKLNVAIGNITENLKDK-REEMTHAVTTLNETRNDVAEALEAAKKRVRRdeksvdmqlVNAKAHELhlqaTT 2474
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ---------ATATPELL----LQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2475 LRQtFDNNKDNTDQAVEAANA-FSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARdkpfpDETKEKIDALSKTVSQD 2553
Cdd:pfam12128 466 LEN-FDERIERAREEQEAANAeVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-----DELELQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2554 L-KETEKLKKQLEQLteLSEKLRKR--------KEAVKAGIPKYSKN-TLDSID--EKVQEVEKLKAEIDA--------- 2612
Cdd:pfam12128 540 LrKEAPDWEQSIGKV--ISPELLHRtdldpevwDGSVGGELNLYGVKlDLKRIDvpEWAASEEELRERLDKaeealqsar 617
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2613 -NIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNklapviVSKFEELKKLSSARSAKVDSVSDKVSQI 2687
Cdd:pfam12128 618 eKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLF------DEKQSEKDKKNKALAERKDSANERLNSL 687
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-656 |
5.13e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 5.13e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPdCRGC 656
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2179-2750 |
5.29e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.76 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2179 ARLARNKKEFND-----INEITKMLNDEENSFGNVFGDAQDILTNSTQI---QNKLVRTKTHSQNSVSSAKNITLNGTEF 2250
Cdd:pfam02463 179 IEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2251 LQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETE 2330
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2331 KLDKQKEtfEAQKKRAEELAAYLNSAQQLLKESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLER-VEAAKGEFQK 2405
Cdd:pfam02463 339 ELEKELK--ELEIKREAEEEEEEELEKLQEKLEQLEEEllakKKLESERLSSAAKLKEEELELKSEEEKeAQLLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2406 LNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQtfdnnKDN 2485
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-----LLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2486 TDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSaepafaESVQNARDKPFPDETKEKIDALSKTVSQDlketEKLKKQLE 2565
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRI------ISAHGRLGDLGVAVENYKVAISTAVIVEV----SATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2566 QltelseklRKRKEAVKAGIPKYsKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLA 2645
Cdd:pfam02463 562 E--------RQKLVRALTELPLG-ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2646 RRNSVQLNKLAPVIVS-KFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA---ANRIKLGAHFEKGSSLDLNIPQRV 2721
Cdd:pfam02463 633 ELTKLKESAKAKESGLrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAeseLAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590
....*....|....*....|....*....|
gi 808356960 2722 TRSAAHADISF-YFRTEQEHGIPLFFGNEE 2750
Cdd:pfam02463 713 KKLKLEAEELLaDRVQEAQDKINEELKLLK 742
|
|
| CBM6-CBM35-CBM36_like |
cd02795 |
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ... |
855-988 |
5.56e-10 |
|
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.
Pssm-ID: 271143 Cd Length: 124 Bit Score: 59.89 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 855 QYEAEDAHTEDQKPVRFA---VDPEQFADFSWRGYAVFSPiqdkilidVDITKATVYRLLFRYRNPTSVPV-TATVTINP 930
Cdd:cd02795 1 RIEAEDATLTGGTAVSTAagaSGGGYVIGFSSGGDSVTFT--------VTVPKAGTYRLAVRYASPNGNGSrSVSLDGNG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 931 RFTHTHDVEQTGkatFAPGDLPAMKEITVDgkpfvlNPGKWSLAISTKQ---RLFLDYVVV 988
Cdd:cd02795 73 KLVGTITVPSTG---GWDTWGTASVSVNLP------DAGGHTLKIVGTGdngGANIDYVVV 124
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2152-2740 |
5.72e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 66.23 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2152 GDVDNL--ELEIDVLGTAIANISSATivgaRLARNKKEFNdiNEITKMLNDEENSfgnVFGDAQDILTNSTQIQNKLVRT 2229
Cdd:TIGR01612 671 DDIDALynELSSIVKENAIDNTEDKA----KLDDLKSKID--KEYDKIQNMETAT---VELHLSNIENKKNELLDIIVEI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2230 KTHSQNSVSSAKNITLNG-----TEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLmtleaasa 2304
Cdd:TIGR01612 742 KKHIHGEINKDLNKILEDfknkeKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNY-------- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2305 DQYPEKAQTVPGKLEEIQKKIQE---------------------ETEKLDKQKETFE--AQKKRAEELAAYLNSAQQLLK 2361
Cdd:TIGR01612 814 DKSKEYIKTISIKEDEIFKIINEmkfmkddflnkvdkfinfennCKEKIDSEHEQFAelTNKIKAEISDDKLNDYEKKFN 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2362 ESKSKADKSNN-IAKMLQ----LTKVENLVAAITDDLERVEAAKGEFQKLNvaignitenlkdkrEEMTHAVTTLNET-- 2434
Cdd:TIGR01612 894 DSKSLINEINKsIEEEYQnintLKKVDEYIKICENTKESIEKFHNKQNILK--------------EILNKNIDTIKESnl 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2435 -----RNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNT--DQAVEAANAFSNLTDTLKNAK 2507
Cdd:TIGR01612 960 ieksyKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyHQFDEKEKATNDIEQKIEDAN 1039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2508 AQIDNAyealsaEPAFAESVQNARDKpFPDETKEKIDALSKTVsqdlkeTEKLKKQLEQLTELSEKLRKRK--EAVKAGI 2585
Cdd:TIGR01612 1040 KNIPNI------EIAIHTSIYNIIDE-IEKEIGKNIELLNKEI------LEEAEINITNFNEIKEKLKHYNfdDFGKEEN 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2586 PKYS----------KNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIagkaEEITEKA--NSAMEGIRLARRNSV--- 2650
Cdd:TIGR01612 1107 IKYAdeinkikddiKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDL----EDVADKAisNDDPEEIEKKIENIVtki 1182
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2651 --------QLNKLAPVIV------SKFEELK--KLSSARS------AKVDSVSDKVSQ-IKEMIAVARDAANRIKLGAHF 2707
Cdd:TIGR01612 1183 dkkkniydEIKKLLNEIAeiekdkTSLEEVKgiNLSYGKNlgklflEKIDEEKKKSEHmIKAMEAYIEDLDEIKEKSPEI 1262
|
650 660 670
....*....|....*....|....*....|....
gi 808356960 2708 EKGSSLDLNIPQRV-TRSAAHADISFYFRTEQEH 2740
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMeTFNISHDDDKDHHIISKKH 1296
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2539-2842 |
8.38e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.77 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2539 TKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpKYSKNTLDSIDEKVQEVEKLKAEIDANIEETR 2618
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL-EQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2619 AKISEIAGKAEEITEKANSamegirlARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAA 2698
Cdd:COG4372 101 EELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2699 NRIKLGAHFEKGSSLDLNIPQRVTRSAAHAD-----ISFYFRTEQEHGIPLFFGNEETAVGSRAVPTADY---VAAEIEY 2770
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEaekliESLPRELAEELLEAKDSLEAKLGLALSALLDALEleeDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2771 GRPKITVDLGDAPAVVKLDTPVNDGLWRRL-----------NIERIGKTVSVTLSKPNSVETAETKSSVAGGNKSVLNLN 2839
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALelealeeaaleLKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
...
gi 808356960 2840 QQI 2842
Cdd:COG4372 334 ILL 336
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
656-696 |
8.71e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFP 696
Cdd:cd00055 2 CDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2048-2091 |
8.97e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 808356960 2048 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHG 2091
Cdd:cd00055 2 CDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2317-2696 |
1.21e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEetekLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADK----SNNIAKMLQLTKVENLVAAITDD 2392
Cdd:COG4717 72 ELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleklLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2393 LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLN-ETRNDV------AEALEAAKKRVRRDEKSVDMQLVNAKA 2465
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELqdlaeeLEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2466 HELHLQATTLRQtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYE-----ALSAEPAFAESVQNARDKPFPDETK 2540
Cdd:COG4717 228 ELEQLENELEAA---ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2541 EKIDALSKtvSQDLKEteklkkqlEQLTELSEKLRKRKEAVKAGIPKYSKnTLDSIDEKVQEVEKLKAEIDanIEETRAK 2620
Cdd:COG4717 305 EELQALPA--LEELEE--------EELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEELQ--LEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2621 ISEIAGKA-----EEITEKANSAMEGIRLARRNSV---QLNKLAPVIVS------------KFEELKKLSSARSAKVDSV 2680
Cdd:COG4717 372 IAALLAEAgvedeEELRAALEQAEEYQELKEELEEleeQLEELLGELEEllealdeeeleeELEELEEELEELEEELEEL 451
|
410
....*....|....*.
gi 808356960 2681 SDKVSQIKEMIAVARD 2696
Cdd:COG4717 452 REELAELEAELEQLEE 467
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1840-1883 |
1.23e-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: 56.21 E-value: 1.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 1840 PCECNGHSA---TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1883
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2183-2691 |
1.73e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 64.30 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2183 RNKKEFNDI-NEITKMLN-----DEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKN--ITLNgteflQEV 2254
Cdd:TIGR01612 1511 KNKELFEQYkKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKekFRIE-----DDA 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2255 MK--RAQRA----RQSVRSLAEIALAIGSSSKAVNvdpRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEeiqkKIQEE 2328
Cdd:TIGR01612 1586 AKndKSNKAaidiQLSLENFENKFLKISDIKKKIN---DCLKETESIEKKISSFSIDSQDTELKENGDNLN----SLQEF 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2329 TEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSK-----ADKSNNIAKM----LQLTK------VENLVAAI-TDD 2392
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIAnkeeIESIKelieptIENLISSFnTND 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2393 LERVEAAKgEFQKLNVAIGNITENLKDKREEMTHAVTTL-------NETRNDVAEALEAAKKRVRRDEKSvDMQLVNAKA 2465
Cdd:TIGR01612 1739 LEGIDPNE-KLEEYNTEIGDIYEEFIELYNIIAGCLETVskepityDEIKNTRINAQNEFLKIIEIEKKS-KSYLDDIEA 1816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2466 HELHLQATTLRQTFDNNKDN-TDQAVEAANAFSNLTDTLKNAKAQID------------NAYEAL----------SAEPA 2522
Cdd:TIGR01612 1817 KEFDRIINHFKKKLDHVNDKfTKEYSKINEGFDDISKSIENVKNSTDenllfdilnktkDAYAGIigkkyysykdEAEKI 1896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2523 F------AES----VQNARDKPFPDETkeKIDALSkTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAV------KAGIP 2586
Cdd:TIGR01612 1897 FinisklANSiniqIQNNSGIDLFDNI--NIAILS-SLDSEKEDTLKFIPSPEKEPEIYTKIRDSYDTLldifkkSQDLH 1973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2587 KYSKNTLDSIDEKVQEVEKLKAEidaniEETRAKISEIAGKAEEITekansamegirlarrNSVQLnklapvIVSKFEEL 2666
Cdd:TIGR01612 1974 KKEQDTLNIIFENQQLYEKIQAS-----NELKDTLSDLKYKKEKIL---------------NDVKL------LLHKFDEL 2027
|
570 580
....*....|....*....|....*..
gi 808356960 2667 KKLsSARSAKVDSV--SDKVSQIKEMI 2691
Cdd:TIGR01612 2028 NKL-SCDSQNYDTIleLSKQDKIKEKI 2053
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
808-854 |
1.91e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.91e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 808 SCHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHYFPTLWHN 854
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
656-701 |
2.06e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFPiCEEC 701
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2290-2640 |
3.22e-09 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 62.85 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2290 KEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEelaaylNSAQQLLKESKSKADK 2369
Cdd:pfam09731 102 AEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAV------KAHTDSLKEASDTAEI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2370 SNNIAKMLQLTKVEnlvAAITDDLERVEAAK-GEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRnDVAEALEAAKKR 2448
Cdd:pfam09731 176 SREKATDSALQKAE---ALAEKLKEVINLAKqSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQ-SLAKLVDQYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2449 VRRDEKSVDMQLV--------NAKAHELhLQATTLRQTFDNNKDNTDQAVEA-----ANAFSNLTDTLKNAKAQIDNAYE 2515
Cdd:pfam09731 252 VASERIVFQQELVsifpdiipVLKEDNL-LSNDDLNSLIAHAHREIDQLSKKlaelkKREEKHIERALEKQKEELDKLAE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2516 ALSAEpafAESVQNARDKPFPDETKEKIDALSKtvsqdlKETEKLKKQLEQLTE-LSEKLRKRkeavkagipkyskntld 2594
Cdd:pfam09731 331 ELSAR---LEEVRAADEAQLRLEFEREREEIRE------SYEEKLRTELERQAEaHEEHLKDV----------------- 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2595 sidEKVQEVE---KLKAEIDANIEETRA----KISEIAGKAEEItEKA---NSAME 2640
Cdd:pfam09731 385 ---LVEQEIElqrEFLQDIKEKVEEERAgrllKLNELLANLKGL-EKAtssHSEVE 436
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2257-2690 |
3.50e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 62.58 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2257 RAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQ---YPEKAQtvpgKLEE-IQKKIQEEtekL 2332
Cdd:pfam02029 11 RRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeaFLDRTA----KREErRQKRLQEA---L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2333 DKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlqltkveNLVAAITDDLERVEAakgEFQKLNVAIGN 2412
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDS-----------RLGRYKEEETEIREK---EYQENKWSTEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2413 ITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvRRDEKSVDMqlvnakahelhlqattlRQTFDNNKDNTDQAVEA 2492
Cdd:pfam02029 150 RQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIK-KEKKVKYES-----------------KVFLDQKRGHPEVKSQN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2493 ANAFSNLTDTLKNAKAQIDNAYEALSAEpafAESVQNARDKpfpdetKEKID-ALSKTVSQdlkETEKLK-KQLEQLTEL 2570
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQEREEE---AEVFLEAEQK------LEELRrRRQEKESE---EFEKLRqKQQEAELEL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2571 SEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVE---KLKAEID---ANIEETRAKISEIaGKAEE-------------- 2630
Cdd:pfam02029 280 EELKKKREERRKLLEEEEQRRKQEEAERKLREEEekrRMKEEIErrrAEAAEKRQKLPED-SSSEGkkpfkcfspkgssl 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2631 -ITEKANSAMEGirLARRNSVQLNKlAPVIVSKFE------------ELKKLSSARSAKVD--SVSDKVSQIKEM 2690
Cdd:pfam02029 359 kITERAEFLNKS--LQKSSSVKKTH-PPAVVSKIDsrleqytsaiesSTKEAKPTKPAASDlpVPAEGVRNIKSM 430
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1841-1888 |
3.58e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 3.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 1841 CECNGH---SATCDPDTGICtDCEHNTNGDHCEFCNEGHYGNAtNGSPYDC 1888
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2295-2533 |
3.60e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2295 TLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQketfeaqkkrAEELAAYLNSAQQLLKESKSKADKSNNia 2374
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAE----------LEELNEEYNELQAELEALQAEIDKLQA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2375 kmlQLTKVENLVAAITDDL-ERVEAAK---GEFQKLNVAIGNitENLKD--KReemTHAVTTLNETRNDVAEALEAAKKR 2448
Cdd:COG3883 73 ---EIAEAEAEIEERREELgERARALYrsgGSVSYLDVLLGS--ESFSDflDR---LSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2449 VRRDEKSVDMQLVNAKAhelhlqattLRQTFDNNKDNTDQAVEAANAfsnLTDTLKNAKAQIDNAYEALSAEPAFAESVQ 2528
Cdd:COG3883 145 LEAKKAELEAKLAELEA---------LKAELEAAKAELEAQQAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
....*
gi 808356960 2529 NARDK 2533
Cdd:COG3883 213 AAAAA 217
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2259-2769 |
3.69e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2259 QRARQSVRSLAEIALAIGSSSKAV--NVDPRLLKEAE---ETLMTLEAASADQYPEKAQTVPGKLEEiqkkiqEETEKLD 2333
Cdd:NF041483 629 AQAEQEAERLRTEAAADASAARAEgeNVAVRLRSEAAaeaERLKSEAQESADRVRAEAAAAAERVGT------EAAEALA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2334 KQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAITDdleRVEAAKGEFQKLnvaignI 2413
Cdd:NF041483 703 AAQE--EAARRRRE--------AEETLGSARAEADQERERAR----EQSEELLASARK---RVEEAQAEAQRL------V 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2414 TEnlKDKR--EEMTHAVTTLNETRNDVA--------------EALEAAKKRVRRdEKSVDMQLVNAKAHelhlqATTLRQ 2477
Cdd:NF041483 760 EE--ADRRatELVSAAEQTAQQVRDSVAglqeqaeeeiaglrSAAEHAAERTRT-EAQEEADRVRSDAY-----AERERA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2478 TFDNNK--DNTDQAVEAANAFSNLT-------------DTLKNAKAQIDNAYEAL-SAEPAFAESVQNARDkpfpDETKE 2541
Cdd:NF041483 832 SEDANRlrREAQEETEAAKALAERTvseaiaeaerlrsDASEYAQRVRTEASDTLaSAEQDAARTRADARE----DANRI 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALSKT---VSQDLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAgipkyskntldsidEKVQEVEKLKAEIDANIEET 2617
Cdd:NF041483 908 RSDAAAQAdrlIGEATSEAERLTAEARAEAErLRDEARAEAERVRA--------------DAAAQAEQLIAEATGEAERL 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2618 RAKISEIAGKAEEITE---------KANSAMEGIRL-------------------ARRNSVQLNKLAPVIVSKFEELKKL 2669
Cdd:NF041483 974 RAEAAETVGSAQQHAErirteaervKAEAAAEAERLrteareeadrtldearkdaNKRRSEAAEQADTLITEAAAEADQL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2670 -SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEkGSSLdlnipqrVTRSAAHADisfyfrteqehgiPLFFG- 2747
Cdd:NF041483 1054 tAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVE-GNSL-------VEKARTDAD-------------ELLVGa 1112
|
570 580
....*....|....*....|...
gi 808356960 2748 -NEETAVGSRAVPTADYVAAEIE 2769
Cdd:NF041483 1113 rRDATAIRERAEELRDRITGEIE 1135
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2001-2045 |
3.74e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 2001 CECSQCGS--QYCDNKSGGCECKINVEGDSCDRCKPDHWGFSkCQGC 2045
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2317-2773 |
3.80e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.07 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQ---KETFEAQKKRaeelaaylnsaqqLLKESKSKADKsnniaKMLQLTKVENLVAAITDDL 2393
Cdd:pfam02463 170 KKKEALKKLIEETENLAELiidLEELKLQELK-------------LKEQAKKALEY-----YQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2394 ERVEAakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKrvrrdEKSVDMQLVNAKAHELHLQAT 2473
Cdd:pfam02463 232 LKLNE---ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-----LQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2474 TLRQtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIdnayEALSAEPAFAESVQNARdkpfpdetKEKIDALSKtvsqd 2553
Cdd:pfam02463 304 KLER---RKVDDEEKLKESEKEKKKAEKELKKEKEEI----EELEKELKELEIKREAE--------EEEEEELEK----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2554 lketeKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDsIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITE 2633
Cdd:pfam02463 364 -----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL-KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2634 KANSAMEGIRLarrNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVsdKVSQIKEMIAVARDAANRIKLGAHFEKGSSL 2713
Cdd:pfam02463 438 SIELKQGKLTE---EKEELEKQELKLLKDELELKKSEDLLKETQLVK--LQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2714 DLNIPQRVTRSAAHADIsfyFRTEQEHGIPLFFGNEETAVGSRAVPTADYVAAEIEYGRP 2773
Cdd:pfam02463 513 LALIKDGVGGRIISAHG---RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2095-2141 |
4.55e-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: 54.67 E-value: 4.55e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPT--YGCR 2141
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1565-1613 |
4.90e-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: 54.67 E-value: 4.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLSAENPLGC 1613
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
2167-2669 |
5.12e-09 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 61.96 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2167 AIANISSATIVGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLN 2246
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2247 GTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQ 2326
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2327 EETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAitDDL-ERVEA-AKGEFQ 2404
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAE--GDLtVRIDVdSKDEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2405 KLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHELhlqattlRQTFDNNKD 2484
Cdd:COG0840 239 QLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA--EEQAASLEETAAAMEEL-------SATVQEVAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2485 NTDQAVEAAN-----------AFSNLTDTLKNAKAQIDNAYE-----------------------------ALSA--EPA 2522
Cdd:COG0840 310 NAQQAAELAEeaselaeeggeVVEEAVEGIEEIRESVEETAEtieelgessqeigeivdviddiaeqtnllALNAaiEAA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2523 --------FA-----------ESVQNARdkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKlrkrkeavka 2583
Cdd:COG0840 390 rageagrgFAvvadevrklaeRSAEATK------EIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEE---------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2584 gipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLApvivskf 2663
Cdd:COG0840 454 -----AGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELA------- 521
|
....*.
gi 808356960 2664 EELKKL 2669
Cdd:COG0840 522 EELQEL 527
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
472-516 |
5.22e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTA-GC 516
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPpGC 46
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2151-2645 |
5.29e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2151 IGDVDNLELEIDVLGTAI----ANISSATIVGARLarnKKEFNDINEITKMLNDEENSFGNVFgdaQDILTNSTQIQNKl 2226
Cdd:PRK01156 158 ILEINSLERNYDKLKDVIdmlrAEISNIDYLEEKL---KSSNLELENIKKQIADDEKSHSITL---KEIERLSIEYNNA- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2227 vrtkthsqnsvsSAKNITLNGTefLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVdprlLKEAEETLMTLEAASA-- 2304
Cdd:PRK01156 231 ------------MDDYNNLKSA--LNELSSLEDMKNRYESEIKTAESDLSMELEKNNY----YKELEERHMKIINDPVyk 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2305 ------------DQYPEKAQTVPGKLEEIQK--KIQEETEKLDKQKETFEAQKKRAEEL--------------AAYLNSA 2356
Cdd:PRK01156 293 nrnyindyfkykNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDLnnqilelegyemdyNSYLKSI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2357 QQLLK----ESKSKADKSNNIAKMLQLTKVE-----NLVAAITDDLERVEaakGEFQKLNVAIGNITENLKDKREEMT-- 2425
Cdd:PRK01156 373 ESLKKkieeYSKNIERMSAFISEILKIQEIDpdaikKELNEINVKLQDIS---SKVSSLNQRIRALRENLDELSRNMEml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2426 --HAV-----TTL-----NETRNDVAE---ALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQ--TFDNN------ 2482
Cdd:PRK01156 450 ngQSVcpvcgTTLgeeksNHIINHYNEkksRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKsiNEYNKiesara 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2483 ------------KDNTDQAVEAANAFSNL---------TDTLkNAKAQIDN--------AYEALSAEPAFAESVQNARDK 2533
Cdd:PRK01156 530 dledikikinelKDKHDKYEEIKNRYKSLkledldskrTSWL-NALAVISLidietnrsRSNEIKKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2534 PFPDETK------EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPkySKNTLDS----IDEKVQEV 2603
Cdd:PRK01156 609 GFPDDKSyidksiREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP--DLKEITSrindIEDNLKKS 686
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 808356960 2604 EKL-------KAEIDANIEETRAKISEIAGKAEEITEKANSaMEGIRLA 2645
Cdd:PRK01156 687 RKAlddakanRARLESTIEILRTRINELSDRINDINETLES-MKKIKKA 734
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
519-559 |
5.62e-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: 54.28 E-value: 5.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 808356960 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGD 559
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2327-2669 |
1.13e-08 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 59.82 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2327 EETEKLDKQKETFEAQKKRAEELAAYLNSAQQL----LKESKSKADKSNNIAKML---------QLTKVENLVAAITDDL 2393
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVksleLKKKSQKNLKESKDQKELekeiralvqERGEQDKRLQALEEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2394 ERVEAakgefqKLNVAIgnitenlKDKREeMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQAT 2473
Cdd:pfam15905 104 EKVEA------KLNAAV-------REKTS-LSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2474 TLRQTFDNNKDNTDQAVEAANafsnltDTLKNAKAQIDNAYEALSaepafaesvqnardkpfpDETKEKIDALSktvsqd 2553
Cdd:pfam15905 170 AKMKEVMAKQEGMEGKLQVTQ------KNLEHSKGKVAQLEEKLV------------------STEKEKIEEKS------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2554 lkETEKLKKQLEQLTELSEKLRKRKEAVkagipKYSKNTLdsiDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEI-T 2632
Cdd:pfam15905 220 --ETEKLLEYITELSCVSEQVEKYKLDI-----AQLEELL---KEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLeS 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 808356960 2633 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2669
Cdd:pfam15905 290 EKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2239-2687 |
1.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2239 SAKNITLNGTEfLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASA--DQYPEKAQT--- 2313
Cdd:COG4717 62 QGRKPELNLKE-LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALeae 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2314 ---VPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQLLKESKSKADKSNNIAKmlQLTKVENLVAAI 2389
Cdd:COG4717 141 laeLPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQ--RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2390 TDDLERVEAAKGEFQKlNVAIGNITENLKDKRE---------EMTHAVTTLNETRNDVAEAL---------EAAKKRVRR 2451
Cdd:COG4717 219 QEELEELEEELEQLEN-ELEAAALEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLflvlgllalLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2452 DEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAEsvqnaR 2531
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-----I 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2532 DKPFPDETKEKIDALSKTVSQdLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEI 2610
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEqLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2611 DANIEETRAKISEIA--GKAEEITEKANSAMEGIR-LARRNSVqlNKLAPVIVSKFEELkklssARSAKVDSVSDKVSQI 2687
Cdd:COG4717 452 REELAELEAELEQLEedGELAELLQELEELKAELReLAEEWAA--LKLALELLEEAREE-----YREERLPPVLERASEY 524
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1947-1998 |
1.24e-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: 53.51 E-value: 1.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 1947 PCQCNGNNNLtdSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVTAKNC 1998
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2150-2517 |
1.30e-08 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 60.78 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2150 LIGDVDNLELEIDVLGTAIANISSATIVGARLARNKKEFNDINEITKMLNDEENSF--GNVFGDAQDILTNSTQIQNKLV 2227
Cdd:COG5281 50 AAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAAAEAALAALAAAalALAAAALAEAALAAAAAAAAAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2228 RTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQY 2307
Cdd:COG5281 130 AAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2308 PEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLL--KESKSKADKSNNIAKMLQLTKVENL 2385
Cdd:COG5281 210 AAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAAAAAALALAaaAELALTAQAEAAAAAAAAAAAAAQA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2386 VAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQL---VN 2462
Cdd:COG5281 290 AEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALeaaAA 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356960 2463 AKAHELHLQATTLRQTFDNNKDNTDQAVEAA--------NAFSNLTDTLKNAKAQIDNAYEAL 2517
Cdd:COG5281 370 AAAAELAAAGDWAAGAKAALAEYADSATNVAaqvaqaatSAFSGLTDALAGAVTTGKLLFDAL 432
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2256-2673 |
1.36e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 60.44 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2256 KRAQRARQSVRSLAEIAlaigssskavnvdpRLLKEAEETLMTLEAASADqypEKAQtvpgKLEEIQKKIQEETEKLDKQ 2335
Cdd:COG3064 60 AKAEAEQRAAELAAEAA--------------KKLAEAEKAAAEAEKKAAA---EKAK----AAKEAEAAAAAEKAAAAAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2336 KETFEAQKKRAEElaaylnSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITE 2415
Cdd:COG3064 119 KEKAEEAKRKAEE------EAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2416 NLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANA 2495
Cdd:COG3064 193 ADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2496 FSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFPDETkekidalSKTVSQDLKETEKLKKQLEQLTELSEKLR 2575
Cdd:COG3064 273 ALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA-------VLAAAAAAGALVVRGGGAASLEAALSLLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2576 KRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKL 2655
Cdd:COG3064 346 AGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLA 425
|
410
....*....|....*...
gi 808356960 2656 APVIVSKFEELKKLSSAR 2673
Cdd:COG3064 426 LAGAAGAVVALLVKLVAD 443
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2189-2688 |
1.52e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 61.39 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2189 NDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKL--VRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVR 2266
Cdd:PTZ00440 536 NEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIkyIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFI 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2267 SLAEIaLAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTvpGKLEEIQKKIQEETEKLDKQKETFEAQ--KK 2344
Cdd:PTZ00440 616 NEKND-LQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSK--EDLQTLLNTSKNEYEKLEFMKSDNIDNiiKN 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2345 RAEELAAYLNSAQQLLKEskskadKSNNIAKMLQ--LTKVENLVAAITDDLERVEAAKGEF--------QKLNVAIGNIT 2414
Cdd:PTZ00440 693 LKKELQNLLSLKENIIKK------QLNNIEQDISnsLNQYTIKYNDLKSSIEEYKEEEEKLevykhqiiNRKNEFILHLY 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2415 ENLKD-------KREEMTHAVTTLNETR--NDVAEALEAAKKRVRRDEKSVDMQLVNAKAH-ELHLQAT-TLRQTFDNNK 2483
Cdd:PTZ00440 767 ENDKDlpdgkntYEEFLQYKDTILNKENkiSNDINILKENKKNNQDLLNSYNILIQKLEAHtEKNDEELkQLLQKFPTED 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2484 DNTDQAvEAANAFSNLTDTLKNAKAQIDNAYEALSAepafAESVQNARD------------KPFPDETKEKIDALSKTVS 2551
Cdd:PTZ00440 847 ENLNLK-ELEKEFNENNQIVDNIIKDIENMNKNINI----IKTLNIAINrsnsnkqlvehlLNNKIDLKNKLEQHMKIIN 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2552 QDL---------------KETEKLKKQL--EQLTELS---EKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEID 2611
Cdd:PTZ00440 922 TDNiiqkneklnllnnlnKEKEKIEKQLsdTKINNLKmqiEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEID 1001
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2612 ----------ANIEETRAK---------ISEIAGKAEEITEKAN---SAMEGIR-----LARRNSVQLNKlAPVIVSKFE 2664
Cdd:PTZ00440 1002 klnvnynilnKKIDDLIKKqhddiieliDKLIKEKGKEIEEKVDqyiSLLEKMKtklssFHFNIDIKKYK-NPKIKEEIK 1080
|
570 580
....*....|....*....|....
gi 808356960 2665 ELKKLSSARSAKVDSVSDKVSQIK 2688
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKLIEIK 1104
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2048-2097 |
1.56e-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: 53.13 E-value: 1.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2048 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYgeHGCDKCDC 2097
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL--PSDPPQGC 49
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2238-2657 |
1.65e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2238 SSAKNITLNGTEFLQEVMKRAQRARQSVRSLaeialaigssskavnvdprllkEAEETLMTLEAASADQY-PEKAQTVPG 2316
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSL----------------------HGKAELLTLRSQLLTLCtPCMPDTYHE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlQLTKVENLVAAItdDLERV 2396
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRA-----QEAVLEETQERI--NRARK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2397 EAAKGEFQKlnvAIGNItenlkDKREEMTHavTTLNETRNDVAEALeAAKKRVRRDEKSVDMQLV-----------NAKA 2465
Cdd:TIGR00618 292 AAPLAAHIK---AVTQI-----EQQAQRIH--TELQSKMRSRAKLL-MKRAAHVKQQSSIEEQRRllqtlhsqeihIRDA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2466 HELHL-------QATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQID---NAYEALSAEPAFAESVQNARDKPF 2535
Cdd:TIGR00618 361 HEVATsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtSAFRDLQGQLAHAKKQQELQQRYA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2536 P----------DETKEKIDALSKtVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVK----------------------- 2582
Cdd:TIGR00618 441 ElcaaaitctaQCEKLEKIHLQE-SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepcplcgscihpnparqd 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2583 AGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEI-------TEKANSAMEGIRLARRNSVQLNKL 2655
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLQDL 599
|
..
gi 808356960 2656 AP 2657
Cdd:TIGR00618 600 TE 601
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2537-2669 |
1.75e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLR-KRKEAVKagipkyskntldSIDEKVQEVEKLKAEIDANIE 2615
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNA------------QVKELREEAQELREKRDELNE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2616 etraKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2669
Cdd:COG1340 72 ----KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL 121
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2000-2046 |
1.85e-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: 53.13 E-value: 1.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2000 SCECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGF-SKCQGCQ 2046
Cdd:cd00055 1 PCDCNGHGSLsgQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1565-1614 |
3.04e-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: 52.36 E-value: 3.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLsAENPLGCV 1614
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2330-2702 |
3.40e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2330 EKLDKQKETFEAQKKRAEELAAYLNSAqqlLKESKSKADKSNNiakmlQLTKVENLVAAITDDLERVEA----AKGEFQK 2405
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQ---LRKALFELDKLQE-----ELEQLREELEQAREELEQLEEeleqARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2406 LNvaignitENLKDKREEMTHAVTTLNETRndvaEALEAAKKRVRRDEKSVDmqlvnakahELHLQATTLRQTfdnNKDN 2485
Cdd:COG4372 78 LE-------EELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELE---------ELQKERQDLEQQ---RKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2486 TDQAVEAANAFSNLTDTLKNAKAQIDNayeaLSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKETEKLKKQLE 2565
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLES----LQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2566 QLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRaKISEIAGKAEEITEKANSAMEGIRLA 2645
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI-EELELAILVEKDTEEEELEIAALELE 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2646 RRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
427-474 |
3.72e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 427 CDCDPD-KHTGACAEETGKCECLPRFVGEDCDQCASGYYDAPKCKPCEC 474
Cdd:pfam00053 1 CDCNPHgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2095-2143 |
4.35e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 4.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 2095 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGCRRC 2143
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2313-2449 |
4.46e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2313 TVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiAKMLQ-LTK-VENLVAAIT 2390
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEaLQKeIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2391 D--D-----LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRV 2449
Cdd:COG1579 107 DleDeilelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2306-2668 |
5.67e-08 |
|
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: 58.89 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2306 QYPEKAQTVPGKLEeiqkKIQEETEKLDKQKETFEAQKKRA-----------EELAAYLNSAQqlLKESKSKADksNNIA 2374
Cdd:pfam05701 32 QTVERRKLVELELE----KVQEEIPEYKKQSEAAEAAKAQVleelestkrliEELKLNLERAQ--TEEAQAKQD--SELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2375 KMlqltKVENLVAAITDDlERV------EAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKR 2448
Cdd:pfam05701 104 KL----RVEEMEQGIADE-ASVaakaqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2449 vrrdEKSVD---MQLVNAK-----AHELHLQA--------TTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDN 2512
Cdd:pfam05701 179 ----EKTVEeltIELIATKeslesAHAAHLEAeehrigaaLAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2513 AYE---ALSAEpaFAESVQNARDKPFPDETKEKIDALS--KTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPK 2587
Cdd:pfam05701 255 ASAlllDLKAE--LAAYMESKLKEEADGEGNEKKTSTSiqAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2588 ySKNTLDSIdeKVQE------VEKLKAEID----------ANIEETRAKISEIAGK-------AEEITEKANSAMEGIRL 2644
Cdd:pfam05701 333 -EKAELASL--RQREgmasiaVSSLEAELNrtkseialvqAKEKEAREKMVELPKQlqqaaqeAEEAKSLAQAAREELRK 409
|
410 420
....*....|....*....|....
gi 808356960 2645 ARRNSVQLNKLAPVIVSKFEELKK 2668
Cdd:pfam05701 410 AKEEAEQAKAAASTVESRLEAVLK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2251-2534 |
6.06e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2251 LQEVMKRAQRARQSVRS-LAEIALAIGSSSKAVNvdpRLLKEAEETLMTLEAASADQYPEKAQTvpGKLEEIQKKIQEET 2329
Cdd:COG1196 251 LEAELEELEAELAELEAeLEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2330 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLvAAITDDLERVEAAKGEFQKLNVA 2409
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2410 IGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVdmqlvnAKAHELHLQATTLRQtfdnnkDNTDQA 2489
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE------AELEEEEEALLELLA------ELLEEA 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 808356960 2490 VEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKP 2534
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2319-2705 |
7.20e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2319 EEIQKKIQEETEkLDKQKETFEAQKKR----AEELAAYLNS-AQQLLKESKSKADKSnniakmlqltkvenLVAAitddl 2393
Cdd:NF041483 124 EAVQRRQQLDQE-LAERRQTVESHVNEnvawAEQLRARTESqARRLLDESRAEAEQA--------------LAAA----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2394 eRVEAAKgefqklnvaignITEnlkDKREEMThavttlNETRNDVAEAlEAAKKRVRRDEKsvdmQLVNA---KAHELHL 2470
Cdd:NF041483 184 -RAEAER------------LAE---EARQRLG------SEAESARAEA-EAILRRARKDAE----RLLNAastQAQEATD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2471 QATTLRQTFDNNKDNT-DQAVEAANA----FSNLTDTLKNAKAQIDN----AYEALSAEPAFAESVQNARDKpfpdETKE 2541
Cdd:NF041483 237 HAEQLRSSTAAESDQArRQAAELSRAaeqrMQEAEEALREARAEAEKvvaeAKEAAAKQLASAESANEQRTR----TAKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2542 KIDALsktVSQDLKETEKLKKQLEQL------------TELSEKLR-KRKEAVKAGIPKYSKNTLD-----SIDEK---- 2599
Cdd:NF041483 313 EIARL---VGEATKEAEALKAEAEQAladaraeaeklvAEAAEKARtVAAEDTAAQLAKAARTAEEvltkaSEDAKattr 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2600 --VQEVEKLKAEIDANIEETRAKISEIA----GKAEEITE----KANSAMEGIRLARRNSVQLNKLApviVSKFEELKkl 2669
Cdd:NF041483 390 aaAEEAERIRREAEAEADRLRGEAADQAeqlkGAAKDDTKeyraKTVELQEEARRLRGEAEQLRAEA---VAEGERIR-- 464
|
410 420 430
....*....|....*....|....*....|....*.
gi 808356960 2670 SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGA 2705
Cdd:NF041483 465 GEARREAVQQIEEAARTAEELLTKAKADADELRSTA 500
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1891-1945 |
8.22e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 8.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 1891 CACPFAPTNNfaKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHPQISGESC 1945
Cdd:pfam00053 1 CDCNPHGSLS--DTCD-PETGQ---CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
472-509 |
8.30e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 8.30e-08
10 20 30
....*....|....*....|....*....|....*...
gi 808356960 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGY 509
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
427-467 |
9.47e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 427 CDCDPDKH-TGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
809-847 |
9.75e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.75e-08
10 20 30
....*....|....*....|....*....|....*....
gi 808356960 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1472-1515 |
1.02e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.82 E-value: 1.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDPLI-GCQ 1515
Cdd:cd00055 2 CDCNghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1472-1510 |
1.17e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.17e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDP 1510
Cdd:smart00180 1 CDCDpggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2317-2701 |
1.45e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 57.56 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQE-ETEKLDKqketFEAQKKRAEELAAY--LNSAQQLLKESKSKADK-SNNIAKMLQltKVENLVAAITDD 2392
Cdd:pfam06160 46 KFEEWRKKWDDiVTKSLPD----IEELLFEAEELNDKyrFKKAKKALDEIEELLDDiEEDIKQILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2393 LERVEAAKGEFQKLN-----------VAIGNITENLKDKREEMTHAVTtLNETRNDVA--EALEAAKKRVRRDEKsvDMQ 2459
Cdd:pfam06160 120 REEVEELKDKYRELRktllanrfsygPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEarEVLEKLEEETDALEE--LME 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2460 LVNAKAHELHlqaTTLRQTFDNNKDNTDQAVEAANAFS--NLTDTLKNAKAQIDNAYEAL-SAEPAFAESVQnardkpfp 2536
Cdd:pfam06160 197 DIPPLYEELK---TELPDQLEELKEGYREMEEEGYALEhlNVDKEIQQLEEQLEENLALLeNLELDEAEEAL-------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 DETKEKIDALsktvsQDLKETE------------KLKKQLEQLTELSEKLRKRKEAVK---------AGIPKYSKNTLDS 2595
Cdd:pfam06160 266 EEIEERIDQL-----YDLLEKEvdakkyveknlpEIEDYLEHAEEQNKELKEELERVQqsytlneneLERVRGLEKQLEE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2596 IDEKVQE-VEKLKA------EIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNK-------------L 2655
Cdd:pfam06160 341 LEKRYDEiVERLEEkevaysELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLelreikrlveksnL 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2656 aPVIVSKFEELKKLSSARSAKV-----------DSVSDKVSQIKEMIAVARDAANRI 2701
Cdd:pfam06160 421 -PGLPESYLDYFFDVSDEIEDLadelnevplnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2158-2534 |
1.48e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 57.66 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2158 ELEIDVLGTAIANISSATI---VGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNklVRTKTHSQ 2234
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGnlgSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTD--LRLEKLGE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2235 NsVSSAKNITLNGTEFLQEVmkraQRARQSVRSLAEIALAIGSSSKAVNVDPR--LLKEAEETLMTLEAASADQYPEKAQ 2312
Cdd:COG5185 273 N-AESSKRLNENANNLIKQF----ENTKEKIAEYTKSIDIKKATESLEEQLAAaeAEQELEESKRETETGIQNLTAEIEQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2313 TVPgKLEEIQKKIQEE------TEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLV 2386
Cdd:COG5185 348 GQE-SLTENLEAIKEEienivgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2387 AAITDDLERVEAAKgefQKLNVAIGNITENLKDKREEMTHAVT-TLNETRNDVAEALEAAKKRVRRDEKSVDmqlvnaka 2465
Cdd:COG5185 427 RQIEQATSSNEEVS---KLLNELISELNKVMREADEESQSRLEeAYDEINRSVRSKKEDLNEELTQIESRVS-------- 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2466 helhlqatTLRQTFDNNKDNTDQAVEAA-NAFSNLTDTLKNA-KAQIDNAYEALSAEPAFAESVQNARDKP 2534
Cdd:COG5185 496 --------TLKATLEKLRAKLERQLEGVrSKLDQVAESLKDFmRARGYAHILALENLIPASELIQASNAKT 558
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-467 |
1.66e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 1.66e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 808356960 427 CDCDPD-KHTGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:cd00055 2 CDCNGHgSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2190-2433 |
1.75e-07 |
|
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: 55.50 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2190 DINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNgtefLQEVMKRAQRARQSVRSLA 2269
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDN----IKEINEKVATLGENDFALP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2270 EIALaigsSSKAVNVDpRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLdkqketFEAQKKRAEEL 2349
Cdd:pfam06008 117 SSDL----SRMLAEAQ-RMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAL------ANALRDSLAEY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2350 AAYLNSAQQLLKESKSKADKSNniaKMLQLTKvenlvAAITDDLERVEAAKGefQKLnvaigNITENLKDKREEMTHAVT 2429
Cdd:pfam06008 186 EAKLSDLRELLREAAAKTRDAN---RLNLANQ-----ANLREFQRKKEEVSE--QKN-----QLEETLKTARDSLDAANL 250
|
....
gi 808356960 2430 TLNE 2433
Cdd:pfam06008 251 LLQE 254
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1472-1514 |
2.04e-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: 50.04 E-value: 2.04e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1472 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGY--DPLIGC 1514
Cdd:pfam00053 1 CDCNphgsLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2251-2574 |
2.34e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.29 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2251 LQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVD-PRLLKEAEETLMTLEAASadqypEKAQTVPGKLEEIQKKIQEET 2329
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLS-----EAEDMLACEQHALLRKLQPEQ 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2330 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVA 2409
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2410 IGNITENLKD---KREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHElHLQATTLRQTFDNNKDNT 2486
Cdd:TIGR00618 706 LRELETHIEEydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN-NEEVTAALQTGAELSHLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2487 DQAVEAANAFSNLTDTLKNAKAQIDNayEALSAEPAF-AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLE 2565
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQ--EIPSDEDILnLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*....
gi 808356960 2566 QLTELSEKL 2574
Cdd:TIGR00618 863 QLTQEQAKI 871
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2346-2633 |
2.52e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2346 AEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVE--NLVAAITDDLERVEAAKgefqKLNvAIGN--ITENLKDKR 2421
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKgsNVIEISYTSPDPELAAA----VAN-ALAEayLEQNLELRR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2422 EEMTHAVTTLNETRNDVAEALEAAKKRV---RRDEKSVDMQlvnakahelhlqattlrqtfDNNKDNTDQAVEAANAFSN 2498
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLS--------------------EEAKLLLQQLSELESQLAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2499 LTDTLKNAKAQIDNAYEALSAEPAFAESVQNardkpfpdetkekiDALSKTVSQDLKETE-KLKKQLEQLTELSEK---L 2574
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQ--------------SPVIQQLRAQLAELEaELAELSARYTPNHPDviaL 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 808356960 2575 RKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITE 2633
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1565-1613 |
2.52e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 1565 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDlsaENPLGC 1613
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1891-1938 |
2.55e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 808356960 1891 CACPfaPTNNFAKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHP 1938
Cdd:smart00180 1 CDCD--PGGSASGTCD-PDTGQ---CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2323-2609 |
2.71e-07 |
|
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: 56.58 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2323 KKIQEETEKLDKQ-------KETFEA----QKKRAEELAAYLNSAqqlLKESKSKADKSNNIAKMLQLTkvenlVAAITD 2391
Cdd:pfam05701 229 KQAEEELQRLNQQllsakdlKSKLETasalLLDLKAELAAYMESK---LKEEADGEGNEKKTSTSIQAA-----LASAKK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2392 DLERV----EAAKGEFQKLNVAIGNITENL-KDK--------REEMTH-AVTTLNETRNDVAEALEAAKKRVRRD-EKSV 2456
Cdd:pfam05701 301 ELEEVkaniEKAKDEVNCLRVAAASLRSELeKEKaelaslrqREGMASiAVSSLEAELNRTKSEIALVQAKEKEArEKMV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2457 DM--QLVNA--KAHELHLQATTLRQTFDNNKDNTDQAVEAANAF-SNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNAR 2531
Cdd:pfam05701 381 ELpkQLQQAaqEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVeSRLEAVLKEIEAAKASEKLALAAIKALQESESSAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2532 DKPFPDE------TKEKIDALSK---------------TVSQ--DLKETEKlkKQLEQLTELSEKLRKRKEAVKAGIPKY 2588
Cdd:pfam05701 461 STNQEDSprgvtlSLEEYYELSKraheaeelankrvaeAVSQieEAKESEL--RSLEKLEEVNREMEERKEALKIALEKA 538
|
330 340
....*....|....*....|....
gi 808356960 2589 SKNTldsiDEKV---QEVEKLKAE 2609
Cdd:pfam05701 539 EKAK----EGKLaaeQELRKWRAE 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2178-2719 |
2.94e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2178 GARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQdiltnstqiqnklVRTKTHSQNSVSSAKNITLNGTEFLQEVMKR 2257
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-------------LQADRHQEHIRARDSLIQSLATRLELDGFER 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2258 AQRARQSVRSLaeIALAIGSSSKAVNVDPRLLKEAEETLMTLEaasadqypEKAQTVPGKLEEIQKKIQEETEKLDKQKE 2337
Cdd:TIGR00606 385 GPFSERQIKNF--HTLVIERQEDEAKTAAQLCADLQSKERLKQ--------EQADEIRDEKKGLGRTIELKKEILEKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2338 TFEAQKKRAEELAA----YLNSAQQLLKESK--SKADKSNNI-AKMLQLTKVENLVAaitdDLERVEAAkgefqklnvai 2410
Cdd:TIGR00606 455 ELKFVIKELQQLEGssdrILELDQELRKAERelSKAEKNSLTeTLKKEVKSLQNEKA----DLDRKLRK----------- 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2411 gnitenLKDKREEMTHAVTTLNETrndvaeaLEAAKKRVRRDEksvdmqlvnakahelhlqattlrQTFDNNKDNTDQAV 2490
Cdd:TIGR00606 520 ------LDQEMEQLNHHTTTRTQM-------EMLTKDKMDKDE-----------------------QIRKIKSRHSDELT 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2491 EAANAFSN---LTDTL---KNAKAQIDNAYEALSAEPAFAESVQNARDKpfpdETKEKIDALSKTVSQ--DLKETEKLKK 2562
Cdd:TIGR00606 564 SLLGYFPNkkqLEDWLhskSKEINQTRDRLAKLNKELASLEQNKNHINN----ELESKEEQLSSYEDKlfDVCGSQDEES 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2563 QLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEK------VQEVEKLKAEIDANIEETRAKISEIAGKAEEIT---- 2632
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTEselk 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2633 --EKANSAMEGIRLARRNSVQL---------NKLAPV------IVSKFEELKKLSSARSAKVDSVSD---KVSQIKEMIA 2692
Cdd:TIGR00606 720 kkEKRRDEMLGLAPGRQSIIDLkekeipelrNKLQKVnrdiqrLKNDIEEQETLLGTIMPEEESAKVcltDVTIMERFQM 799
|
570 580
....*....|....*....|....*..
gi 808356960 2693 VARDAANRIKLGAHFEKGSSLDLNIPQ 2719
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGSDLDRTVQQ 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2284-2627 |
3.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2284 VDPRLLKEAEETlmtleaASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEEL---AAYLNSAQQLL 2360
Cdd:PTZ00121 1635 VEQLKKKEAEEK------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELK 1708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2361 KESKSKADKSNNIAKM--LQLTKVENLVAAITDDLERVEAAK-GEFQKLNVAignitenlKDKREEMTHAVTTLNETRND 2437
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAeeENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIA--------HLKKEEEKKAEEIRKEKEAV 1780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2438 VAEAL--EAAKKRVRRDEKSVDM----QLVNAKAHELHLQATTLRQTFDNnkdNTDQAVEAANAFSNLTDTLKNAKAQID 2511
Cdd:PTZ00121 1781 IEEELdeEDEKRRMEVDKKIKDIfdnfANIIEGGKEGNLVINDSKEMEDS---AIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2512 NayeaLSAEPAFAESVQNardkpfpdetkekidalsktvsqdlKETEKLKKQLEQLTELSEKLRKRKEAVKAGIP--KYS 2589
Cdd:PTZ00121 1858 N----ENGEDGNKEADFN-------------------------KEKDLKEDDEEEIEEADEIEKIDKDDIEREIPnnNMA 1908
|
330 340 350
....*....|....*....|....*....|....*...
gi 808356960 2590 KNTLDSIDEKVQEVEKLKaeidANIEETRAKISEIAGK 2627
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIK----RDAEETREEIIKISKK 1942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2487-2634 |
3.78e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2487 DQAVEAANAFSNLTDTLKNAKAQIDNA------YEALSaepafaESVQNARDkpfpdetkekIDALSKTVSQDLKETEKL 2560
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVearikkYEEQL------GNVRNNKE----------YEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2561 KKQLEQLTELSEKLRKRKEAVKAgipkyskntldSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEK 2634
Cdd:COG1579 109 EDEILELMERIEELEEELAELEA-----------ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2317-2573 |
3.91e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELaaylnsaQQLLKEsksKADKSNNIAKmlQLTKVENLVAAITDDLERV 2396
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK-------QELIDQ---KEKEKKDLIK--EIEEKEKKISSLEKELEKA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2397 EAakgEFQKLNVAIGNItENLKDKREEMTHAV-TTLNETRNDVAEaleaakkrvrrdeksvdmqlvnakahelhlqattl 2475
Cdd:TIGR04523 623 KK---ENEKLSSIIKNI-KSKKNKLKQEVKQIkETIKEIRNKWPE----------------------------------- 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2476 rqTFDNNKDntdqAVEAANAFSNLTDTLKNAKAqidnayeaLSAEPAFAESVqnaRDKPFPdetkeKIDALSKTVSQDLK 2555
Cdd:TIGR04523 664 --IIKKIKE----SKTKIDDIIELMKDWLKELS--------LHYKKYITRMI---RIKDLP-----KLEEKYKEIEKELK 721
|
250
....*....|....*...
gi 808356960 2556 ETEKLKKQLEQLTELSEK 2573
Cdd:TIGR04523 722 KLDEFSKELENIIKNFNK 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2244-2493 |
5.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2244 TLNGTEflqevmKRAQRARQSVRSLAEIALAIGSsskavnvdprlLKEAEETLMTLEAASADQYPEKAQTvpgKLEEIQK 2323
Cdd:COG4913 236 DLERAH------EALEDAREQIELLEPIRELAER-----------YAAARERLAELEYLRAALRLWFAQR---RLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2324 KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKadksnniakmlQLTKVENLVAAITDDLERVEAAKGEF 2403
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-----------RLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2404 QK----LNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKsvdmqlvnaKAHELHLQATTLRQtf 2479
Cdd:COG4913 365 EAllaaLGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---------ELRELEAEIASLER-- 433
|
250
....*....|....
gi 808356960 2480 dnNKDNTDQAVEAA 2493
Cdd:COG4913 434 --RKSNIPARLLAL 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2344-2726 |
5.77e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2344 KRAEELAAYLNSAQQLLKESKSKADKSNN----IAKMLQLTKVENLVAAITD----------DLERVEAAKGEFQKLNVA 2409
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNhegkAEAKAHVGQDEGLKPSYKDfdfdakednrADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2410 IGNITENLKDKREEMTHAvttlnetrNDVAEALEAAK-KRVRRDEKSVDMQlvNAKAHELHLQATTLRQTFDNNKDNTDQ 2488
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKA--------EDARKAEEARKaEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2489 AVEAANAFSNLTDTLKNAKAQ-IDNAYEALSAEPAF-AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQ 2566
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEdARKAEAARKAEEERkAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2567 LTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEiAGKAEEITEKANSAMEGIRLAR 2646
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2647 RNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAA 2726
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2541-2709 |
8.62e-07 |
|
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: 55.46 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2541 EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAK 2620
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2621 ISEIAGKAEEITEKANSAMEGIRLARRN-----SVQLNKLAPVIVSKFEELKKLsSARSAKVDSVSDKVSQIKEMI--AV 2693
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigelEAEIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEELerEI 345
|
170
....*....|....*.
gi 808356960 2694 ARDAANRIKLGAHFEK 2709
Cdd:TIGR02169 346 EEERKRRDKLTEEYAE 361
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2185-2645 |
1.02e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.47 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2185 KKEFNDINEITKMLNDEENsfgnvfgDAQDILTNSTQIqnklvrTKTHSQNSvssaknitlngtEFLQEVMKRAQRARqs 2264
Cdd:pfam06160 82 KKAKKALDEIEELLDDIEE-------DIKQILEELDEL------LESEEKNR------------EEVEELKDKYRELR-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2265 vRSLAEIALAIGSSSKAVNVDprlLKEAEETLMTLEAASADQYPEKAqtvpgklEEIQKKIQEETEKLDKQ--------- 2335
Cdd:pfam06160 135 -KTLLANRFSYGPAIDELEKQ---LAEIEEEFSQFEELTESGDYLEA-------REVLEKLEEETDALEELmedipplye 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2336 --KETFEAQkkrAEELAA---------YLNSAQQLLKESKSKADK-SNNIAKM--LQLTKVENLVAAIT-------DDLE 2394
Cdd:pfam06160 204 elKTELPDQ---LEELKEgyremeeegYALEHLNVDKEIQQLEEQlEENLALLenLELDEAEEALEEIEeridqlyDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEAAKGEFQKlNVA-----IGNITENLKDKREEMTHAVT--TLNEtrNDVAEALEAAKkrvrrdeksvdmQLvnakaHE 2467
Cdd:pfam06160 281 KEVDAKKYVEK-NLPeiedyLEHAEEQNKELKEELERVQQsyTLNE--NELERVRGLEK------------QL-----EE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2468 LHLQATTLRQTFDNNKdntdqaveaaNAFSNLTDTLKNAKAQIDNaYEALSAEpaFAESVQNARDkpfpDETKEKidals 2547
Cdd:pfam06160 341 LEKRYDEIVERLEEKE----------VAYSELQEELEEILEQLEE-IEEEQEE--FKESLQSLRK----DELEAR----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2548 ktvsqdlketeklkkqlEQLTELSEKLRKRKEAVKA----GIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISE 2623
Cdd:pfam06160 399 -----------------EKLDEFKLELREIKRLVEKsnlpGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDE 461
|
490 500
....*....|....*....|..
gi 808356960 2624 IAGKAEEITEKANSAMEGIRLA 2645
Cdd:pfam06160 462 AQDDVDTLYEKTEELIDNATLA 483
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1890-1945 |
1.10e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 1890 ACACPFAPTNNFakSCDVseegQLLQCNCKPGYTGDRCDRCASGFFGHPqISGESC 1945
Cdd:cd00055 1 PCDCNGHGSLSG--QCDP----GTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2213-2691 |
1.14e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.22 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2213 QDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRS-LAEIALAIGSSSKAVNVD------ 2285
Cdd:PTZ00440 1087 EALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKtLKELENMNLEDITLNEVNeieiey 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2286 PRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEET-EKLDkqkeTFEAQKKRAEELAAYlNSAQQLLKESK 2364
Cdd:PTZ00440 1167 ERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERnDHLT----TFEYNAYYDKATASY-ENIEELTTEAK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2365 SKADKSNNIAKM-------------------------------------LQLTKVENLVAAITDDLERVE----AAKGEF 2403
Cdd:PTZ00440 1242 GLKGEANRSTNVdelkeiklqvfsylqqvikennkmenalheiknmyefLISIDSEKILKEILNSTKKAEefsnDAKKEL 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2404 QKLNvaigNITENLKDKREEmthavttLNETRNDVAEALEaaKKRVrrDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK 2483
Cdd:PTZ00440 1322 EKTD----NLIKQVEAKIEQ-------AKEHKNKIYGSLE--DKQI--DDEIKKIEQIKEEISNKRKEINKYLSNIKSNK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2484 DNTDQAVEAANAFSNLTDTLKNAKA------------QIDNAY---EALSAEPAFAESVQNARDKPFPdETKEKIDALSK 2548
Cdd:PTZ00440 1387 EKCDLHVRNASRGKDKIDFLNKHEAiepsnskevniiKITDNInkcKQYSNEAMETENKADENNDSII-KYEKEITNILN 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2549 TVSQDLKET--EKLKKQL---------------EQLTELSEKLRKRKEAvkagiPKYSKNTLDSIDEKVQeveKLKAEID 2611
Cdd:PTZ00440 1466 NSSILGKKTklEKKKKEAtnimddingehsiikTKLTKSSEKLNQLNEQ-----PNIKREGDVLNNDKST---IAYETIQ 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2612 ANIEETRAKISEI---AGKAEEITEKANSAMEGIR-----LARRNSVQLNKLAPVIVS---KFEELKKLSSARSAKVDSV 2680
Cdd:PTZ00440 1538 YNLGRVKHNLLNIlniKDEIETILNKAQDLMRDISkiskiVENKNLENLNDKEADYVKyldNILKEKQLMEAEYKKLNEI 1617
|
570
....*....|.
gi 808356960 2681 SDKVSQIKEMI 2691
Cdd:PTZ00440 1618 YSDVDNIEKEL 1628
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2249-2468 |
1.15e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2249 EFLQEVMK-RAQR--ARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEaasaDQY------PEKAQTVPGKLE 2319
Cdd:COG1340 68 ELNEKVKElKEERdeLNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE----WRQqtevlsPEEEKELVEKIK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2320 EIQKKIqEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADK-SNNIAKMLQltKVENLVAAItddlervEA 2398
Cdd:COG1340 144 ELEKEL-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQElHEEMIELYK--EADELRKEA-------DE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2399 AKGEFQKLNVAIGNITENLKDKREEMthavttlnetrNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHEL 2468
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKEL-----------RELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
2338-2698 |
1.19e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 54.26 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2338 TFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENL 2417
Cdd:COG0840 8 LALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2418 KDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFS 2497
Cdd:COG0840 88 LLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2498 NLTDTLKNAKAQIDNAYEALSAEP-----AFAESVQNARDKPFpDETKEKIDALSK---TVSQDLK---ETEKLKKQLEQ 2566
Cdd:COG0840 168 EAAALALAAAALALALLAAALLALvalaiILALLLSRSITRPL-RELLEVLERIAEgdlTVRIDVDskdEIGQLADAFNR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2567 LTElseKLRKRKEAVKAGIPKYSKNTlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLAR 2646
Cdd:COG0840 247 MIE---NLRELVGQVRESAEQVASAS-EELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2647 RNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAA 2698
Cdd:COG0840 323 ELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIA 374
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
701-753 |
1.24e-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: 47.73 E-value: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEDGC 753
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPET-GQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2001-2048 |
1.56e-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: 47.35 E-value: 1.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2001 CECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGFSKCQGcQGC 2048
Cdd:pfam00053 1 CDCNPHGSLsdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP-QGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1841-1883 |
1.56e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 808356960 1841 CECN--GHSA-TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1883
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1819-2144 |
1.59e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 53.82 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1819 CQLCASGYHRVQSGSFLGACVPCECNGHSATCDPDTGICTDCEHNTNGDHCEFCNEghygnatngspyDCMACACPFAPT 1898
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCKTENCKACSNDKREVCEECNSNNYLTPTSQCID------------DCAKIGNYYYTT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1899 NNFAK-SCDVSEEGQLLQCNCKpgytgDRCDRCASGFFghpqISGESCSPCQCNgnnnltdSRSCH-PNSGDCylceqnt 1976
Cdd:pfam03302 69 NANNKkICKECTVANCKTCEDQ-----GQCQACNDGFY----KSGDACSPCHES-------CKTCSgGTASDC------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 1977 dgRHCESCAAWFYGDAVTAKNCSSCECSQCGSQYCDNksggceCKINVEGDS-CDRCKPDHwGFSKCQGCQGCHCGTAAF 2055
Cdd:pfam03302 126 --TECLTGKALRYGNDGTKGTCGEGCTTGTGAGACKT------CGLTIDGTSyCSECATET-EYPQNGVCTSTAARATAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2056 NTQCNVENGqctcrpgatgmRCEHCEHGYWNYgEHGC-------DKCDCEADLSMGTV-----------CDVRTGQCHCQ 2117
Cdd:pfam03302 197 CKASSVANG-----------MCSSCANGYFRM-NGGCyettkfpGKSVCEEANSGGTCqkeapgyklnnGDLVTCSPGCK 264
|
330 340
....*....|....*....|....*..
gi 808356960 2118 EGATGSRCDQCLPSYLRIpTYGCRRCD 2144
Cdd:pfam03302 265 TCTSNTVCTTCMDGYVKT-SDSCTKCD 290
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2289-2702 |
2.09e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.28 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEaasadQYPEKAQTVPGKLeeIQKKIQEETEKldkqketfEAQKKRAEELAAyLNSAQQLLKESKSKAD 2368
Cdd:TIGR00606 202 VQEHQMELKYLK-----QYKEKACEIRDQI--TSKEAQLESSR--------EIVKSYENELDP-LKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2369 KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEMT---HAVTTLNETRNDVAEALEAA 2445
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVdcqRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2446 KKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFsnltdTLKnAKAQIDNAYEALSAEPAFAE 2525
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFH-----TLV-IERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2526 SVQNARDKPfpDETKEKIDALSKTVSQDL----KETEKLK---KQLEQLTELSEKLRKRKEAVK---AGIPKYSKNTLds 2595
Cdd:TIGR00606 420 KERLKQEQA--DEIRDEKKGLGRTIELKKeileKKQEELKfviKELQQLEGSSDRILELDQELRkaeRELSKAEKNSL-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2596 IDEKVQEVEKLKAEiDANIEETRAKISE----------IAGKAEEITEKANSAMEGIR-LARRNSVQLNKLAPVIVSKfE 2664
Cdd:TIGR00606 496 TETLKKEVKSLQNE-KADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKDEQIRkIKSRHSDELTSLLGYFPNK-K 573
|
410 420 430
....*....|....*....|....*....|....*...
gi 808356960 2665 ELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2355-2638 |
2.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2355 SAQQLLKESKSKADKSNNiakmlQLTKVENLVAAITDDLErveAAKGEFQKLNVAIGNITENLKDKREEmthavttLNET 2434
Cdd:COG3883 13 FADPQIQAKQKELSELQA-----ELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAE-------IAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2435 RNDVAEALEAAKKRVR---RDEKSVDM--QLVNAKahelhlqattlrqtfdnnkdNTDQAVEAANAFSNLTDtlknAKAQ 2509
Cdd:COG3883 78 EAEIEERREELGERARalyRSGGSVSYldVLLGSE--------------------SFSDFLDRLSALSKIAD----ADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2510 IDNAYEALsaepafaesvqnardkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVkagipkys 2589
Cdd:COG3883 134 LLEELKAD----------------------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL-------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 808356960 2590 kntLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSA 2638
Cdd:COG3883 184 ---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2317-2701 |
2.79e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEI-QKKIQEETEKLDK------QKETFEAQKKRAEEL-AAYLNSAQQLLKESKSKADKSNNI-AKML------QLTK 2381
Cdd:PRK04778 37 RKQELeNLPVNDELEKVKKlnltgqSEEKFEEWRQKWDEIvTNSLPDIEEQLFEAEELNDKFRFRkAKHEineiesLLDL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2382 VENLVAAITDDL-----------ERVEAAKGEFQKLN-----------VAIGNITENLKDKREEMTHAVTtLNETrNDVA 2439
Cdd:PRK04778 117 IEEDIEQILEELqelleseeknrEEVEQLKDLYRELRksllanrfsfgPALDELEKQLENLEEEFSQFVE-LTES-GDYV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2440 EA---LEAAKKRVRRDEKsvDMQLVNAKAHELhlqATTLRQTFDNNKDNTDQAVEAANAFS--NLTDTLKNAKAQIDNAY 2514
Cdd:PRK04778 195 EAreiLDQLEEELAALEQ--IMEEIPELLKEL---QTELPDQLQELKAGYRELVEEGYHLDhlDIEKEIQDLKEQIDENL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2515 EALSA-EPAFAEsVQNardkpfpDETKEKIDALsktvsQDLKETE-----KLKKQLEQLTELSEKLRKRKEAVKAGIPKY 2588
Cdd:PRK04778 270 ALLEElDLDEAE-EKN-------EEIQERIDQL-----YDILEREvkarkYVEKNSDTLPDFLEHAKEQNKELKEEIDRV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2589 SKN-TLD--------SIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIT----------EKANSAMEGIRL----A 2645
Cdd:PRK04778 337 KQSyTLNeselesvrQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILkqleeiekeqEKLSEMLQGLRKdeleA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356960 2646 RRNSVQL-NKLA-----------PVI----VSKFE----ELKKLSSARSAK---VDSVSDKVSQIKEMIAVARDAANRI 2701
Cdd:PRK04778 417 REKLERYrNKLHeikryleksnlPGLpedyLEMFFevsdEIEALAEELEEKpinMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2325-2666 |
2.94e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 53.68 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2325 IQEETEKLDKQKETFEAQKKRAEELaaYLNSAQQLLKESKSKADKSNNIAKMLqltkveNLVaaitddlerVEAAKGEFQ 2404
Cdd:PTZ00440 2192 LENTADKLKELYENLKKKKNIINNI--YKKINFIKLQEIENSSEKYNDISKLF------NNV---------VETQKKKLL 2254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2405 KLNVAIGNITENLKDKREEMTHAVTTLN-ETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATT----LRQTF 2479
Cdd:PTZ00440 2255 DNKNKINNIKDKINDKEKELINVDSSFTlESIKTFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENIThllnRINTL 2334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2480 DNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEpaFAESVQNARD----------KPFPDETKEKIDALSKT 2549
Cdd:PTZ00440 2335 INDLDNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKEE--FSKLLKNIKRnntlcnnnniKDFISNIGKSVETIKQR 2412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2550 VSQDLKETEKLKKQLEQLTELSEKLR--KRKEAVKAGIPKYSKN------------TLDSIDEKVQEVEKLKAEIDANIE 2615
Cdd:PTZ00440 2413 FSSNLPEKEKLHQIEENLNEIKNIMNetKRISNVDAFTNKILQDidneknkennnmNAEKIDDLIENVTSHNEKIKSELL 2492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 2616 ET-------RAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEEL 2666
Cdd:PTZ00440 2493 IIndalrrvKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYIINELESHVSKLNEL 2550
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2190-2689 |
3.13e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2190 DINEITKMLNDEENSFGNvfgDAQDILTNSTQIQNKLVRtKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLA 2269
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQN---EKADLDRKLRKLDQEMEQ-LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2270 -------EIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEEIQKKI------QEETEKLDKQK 2336
Cdd:TIGR00606 567 gyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLK 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2337 ETFEAQKKRAEELAAYLNSAQQLLKESKSKA-------DKSNNIAKMLQ--LTKVENLVAAITDDLERVEAAKGEFQK-- 2405
Cdd:TIGR00606 646 EEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQefISDLQSKLRLAPDKLKSTESELKKKEKrr 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2406 ---LNVA------IGNITENLKDKREEMTHAVTTLNETRNDVAE----------ALEAAK-------------KRVRRDE 2453
Cdd:TIGR00606 726 demLGLApgrqsiIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetllgtimpEEESAKvcltdvtimerfqMELKDVE 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2454 KSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAV--------------EAANAFSNLTDTLKNAKAQIDnayEALSA 2519
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVskielnrkliqdqqEQIQHLKSKTNELKSEKLQIG---TNLQR 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2520 EPAFAE--------------SVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEqLTELSEKLRKrkeavkagI 2585
Cdd:TIGR00606 883 RQQFEEqlvelstevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-VNDIKEKVKN--------I 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2586 PKYSKntldSIDEKVQE-VEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLAR-RNSVQLNKLAPVIVSkf 2663
Cdd:TIGR00606 954 HGYMK----DIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNLTLRKRE-- 1027
|
570 580
....*....|....*....|....*..
gi 808356960 2664 EELKKLSSARSAKVDSVS-DKVSQIKE 2689
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEMGqMQVLQMKQ 1054
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1948-1991 |
3.20e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 3.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 808356960 1948 CQCNGNNNLTDSrsCHPNSGDCyLCEQNTDGRHCESCAAWFYGD 1991
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2318-2703 |
3.20e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAK----------MLQLTKVENLVA 2387
Cdd:pfam10174 132 LFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEaemqlghlevLLDQKEKENIHL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2388 --------AITDDLERVEAAKGEFQKLNVAIGNITENLKDKREE--MTHAVTTLN-ETRNDVAEALEAAKKRVRRDEKSV 2456
Cdd:pfam10174 212 reelhrrnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEvqMLKTNGLLHtEDREEEIKQMEVYKSHSKFMKNKI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2457 DM--QLVNAKAHELHLQATTLrQTFDNNKDNTDQAVEAanafsnLTDTLkNAKAQ----IDNAYEALSAEPAFAESVQNA 2530
Cdd:pfam10174 292 DQlkQELSKKESELLALQTKL-ETLTNQNSDCKQHIEV------LKESL-TAKEQraaiLQTEVDALRLRLEEKESFLNK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2531 RDKPFPDETKEKiDALSKTVSqDLKET------------EKLKKQLEQLTELSEKLRKRKEAVKaGIPKYSKNT---LDS 2595
Cdd:pfam10174 364 KTKQLQDLTEEK-STLAGEIR-DLKDMldvkerkinvlqKKIENLQEQLRDKDKQLAGLKERVK-SLQTDSSNTdtaLTT 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2596 IDEKVQE----VEKLKAEIDaniEETRAKISEIAG--KAEEITEKANSAMEGIRLARRNSV-----QLNKLAPVIVSKFE 2664
Cdd:pfam10174 441 LEEALSEkeriIERLKEQRE---REDRERLEELESlkKENKDLKEKVSALQPELTEKESSLidlkeHASSLASSGLKKDS 517
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 808356960 2665 ELKKLSSARSAKVDSVSDKVSQIK---EMIAVAR---DAANRIKL 2703
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKLENQLKkahNAEEAVRtnpEINDRIRL 562
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
297-345 |
3.20e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 3.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808356960 297 RCVCNGHA---VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQA 345
Cdd:cd00055 1 PCDCNGHGslsGQCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
809-847 |
3.76e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 3.76e-06
10 20 30
....*....|....*....|....*....|....*....
gi 808356960 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2457-2636 |
3.77e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 49.95 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2457 DMQLVNAKAHELHLQATTLRQTFdnnKDNTDQAVEAANAfsNLTDTLKNAKAQIDNAYEALSAEpaFAESVQNARDKpfp 2536
Cdd:pfam01442 5 SLDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRE--RLQKDLEEVRAKLEPYLEELQAK--LGQNVEELRQR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 deTKEKIDALSKTVSQDLKEtekLKKQLEQLT-ELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQE--------VEKLK 2607
Cdd:pfam01442 75 --LEPYTEELRKRLNADAEE---LQEKLAPYGeELRERLEQNVDALRARLAPYAEELRQKLAERLEElkeslapyAEEVQ 149
|
170 180
....*....|....*....|....*....
gi 808356960 2608 AEIDANIEETRAKiseIAGKAEEITEKAN 2636
Cdd:pfam01442 150 AQLSQRLQELREK---LEPQAEDLREKLD 175
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
701-754 |
4.01e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 4.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEdGCR 754
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGT-GQ-CECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2373-2623 |
4.62e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2373 IAKMLQL----TKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEmthavttlnetRNDVAEALEAAKKR 2448
Cdd:COG1579 6 LRALLDLqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-----------IKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2449 VRRDEKsvdmQLVNAKahelhlqattlrqtfdNNKDntdqaveaanafsnltdtlknakaqidnaYEALSAEPAFAesvq 2528
Cdd:COG1579 75 IKKYEE----QLGNVR----------------NNKE-----------------------------YEALQKEIESL---- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2529 nardkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipkyskntldSIDEKVQEVEKLKA 2608
Cdd:COG1579 102 -----------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------ELDEELAELEAELE 159
|
250
....*....|....*
gi 808356960 2609 EIDANIEETRAKISE 2623
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2260-2702 |
4.77e-06 |
|
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: 52.76 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2260 RARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF 2339
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2340 EAQKKRAEELAAYLNSAQQLLKESKSKADKSN--------NIAKMLQ-LTKVENLVAAITDDLERVEAAKGEFQklnvai 2410
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKreinelkrELDRLQEeLQRLSEELADLNAAIAGIEAKINELE------ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2411 gnitENLKDKREEMTHAVTTLNETRNDVA------EALEAAKKRVRRDEKSVDMQLVNAKAhelhlQATTLRQTFDNNKD 2484
Cdd:TIGR02169 441 ----EEKEDKALEIKKQEWKLEQLAADLSkyeqelYDLKEEYDRVEKELSKLQRELAEAEA-----QARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2485 NTD------------------------QAVEAA--NAFSNL---TDT--------LKNAKA------------------- 2508
Cdd:TIGR02169 512 VEEvlkasiqgvhgtvaqlgsvgeryaTAIEVAagNRLNNVvveDDAvakeaielLKRRKAgratflplnkmrderrdls 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2509 ------QIDNAYEALSAEPAFA-------------ESVQNARD-------------------------------KPFPDE 2538
Cdd:TIGR02169 592 ilsedgVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAARRlmgkyrmvtlegelfeksgamtggsraprggILFSRS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2539 TKEK----------------------------IDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysk 2590
Cdd:TIGR02169 672 EPAElqrlrerleglkrelsslqselrrienrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL----- 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2591 ntlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIteKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLS 2670
Cdd:TIGR02169 747 ---SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
570 580 590
....*....|....*....|....*....|..
gi 808356960 2671 SARSAKVDSVSDKVSQIKEMIavaRDAANRIK 2702
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQR---IDLKEQIK 850
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2408-2689 |
5.10e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2408 VAIGNITENLKDKREEMTHAVTTL-NETRNDVAEaLEAAKKRVRRDEKsvDMQLVNAKAHELHLQATTLRQTFDNNKDNT 2486
Cdd:TIGR04523 22 VGYKNIANKQDTEEKQLEKKLKTIkNELKNKEKE-LKNLDKNLNKDEE--KINNSNNKIKILEQQIKDLNDKLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2487 DQAveaaNA-FSNLTDTLKNAKAQIDNayealsaepafaESVQNARDKPFPDETKEKIDalsktvsQDLKETEKLKKQLE 2565
Cdd:TIGR04523 99 NKL----NSdLSKINSEIKNDKEQKNK------------LEVELNKLEKQKKENKKNID-------KFLTEIKKKEKELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2566 QLTELSEKLRKRKEAVKagipKYSKNTLDSIDEKVQEVEKLKAEIDA------NIEETRAKISEIAGKAEEITEKANSAM 2639
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELE----NELNLLEKEKLNIQKNIDKIKNKLLKlelllsNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2640 EGIRLarrNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKE 2689
Cdd:TIGR04523 232 DNIEK---KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2157-2516 |
5.95e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2157 LELEIDVLGTAIANISSATI-VGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDI---LTNSTQIQNKLVRTKTH 2232
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTsERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNItvrLQDLTEKLSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2233 SQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALA-----IGSSSKAVNVDPRLLKEAEETLMTLEAAsadqy 2307
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqerVREHALSIRVLPKELLASRQLALQKMQS----- 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2308 pEKAQTVPGK--LEEIQKKIQEETEKLDKQKETFE----AQKKRAEELAAYLNSAQQLLKESKSKADksnniakmlqlTK 2381
Cdd:TIGR00618 688 -EKEQLTYWKemLAQCQTLLRELETHIEEYDREFNeienASSSLGSDLAAREDALNQSLKELMHQAR-----------TV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2382 VENLVAAITDDLERVEAAKGEFQKLNVAIGNItENLKDKREEMTHAVTTL----NETRNDVAEALEAAKKRVRRDEKSVD 2457
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEI-QFFNRLREEDTHLLKTLeaeiGQEIPSDEDILNLQCETLVQEEEQFL 834
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 808356960 2458 MQLvnAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLkNAKAQIDNAYEA 2516
Cdd:TIGR00618 835 SRL--EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL-NGINQIKIQFDG 890
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2318-2621 |
6.11e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.46 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKldKQKETFEAQKKRAEELAAYlNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVE 2397
Cdd:pfam13868 103 MDEIVERIQEEDQA--EAEEKLEKQRQLREEIDEF-NEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2398 AAKgefQKLNVAIGNITENLKDKREEMthavttlNETRNDVAEalEAAKKRVRRDEKsvdmqlvnakahelhlqattlrq 2477
Cdd:pfam13868 180 EEK---EREIARLRAQQEKAQDEKAER-------DELRAKLYQ--EEQERKERQKER----------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2478 tfdnnkdntdQAVEAAnafsnltdtlKNAKAQIDNAYEALSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKET 2557
Cdd:pfam13868 225 ----------EEAEKK----------ARQRQELQQAREEQIELKERRLAEEAEREE---EEFERMLRKQAEDEEIEQEEA 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2558 EKLKKQLEQLTELSEKLRKRKEAVKAgipkyskntlDSIDEKVQEVEKLK---AEIDANIEETRAKI 2621
Cdd:pfam13868 282 EKRRMKRLEHRRELEKQIEEREEQRA----------AEREEELEEGERLReeeAERRERIEEERQKK 338
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2498-2697 |
8.41e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 49.18 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2498 NLTDTLKNAKAQIDNAYEALSaePAfaesvqnardkpfpdeTKEKIDALSKtvsqdlkETEKLKKQLEQ-LTELSEKLRK 2576
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLG--PV----------------AQELVDRLEK-------ETEALRERLQKdLEEVRAKLEP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2577 RKEAVKAGIpkysKNTLDSIDEKVQE-VEKLKAEIDANIEETRAKISEiagKAEEITEKANSAMEGIRlarrnsvqlNKL 2655
Cdd:pfam01442 56 YLEELQAKL----GQNVEELRQRLEPyTEELRKRLNADAEELQEKLAP---YGEELRERLEQNVDALR---------ARL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2656 APV-------IVSKFEELKKLSSARSAKV-DSVSDKVSQIKEMIAVARDA 2697
Cdd:pfam01442 120 APYaeelrqkLAERLEELKESLAPYAEEVqAQLSQRLQELREKLEPQAED 169
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2211-2584 |
9.34e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2211 DAQDILTNSTQIQNKLVRTKTHSQNSVSSAknITLNGTEFLQEVMKRAQRARQSVRSLAE--IALAIGSSSkavnvdpRL 2288
Cdd:NF041483 903 DANRIRSDAAAQADRLIGEATSEAERLTAE--ARAEAERLRDEARAEAERVRADAAAQAEqlIAEATGEAE-------RL 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLmtleaASADQYPEKAQTVPGKL--------EEIQKKIQEETEK-LDKQKEtfEAQKKRAE--ELAAYLNS-- 2355
Cdd:NF041483 974 RAEAAETV-----GSAQQHAERIRTEAERVkaeaaaeaERLRTEAREEADRtLDEARK--DANKRRSEaaEQADTLITea 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2356 ---AQQLLKESKSKADKSNNIAKMLQLTKV-------ENLVA-AITDDLERVEAAKGEFQKLNV-------AIGNITENL 2417
Cdd:NF041483 1047 aaeADQLTAKAQEEALRTTTEAEAQADTMVgaarkeaERIVAeATVEGNSLVEKARTDADELLVgarrdatAIRERAEEL 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2418 kdkREEMTHAVTTLNE-TRNDVAEALEAAKKRVRRDEKSVDMQLVNA--KAHEL----HLQATTLRQTfdnnkdntdqAV 2490
Cdd:NF041483 1127 ---RDRITGEIEELHErARRESAEQMKSAGERCDALVKAAEEQLAEAeaKAKELvsdaNSEASKVRIA----------AV 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2491 EAANAFsnltdtLKNA---KAQIDNAYEALSAEpAFAESVQNArdkpfpDETKEKIDALSKTvSQDLK-ETEKLKKQLEQ 2566
Cdd:NF041483 1194 KKAEGL------LKEAeqkKAELVREAEKIKAE-AEAEAKRTV------EEGKRELDVLVRR-REDINaEISRVQDVLEA 1259
|
410
....*....|....*....
gi 808356960 2567 LTEL-SEKLRKRKEAVKAG 2584
Cdd:NF041483 1260 LESFeAPSGGGKGNGVKAG 1278
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2157-2616 |
1.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2157 LELEIDVLGTAIANISsativgARLARNKKEFNDINEITKMLNDEENsfgnvfgDAQDILTNSTQIQNKLVRTKTHSQNS 2236
Cdd:COG1196 321 LEEELAELEEELEELE------EELEELEEELEEAEEELEEAEAELA-------EAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2237 VSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASAdqypEKAQTVPG 2316
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----EEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSnniakmlQLTKVENLVAAITDDLERV 2396
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA-------GLRGLAGAVAVLIGVEAAY 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2397 EAAKGEFqkLNVAIGNIT-----------ENLKDKREEmthAVTTLNETRNDVAEALEAAKKRVRRDEK--SVDMQLVNA 2463
Cdd:COG1196 537 EAALEAA--LAAALQNIVveddevaaaaiEYLKAAKAG---RATFLPLDKIRARAALAAALARGAIGAAvdLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2464 KAHELHLQATTLRQTFDNNKDNTDQAV-----------------------EAANAFSNLTDTLKNAKAQIDNAYEALSAE 2520
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRavtlagrlrevtlegeggsaggsLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2521 PAFAESVQNARDkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKV 2600
Cdd:COG1196 692 ELELEEALLAEE-----EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
490 500
....*....|....*....|...
gi 808356960 2601 QEVEKLKAEIDA----N---IEE 2616
Cdd:COG1196 767 RELERLEREIEAlgpvNllaIEE 789
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2318-2690 |
1.24e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKLD---KQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNniakmlqLTKVENLVAAITDDLE 2394
Cdd:PTZ00440 1583 LENLNDKEADYVKYLDnilKEKQLMEAEYKKLNEIYSDVDNIEKELKKHKKNYEIGL-------LEKVIEINKNIKLYMD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEaakgefQKLNVAIGN--------------ITENLKDKREEMTHAVTTLNETRNDVAEALE---------AAKKRVRR 2451
Cdd:PTZ00440 1656 STK------ESLNSLVNNfsslfnnfylnkynINENLEKYKKKLNEIYNEFMESYNIIQEKMKevsnddvdyNEAKTLRE 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2452 DEKSVDMQLVNA-----------KAHELHLQATTLRQTFDN-NKDNTDQAVEAANAFSNLTDTLKNAKAQID--NAYEAL 2517
Cdd:PTZ00440 1730 EAQKEEVNLNNKeeeakkylndiKKQESFRFILYMKEKLDElSKMCKQQYNIVDEGYNYIKKKIEYIKTLNDenNLSDSL 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2518 SAEPAFAESVQNARDKPFPDETK---EKIDALSK----TVSQDLKETE-KLKKQLEQLTELSEKLrkrKEAVKAGIPKYS 2589
Cdd:PTZ00440 1810 NQAEDKNKEVANLTHYTNKNEAKnllGHVVKSANfigiKIMTGLQPTElTPDASLETAPELTFES---ENNSDLELDHLS 1886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2590 KNTLDS-IDEKVQEVEKLKAEIDANIEEtrakISEIAGKAEEITEKANsameGIRLarrNSVQLNKLAPVIVSkfeeLKK 2668
Cdd:PTZ00440 1887 SNKNELdVYKNIQDAYKSSLQILKYSDD----IDKKQRDCNKLVEDGN----EIYL---KSTAINELKNMINS----VKN 1951
|
410 420
....*....|....*....|..
gi 808356960 2669 LSSARSAKVDSVSDKVSQIKEM 2690
Cdd:PTZ00440 1952 KESAISNKIDNVSNKLSELNKI 1973
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2538-2633 |
1.28e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2538 ETKEKIDALSKTVSQDLKE-TEKLKKQLEQLTELSEKLRKRKEAVKAgipkySKNTLD----SIDEKVQEVEKLKAEIDA 2612
Cdd:PRK12704 61 EAKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKLELLEK-----REEELEkkekELEQKQQELEKKEEELEE 135
|
90 100
....*....|....*....|..
gi 808356960 2613 NIEETRAKISEIAG-KAEEITE 2633
Cdd:PRK12704 136 LIEEQLQELERISGlTAEEAKE 157
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2323-2701 |
1.39e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.11 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2323 KKIQEETEKLDKQKETFEAQKKRAEelaaYLNSAQQL------LKESKS--KADKSNNIAKMLQLTKVENLvaaitDDLE 2394
Cdd:COG5185 77 KKSESSVKARKFLKEKKLDTKILQE----YVNSLIKLpnyewsADILISllYLYKSEIVALKDELIKVEKL-----DEIA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKahELHLQA 2472
Cdd:COG5185 148 DIEASYGEVETGIIKDIFGklTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES--TLLEKA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2473 TTLRQTFDNNKDNTDQAVEAANaFSNLTDTLKNAKAQIDNayeaLSAEPAfaesvqnardkpfpDETKEKidalsktvSQ 2552
Cdd:COG5185 226 KEIINIEEALKGFQDPESELED-LAQTSDKLEKLVEQNTD----LRLEKL--------------GENAES--------SK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2553 DLKE-TEKLKKQLEQLTElseKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANI----------------- 2614
Cdd:COG5185 279 RLNEnANNLIKQFENTKE---KIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIqnltaeieqgqeslten 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2615 -EETRAKISEIAGKA--EEITEKANSAMEGIRLARRN----SVQLNKLAPVIVSKFEELKKLSSARSAKVD-SVSDKVSQ 2686
Cdd:COG5185 356 lEAIKEEIENIVGEVelSKSSEELDSFKDTIESTKESldeiPQNQRGYAQEILATLEDTLKAADRQIEELQrQIEQATSS 435
|
410
....*....|....*
gi 808356960 2687 IKEMIAVARDAANRI 2701
Cdd:COG5185 436 NEEVSKLLNELISEL 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2349-2713 |
1.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2349 LAAYLNSAQQLLKESKSKadKSNNIAKMLQLTKvenlvaaitdDLERVEAAKGEFQKLnvaigniTENLKDKREEMthav 2428
Cdd:COG4717 48 LERLEKEADELFKPQGRK--PELNLKELKELEE----------ELKEAEEKEEEYAEL-------QEELEELEEEL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2429 ttlnetrndvaEALEAAKKRVRRDEKSVDMQLvnaKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKA 2508
Cdd:COG4717 105 -----------EELEAELEELREELEKLEKLL---QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2509 QIDNAYEALSAEpafaesvqnARDKPFPDEtkekidalsKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKY 2588
Cdd:COG4717 171 ELAELQEELEEL---------LEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2589 SKNTLDsiDEKVQEVEKLK---------AEIDANIEETRAKISEIAGKA----------EEITEKANSAMEGIRLARRNS 2649
Cdd:COG4717 233 ENELEA--AALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLflvlgllallFLLLAREKASLGKEAEELQAL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2650 VQLNKLAPVIVSKFEELKKLSSARSAK-VDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSL 2713
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEeLLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2252-2480 |
1.86e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2252 QEVMKRAQRARQSV----RSLAEIALAIGSsskavnvdprlLKEAEETLMTLEAASADqypekaqtvpgkLEEIQKKIQE 2327
Cdd:PRK02224 561 AEAEEEAEEAREEVaelnSKLAELKERIES-----------LERIRTLLAAIADAEDE------------IERLREKREA 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2328 ETEKLDKQKETFEAQKKRAEELAAYLNSAqqllKESKSKADKSNniakmlqltkVENLVAAITDDLERVEAAKGEFQKLN 2407
Cdd:PRK02224 618 LAELNDERRERLAEKRERKRELEAEFDEA----RIEEAREDKER----------AEEYLEQVEEKLDELREERDDLQAEI 683
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2408 VAIGNITENLKDKREEMTHAVTTLN--ETRNDVAEALEAAKKRVRrdeksVDMQLVNAKAHElhlqaTTLRQTFD 2480
Cdd:PRK02224 684 GAVENELEELEELRERREALENRVEalEALYDEAEELESMYGDLR-----AELRQRNVETLE-----RMLNETFD 748
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2298-2802 |
1.99e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.42 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2298 TLEAASADQYPEKAQTvpgKLEEIQKKIQEETEK----LDKQKETFEAQKKRAEElaaylnSAQQLLKESKSKADKSN-N 2372
Cdd:COG3064 4 ALEEKAAEAAAQERLE---QAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEE------EAREAKAEAEQRAAELAaE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2373 IAKmlQLTKVENLVAAITDDLERvEAAKGEfQKLNvaignitENLKDKREEMTHAVTTLNETRndvAEALEAAKKRVRRD 2452
Cdd:COG3064 75 AAK--KLAEAEKAAAEAEKKAAA-EKAKAA-KEAE-------AAAAAEKAAAAAEKEKAEEAK---RKAEEEAKRKAEEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2453 EKSVDMQLVNAKAHELHLQATTLRQTF-DNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNAR 2531
Cdd:COG3064 141 RKAAEAEAAAKAEAEAARAAAAAAAAAaAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2532 DKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEID 2611
Cdd:COG3064 221 VAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2612 ANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMI 2691
Cdd:COG3064 301 AALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2692 AVARDAANRIKLGAHFEKGssldlnipQRVTRSAAHADISFYFRTEQEHGIPLFFGNEETAVGSRAVPTADYVAAEIEYG 2771
Cdd:COG3064 381 ADVEEAAGAGILAAAGGGG--------LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIG 452
|
490 500 510
....*....|....*....|....*....|.
gi 808356960 2772 RpKITVDLGDAPAVVKLDTPVNDGLWRRLNI 2802
Cdd:COG3064 453 K-ALTGDADALLGILKAVALDGGAVLADLLL 482
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3379-3509 |
2.19e-05 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 48.12 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3379 FTFKIRPTSdNGIIFIATNkRTDHIAVMLE-HGR---VVFTYDTGSG--QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIV 3452
Cdd:smart00210 58 TTFRQTPKS-RGVLFAIYD-AQNVRQFGLEvDGRantLLLRYQGVDGkqHTVSFRNLPLADGQWHKLALSVSGSSATLYV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 3453 DDNSYESegaanqnedlIETQPPFYvggVPADLAGFA-RNLVVGVRSQFSGCIKDFKL 3509
Cdd:smart00210 136 DCNEIDS----------RPLDRPGQ---PPIDTDGIEvRGAQAADRKPFQGDLQQLKI 180
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2375-2673 |
2.21e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.62 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2375 KMLQLTKVENLVAAITDDLER------VEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTT-LNET----RNDVAEALE 2443
Cdd:PLN03229 397 RMLKFRKIGGFQEGVPVDPERkvnmkkREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELaLNEMieklKKEIDLEYT 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2444 AAKKRVRRDEKSVDMQLVNAKAH-ELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLT---DTLKNA------------- 2506
Cdd:PLN03229 477 EAVIAMGLQERLENLREEFSKANsQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKyklDMLNEFsrakalsekkska 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2507 ---KAQIDNAYEALSAEPAFAESVQNARDK----------PFPDETKEKIDALSKTVSQDLKETEK---------LKKQL 2564
Cdd:PLN03229 557 eklKAEINKKFKEVMDRPEIKEKMEALKAEvassgassgdELDDDLKEKVEKMKKEIELELAGVLKsmglevigvTKKNK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2565 EQLTELS-EKLRKRKEAVKAGIPKYSKNTLDSIDEKvQEVEKLKAEI-DANIEETRAKISEIAGKAEEITEKANSAMegi 2642
Cdd:PLN03229 637 DTAEQTPpPNLQEKIESLNEEINKKIERVIRSSDLK-SKIELLKLEVaKASKTPDVTEKEKIEALEQQIKQKIAEAL--- 712
|
330 340 350
....*....|....*....|....*....|..
gi 808356960 2643 rlarrNSVQLNklapvivSKFEEL-KKLSSAR 2673
Cdd:PLN03229 713 -----NSSELK-------EKFEELeAELAAAR 732
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1948-1994 |
2.36e-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: 44.27 E-value: 2.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 808356960 1948 CQCNGNNnlTDSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVT 1994
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2286-2510 |
2.67e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 50.06 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2286 PRLLKEAeetlmtLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLD-------KQKETFEAQKK---RAEELAAYLNS 2355
Cdd:pfam13166 266 PAERKAA------LEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPavsdlasLLSAFELDVEDiesEAEVLNSQLDG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2356 AQQLLKEskskadKSNNIAKMLQLTKVENLVAAITDDLerveaakgefQKLNVAIGNitenlkdkreemtHavttlNETR 2435
Cdd:pfam13166 340 LRRALEA------KRKDPFKSIELDSVDAKIESINDLV----------ASINELIAK-------------H-----NEIT 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2436 NDVAEALEAAKKRVRRDEKSvdmqlvnakahelhlQATTLRQTFDNNKDNTDQAVEAA-NAFSNLTDTLKNAKAQI 2510
Cdd:pfam13166 386 DNFEEEKNKAKKKLRLHLVE---------------EFKSEIDEYKDKYAGLEKAINSLeKEIKNLEAEIKKLREEI 446
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2527-2634 |
2.73e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2527 VQNARDkpFPDETKEKID-------ALSKTVSQDLKETEKLKKQLEQL-TELSEKLRKRKEavkagipkYSKNTLDSIDE 2598
Cdd:PRK00409 504 IEEAKK--LIGEDKEKLNeliasleELERELEQKAEEAEALLKEAEKLkEELEEKKEKLQE--------EEDKLLEEAEK 573
|
90 100 110
....*....|....*....|....*....|....*....
gi 808356960 2599 KVQE-VEKLKAEIDANIEETRAKISE--IAGKAEEITEK 2634
Cdd:PRK00409 574 EAQQaIKEAKKEADEIIKELRQLQKGgyASVKAHELIEA 612
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2510-2635 |
2.87e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.93 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2510 IDNAYEALSAepaFAESVQNARDKPFPDET-----------KEKIDALSKTVSQDLKE-TEKLKKQLEQ----LTELSEK 2573
Cdd:cd13769 7 IQKAQEAINN---LAQQVQKQLGLQNPEEVvntlkeqsdnfANNLQEVSSSLKEEAKKkQGEVEEAWNEfktkLSETVPE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2574 LRKRKEAVKAgipkySKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2635
Cdd:cd13769 84 LRKSLPVEEK-----AQELQAKLQSGLQtlvtESQKLAKAISENSQKAQEELQKATKQAYDIAVEA 144
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2317-2651 |
3.70e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKL-DKQKEtFEAQKKRAEEL---AAYLNSAQQLLKESKSKADKSnniakmlqltkVENLVAAIT-D 2391
Cdd:pfam10174 395 KINVLQKKIENLQEQLrDKDKQ-LAGLKERVKSLqtdSSNTDTALTTLEEALSEKERI-----------IERLKEQRErE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2392 DLERVEaakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAE-ALEAAKKRVRRD------EKSVD----MQL 2460
Cdd:pfam10174 463 DRERLE----ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKsleiavEQKKEecskLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2461 VNAKAHELHLQATTlRQTFDNNKDNTDQAV-----EAANAFSNL---------TDTLKNAKAQIDNAYEALSAEPAFAES 2526
Cdd:pfam10174 539 QLKKAHNAEEAVRT-NPEINDRIRLLEQEVarykeESGKAQAEVerllgilreVENEKNDKDKKIAELESLTLRQMKEQN 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2527 VQNARDKPFPDETKEKIDALSKTVS--QDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipKYSkNTLDSIDEKVQEVE 2604
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQLLEEARrrEDNLADNSQQLQLEELMGALEKTRQELDATKA---RLS-STQQSLAEKDGHLT 693
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 808356960 2605 KLKAEIDANIEEtrakISEIAGKA--EEITEK-ANSAMEGIRLARRNSVQ 2651
Cdd:pfam10174 694 NLRAERRKQLEE----ILEMKQEAllAAISEKdANIALLELSSSKKKKTQ 739
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2323-2583 |
3.91e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.10 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2323 KKIQEETEKLDKQKEtfeaqkkRAEElaaylnsAQQLLKESKSKADKSnniakmlqltkvENLVAAIT-------DDLER 2395
Cdd:pfam00261 1 KKMQQIKEELDEAEE-------RLKE-------AMKKLEEAEKRAEKA------------EAEVAALNrriqlleEELER 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2396 VEaakgefQKLNVAIGNITENLKdKREEMTHAVTTLnETR----NDVAEALEAAKKRVRRDEKSVDMQLVNAkahELHLQ 2471
Cdd:pfam00261 55 TE------ERLAEALEKLEEAEK-AADESERGRKVL-ENRalkdEEKMEILEAQLKEAKEIAEEADRKYEEV---ARKLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2472 ATT--LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEalsaepafaesvqnaRDkpfpDETKEKIdalsKT 2549
Cdd:pfam00261 124 VVEgdLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASE---------------RE----DKYEEQI----RF 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 808356960 2550 VSQDLKETE-----------KLKKQLEQLTELSEKLRKRKEAVKA 2583
Cdd:pfam00261 181 LTEKLKEAEtraefaersvqKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2311-2418 |
5.46e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 48.57 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2311 AQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSK-ADKSNNIAKMLQlTKVENLVAAI 2389
Cdd:TIGR04320 249 IPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElANAQAQALQTAQ-NNLATAQAAL 327
|
90 100
....*....|....*....|....*....
gi 808356960 2390 TDDLERVEAAKGEFQKLNVAIGNITENLK 2418
Cdd:TIGR04320 328 ANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
2485-2635 |
5.99e-05 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 45.82 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2485 NTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAepaFAESVQnardkpfpDETKEKIDALSKTVSQdlketekLKKQL 2564
Cdd:pfam07464 4 ELQQSVQKQLGLPSQQEVVETIKENTENLVDQLKQ---VQKSLQ--------EELKKASGEAEEALKE-------LNTKI 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356960 2565 EQLTElseKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2635
Cdd:pfam07464 66 VETAD---KLSEANPEVVQKANELQEKFQSGVQSLVTESQKLAKSISENSQGATEKLQKATKQAYDDAVQA 133
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2320-2620 |
6.04e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.18 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2320 EIqKKIQEETEKLDKQKETFEAQKKRAEElaaylnsaQQLLKESKSKADKSNNIAKMlqltkvENLVAAItddLERVEAA 2399
Cdd:PRK05035 437 EI-RAIEQEKKKAEEAKARFEARQARLER--------EKAAREARHKKAAEARAAKD------KDAVAAA---LARVKAK 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2400 KGEFQKLNVAIGNItenLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTF 2479
Cdd:PRK05035 499 KAAATQPIVIKAGA---RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2480 DNNKDntdqAVEAANAfsnltdtlkNAKAQidnayealSAEPAfAESVQNARDKPFPDETKEKIDALSKTVsqdlketeK 2559
Cdd:PRK05035 576 DPKKA----AVAAAIA---------RAKAK--------KAAQQ-AASAEPEEQVAEVDPKKAAVAAAIARA--------K 625
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2560 LKK-QLEQLTELSEKLRKRKEAVKAGIP--KYSKNTLDSIDEKVQE-VEKLKAEIDANIEETRAK 2620
Cdd:PRK05035 626 AKKaEQQANAEPEEPVDPRKAAVAAAIAraKARKAAQQQANAEPEEaEDPKKAAVAAAIARAKAK 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2489-2700 |
8.74e-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: 47.84 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2489 AVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLT 2568
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2569 ELSEKLRKRKEAVKA-------GIPKYSKNTL-------DSIDEKVQEVEKLKA---EIDANIEETRAKISEIAGKAEEI 2631
Cdd:COG4942 90 KEIAELRAELEAQKEelaellrALYRLGRQPPlalllspEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2632 TEKANSAMEgirLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQ-------IKEMIAVARDAANR 2700
Cdd:COG4942 170 EAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEaeelealIARLEAEAAAAAER 242
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
331-648 |
9.07e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 48.04 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 331 CERCCPGF---VQKQWQAATAHNNF-TCEACNCFGRS--NECEYDAEVDLNKQSIDSQ---GNYEGGGVCKN---CRENT 398
Cdd:pfam03302 1 CDECKPGYelsADKTKCTSSAPCKTeNCKACSNDKREvcEECNSNNYLTPTSQCIDDCakiGNYYYTTNANNkkiCKECT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 399 EGvNCNKCsfgyfrpegvtwNEPQPCKVCDCDPDKHTGACAEETGKCECLPRFVGEDCDQCASGyydapkcKPCECNVNG 478
Cdd:pfam03302 81 VA-NCKTC------------EDQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTG-------KALRYGNDG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 479 TIGDvclpEDGQCPCKAGFGGtfCETCA---DGytnvTAGCVECVCDATGSEHGNCSASTGQ----CECKPAYAGLsCDK 551
Cdd:pfam03302 141 TKGT----CGEGCTTGTGAGA--CKTCGltiDG----TSYCSECATETEYPQNGVCTSTAARatatCKASSVANGM-CSS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 552 CQVGYFgddckfcncdpmGTEGGvCDQTT---GQCLCKEGFAGDKCDRCDIAFY--------GYPNCKACAC-------- 612
Cdd:pfam03302 210 CANGYF------------RMNGG-CYETTkfpGKSVCEEANSGGTCQKEAPGYKlnngdlvtCSPGCKTCTSntvcttcm 276
|
330 340 350
....*....|....*....|....*....|....*..
gi 808356960 613 DGAGITSPECDATSGQCP-CNGNFTgrTCDKCAAGFY 648
Cdd:pfam03302 277 DGYVKTSDSCTKCDSSCEtCTGATT--TCKTCATGYY 311
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2319-2579 |
9.18e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 48.36 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2319 EEIQKKIQEETEKLDKQKETFEAQ-KKRAEELAAYLNSAQQLLKESKSKADK--SNNIAKMLQLTKVENLVAAITDDLER 2395
Cdd:pfam15964 370 ERLEKELASQQEKRAQEKEALRKEmKKEREELGATMLALSQNVAQLEAQVEKvtREKNSLVSQLEEAQKQLASQEMDVTK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2396 VeAAKGEFQkLNVAIGNITENLKDKRE--------------EMTHAVTTLNETRNDVAEALEAAKKRvrRDEKSVDMQLV 2461
Cdd:pfam15964 450 V-CGEMRYQ-LNQTKMKKDEAEKEHREyrtktgrqleikdqEIEKLGLELSESKQRLEQAQQDAARA--REECLKLTELL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2462 NAKAHELHL---QATTLRQTFDNNKdnTDQAVEAANAFSNLTDTLKNAKAQIDNA----YEALSAepafaesvQNArdkp 2534
Cdd:pfam15964 526 GESEHQLHLtrlEKESIQQSFSNEA--KAQALQAQQREQELTQKMQQMEAQHDKTvneqYSLLTS--------QNT---- 591
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 808356960 2535 FPDETKEKIDALSKT---VSQDLK-ETEKLKKQLEQLTELSEKLRKRKE 2579
Cdd:pfam15964 592 FIAKLKEECCTLAKKleeITQKSRsEVEQLSQEKEYLQDRLEKLQKRNE 640
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2536-2723 |
9.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2536 PDETKEKIDALSKTVsQDLKET----EKLKKQLEQLTELSEKLRKRKEA---------VKAGIPKY-------------- 2588
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLERAhealEDAREQIELLEPIRELAERYAAArerlaeleyLRAALRLWfaqrrlelleaele 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2589 -SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKA-EEITEKANSAMEGIRLARRNSVQLNKLA-------PVI 2659
Cdd:COG4913 299 eLRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLaalglplPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2660 VSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANR--------IklgAHFEKGSSldlNIPQRVTR 2723
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelreleaeI---ASLERRKS---NIPARLLA 444
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2207-2702 |
1.19e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.29 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2207 NVFGDAQDILTNSTQI---QNKLVRTKTHSQNSVSSAKNITLNGTEFLQ-EVMKRAQRARQSVrslaeIALAIGSSSKav 2282
Cdd:PTZ00440 1893 DVYKNIQDAYKSSLQIlkySDDIDKKQRDCNKLVEDGNEIYLKSTAINElKNMINSVKNKESA-----ISNKIDNVSN-- 1965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2283 nvdprLLKEAEEtlMTLEAASADQYPEKaqtvpGKLEEIQKK----IQEETE-----KLDKQKETFEAQKKRAEELAAYL 2353
Cdd:PTZ00440 1966 -----KLSELNK--ITCNDESYDEILEK-----EEYEELKDLrnsfNQEKAEtlnnlKLNKIKEDFNSYKNLLDELEKSV 2033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2354 N--SAQQLLKESKSKADKS-NNIAKMLQLTK--VENLVAAITDDLER---VEAAKGEF--QKLNVAIGNITENLKDKREE 2423
Cdd:PTZ00440 2034 KtlKASENIKKIVENKKTSiDAINTNIEDIEkeIESINPSLDELLKKghkIEISRYTSiiDNVQTKISNDSKNINDIEKK 2113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2424 MTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVN--AKAHELHLQAT-----------TLRQTFDNNKDNT--DQ 2488
Cdd:PTZ00440 2114 AQIYLAYIKNNYNSIKKDISTLNEYF--DEKQVSNYILTniDKANKLSSELSeavtnseeiieNIKKEIIEINENTemNT 2191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2489 AVEAANAFSNLTDTLKNAKAQIDNAYEALsaepaFAESVQNARdkpfpdETKEKIDALSKTVSQDLkETEKlKKQLEQLT 2568
Cdd:PTZ00440 2192 LENTADKLKELYENLKKKKNIINNIYKKI-----NFIKLQEIE------NSSEKYNDISKLFNNVV-ETQK-KKLLDNKN 2258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2569 ELSEKLRKRKEAVKAGIPKYSKNTLDSIDE----------KVQEVEKL----KAEID------ANIEETRAKISEIAGKA 2628
Cdd:PTZ00440 2259 KINNIKDKINDKEKELINVDSSFTLESIKTfneiyddiksNIGDLYKLedtnNDELKkvklyiENITHLLNRINTLINDL 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2629 EEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLssARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:PTZ00440 2339 DNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKEEFSKL--LKNIKRNNTLCNNNNIKDFISNIGKSVETIK 2410
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2301-2574 |
1.30e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2301 AASADQYPEKAQtVPGKLEEIQK-KIQEETEKLDKQK--------ETFEAQKKRAEELAAYLNSAQQLLKES-------- 2363
Cdd:PRK11281 29 AASNGDLPTEAD-VQAQLDALNKqKLLEAEDKLVQQDleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAqaelealk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2364 KSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLkdkREEMTHAVTTLNETRNDVAeALE 2443
Cdd:PRK11281 108 DDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERA---QAALYANSQRLQQIRNLLK-GGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2444 AAKKRVRRDEKsvdmQLVNAKAHELHLQATTLRQTFDNNkdntdqaveaanafSNLTDTLKN----AKAQIDNayeaLSA 2519
Cdd:PRK11281 184 VGGKALRPSQR----VLLQAEQALLNAQNDLQRKSLEGN--------------TQLQDLLQKqrdyLTARIQR----LEH 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2520 EPAFAESVQNARDKPFPDETKEKidALSKTVSQDLKETEKLKKQLEQLTELSEKL 2574
Cdd:PRK11281 242 QLQLLQEAINSKRLTLSEKTVQE--AQSQDEAARIQANPLVAQELEINLQLSQRL 294
|
|
| F-BAR_FCHO2 |
cd07673 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ... |
2289-2486 |
1.36e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153357 [Multi-domain] Cd Length: 269 Bit Score: 46.97 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVP---------GKLE----EIQKKIQEETEKLDKQ-KETFEAQKKRAEELAAYLN 2354
Cdd:cd07673 41 IEEAYSRSMTKLAKSASNYSQLGTFAPvwdvfktstEKLAnchlELVRKLQELIKEVQKYgEEQVKSHKKTKEEVAGTLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2355 SAQ--QLLKESKSKAdKSNNIAKMLQLTKvenlvaaitddLERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLN 2432
Cdd:cd07673 121 AVQniQSITQALQKS-KENYNAKCLEQER-----------LKKEGATQREIEKAAVKSKKATESYKLYVEKYALAKADFE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2433 ETRNDVAEALEAAKKRVRRDEKSVDMQLVNAkAHELHLQATTLRQTFDNNKDNT 2486
Cdd:cd07673 189 QKMTETAQKFQDIEETHLIRIKEIIGSYSNS-VKEIHIQIGQVHEEFINNMANT 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2516-2702 |
1.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2516 ALSAEPAFAEsvqnardkPFPDETKEKIDALSKTVSQDLKETEKLKKQLEqltELSEKLRKrkeavkagipkysknTLDS 2595
Cdd:COG3883 6 LAAPTPAFAD--------PQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNE---------------LQAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2596 IDEKVQEVEKLKAEID---ANIEETRAKISEIAgkaeeitekansamegiRLARRNSVQLNKLAPVIVSK-FEE------ 2665
Cdd:COG3883 60 LEALQAEIDKLQAEIAeaeAEIEERREELGERA-----------------RALYRSGGSVSYLDVLLGSEsFSDfldrls 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 808356960 2666 -LKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:COG3883 123 aLSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
701-749 |
1.74e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 808356960 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHH 749
Cdd:smart00180 1 CDCDPGGSASG--TCDPDT-GQ-CECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2318-2520 |
1.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKLD------KQKETFEAQKKRAEELAAYLNSAQQLLKEskskadksnniakmLQLTKVENLVAAITD 2391
Cdd:COG4913 237 LERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2392 DLERVEAAKGEFQKLnvaigniTENLKDKREEMTHAvttLNETRNDVAEALEA--AKKRVRRDEKSVDMQLVNAKAHELH 2469
Cdd:COG4913 303 ELARLEAELERLEAR-------LDALREELDELEAQ---IRGNGGDRLEQLEReiERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2470 LQATTLRQTFDNNKDNTDQAVEAAN----AFSNLTDTLKNAKAQIDNAYEALSAE 2520
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAE 427
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2543-2643 |
2.08e-04 |
|
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: 44.39 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2543 IDALSKTVSQDLKETEKLKKQLEQL-TELSEKLRK-RKEAvkAGIpkyskntldsIDEKVQEVEKLKAEIdanIEETRAK 2620
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAAlAEYEEKLAEaRAEA--AEI----------IAEARKEAEAIAEEA---KAEAEAE 93
|
90 100
....*....|....*....|....
gi 808356960 2621 ISEIAGKAE-EITEKANSAMEGIR 2643
Cdd:COG0711 94 AERIIAQAEaEIEQERAKALAELR 117
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2186-2702 |
3.29e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2186 KEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLV--------------------------RTKTHSQNSVSS 2239
Cdd:PTZ00440 1927 EDGNEIYLKSTAINELKNMINSVKNKESAISNKIDNVSNKLSelnkitcndesydeilekeeyeelkdLRNSFNQEKAET 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2240 AKNITLNGT-EFLQEVMKRAQRARQSVRSL---AEIALAIGSSSKAVNVdprLLKEAEETLMTLEA--ASADQYPEKAQT 2313
Cdd:PTZ00440 2007 LNNLKLNKIkEDFNSYKNLLDELEKSVKTLkasENIKKIVENKKTSIDA---INTNIEDIEKEIESinPSLDELLKKGHK 2083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2314 VPGKL-----EEIQKKIQEETEKLDKQK----ETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTkvEN 2384
Cdd:PTZ00440 2084 IEISRytsiiDNVQTKISNDSKNINDIEkkaqIYLAYIKNNYNSIKKDISTLNEYFDEKQVSNYILTNIDKANKLS--SE 2161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2385 LVAAITDDLERVEAAKGEFQKLN-----VAIGNITENLKDKREEMTHAVTTLN------------------ETRNDVAEA 2441
Cdd:PTZ00440 2162 LSEAVTNSEEIIENIKKEIIEINentemNTLENTADKLKELYENLKKKKNIINniykkinfiklqeienssEKYNDISKL 2241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2442 ----LEAAKKRVRRDEKSVD--MQLVNAKAHEL--HLQATTLR--QTFDNNKDNTDQAVEAANAFSNLT-DTLKNAKAQI 2510
Cdd:PTZ00440 2242 fnnvVETQKKKLLDNKNKINniKDKINDKEKELinVDSSFTLEsiKTFNEIYDDIKSNIGDLYKLEDTNnDELKKVKLYI 2321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2511 DNAYEALSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKETEKLKKQLEQltELSEKLRKRKEAVKAgipKYSK 2590
Cdd:PTZ00440 2322 ENITHLLNRINTLINDLDNYQDE---NYGKDKNIELNNENNSYIIKTKEKINNLKE--EFSKLLKNIKRNNTL---CNNN 2393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2591 NTLDSIDEKVQEVEKLKAEIDANIEEtRAKISEIAGKAEEItekaNSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLS 2670
Cdd:PTZ00440 2394 NIKDFISNIGKSVETIKQRFSSNLPE-KEKLHQIEENLNEI----KNIMNETKRISNVDAFTNKILQDIDNEKNKENNNM 2468
|
570 580 590
....*....|....*....|....*....|....
gi 808356960 2671 SARSAK--VDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:PTZ00440 2469 NAEKIDdlIENVTSHNEKIKSELLIINDALRRVK 2502
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2282-2389 |
3.46e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 43.34 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2282 VNVDpRLLKEAEETlmtlEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKKRAEELAAYLNSAQQL 2359
Cdd:smart00935 4 VDVQ-KILQESPAG----KAAQK-QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseAAREKKEKELQKKVQEFQRK 77
|
90 100 110
....*....|....*....|....*....|..
gi 808356960 2360 LKESKSKADKSNN--IAKMLQltKVENLVAAI 2389
Cdd:smart00935 78 QQKLQQDLQKRQQeeLQKILD--KINKAIKEV 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2276-2532 |
3.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2276 GSSSKAVNVDP--------RLLKEAEEtlmtleAASADQYPEK-AQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRA 2346
Cdd:PRK09510 47 GSVIDAVMVDPgavveqynRQQQQQKS------AKRAEEQRKKkEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2347 EElAAYLNSAQQllKESKSKADKSNNIAKMlqltkvenlvaaitddlerveAAKGEFQKLNVAIGNITENlKDKREEMTH 2426
Cdd:PRK09510 121 EE-AAKQAALKQ--KQAEEAAAKAAAAAKA---------------------KAEAEAKRAAAAAKKAAAE-AKKKAEAEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2427 AVTTLNETRndvAEALEAAKKRVRRDEKSVDMQLVNAKAHELhlqattlrqtfDNNKDNTDQAVEAANAfsnltdtLKNA 2506
Cdd:PRK09510 176 AKKAAAEAK---KKAEAEAAAKAAAEAKKKAEAEAKKKAAAE-----------AKKKAAAEAKAAAAKA-------AAEA 234
|
250 260
....*....|....*....|....*.
gi 808356960 2507 KAQIDNAYEALSAEPAFAESVQNARD 2532
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2284-2494 |
3.83e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2284 VDPRLLKEAEETLMTLEAA-----SADQYPEKAQTVPGKLEEIQKKIqeetEKLDKQKETFEAQKKRAEELAAyLNsaQQ 2358
Cdd:pfam12795 14 AKKKLLQDLQQALSLLDKIdaskqRAAAYQKALDDAPAELRELRQEL----AALQAKAEAAPKEILASLSLEE-LE--QR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2359 LLKESKSKADKSNniakmlQLTKVENLVAAITDDLERVEAAKGEfqkLNVAIGNITENLKDKReemtHAVTTLNETRNDV 2438
Cdd:pfam12795 87 LLQTSAQLQELQN------QLAQLNSQLIELQTRPERAQQQLSE---ARQRLQQIRNRLNGPA----PPGEPLSEAQRWA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356960 2439 AEALEAAKK--------------------RVRRDeksvdmqLVNAKAHELHLQATTLRQTFDN-NKDNTDQAVEAAN 2494
Cdd:pfam12795 154 LQAELAALKaqidmleqellsnnnrqdllKARRD-------LLTLRIQRLEQQLQALQELLNEkRLQEAEQAVAQTE 223
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2161-2682 |
4.03e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2161 IDVLGTAIANISSA-----TIVGARLARNKKEFNDINEITKMLN--DEENSFGNVfgdaqdILTN---STQIQNKLVRTK 2230
Cdd:PTZ00440 2093 IDNVQTKISNDSKNindieKKAQIYLAYIKNNYNSIKKDISTLNeyFDEKQVSNY------ILTNidkANKLSSELSEAV 2166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2231 THSQNSVSSAKNITLNGTE-----FLQEVMKRAQRARQSVR----SLAEIALAIGSSSkavnvdprlLKEAEetlmtlea 2301
Cdd:PTZ00440 2167 TNSEEIIENIKKEIIEINEntemnTLENTADKLKELYENLKkkknIINNIYKKINFIK---------LQEIE-------- 2229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2302 ASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKEtfeaqkKRAEELAAYLNSAQQLLKESKSKADK--SNNIAKMLQL 2379
Cdd:PTZ00440 2230 NSSEKYNDISKLFNNVVETQKKKLLDNKNKINNIKD------KINDKEKELINVDSSFTLESIKTFNEiyDDIKSNIGDL 2303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2380 TKVEnlvaaitddlervEAAKGEFQKLNVAIGNIT------ENLK---DKREEMTHAVTTLNETRNDVAEALEAAKKRVR 2450
Cdd:PTZ00440 2304 YKLE-------------DTNNDELKKVKLYIENIThllnriNTLIndlDNYQDENYGKDKNIELNNENNSYIIKTKEKIN 2370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2451 RDEKSVDMQLVNAKAHELHLQATTLRQTFdnnkDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAepAFAESVQNA 2530
Cdd:PTZ00440 2371 NLKEEFSKLLKNIKRNNTLCNNNNIKDFI----SNIGKSVETIKQRFSSNLPEKEKLHQIEENLNEIKN--IMNETKRIS 2444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2531 RDKPFPDETKEKIDAlSKTVSQDLKETEKLKKQLEQLTELSEKLRKR----KEAVKAGIPKYSK-------------NTL 2593
Cdd:PTZ00440 2445 NVDAFTNKILQDIDN-EKNKENNNMNAEKIDDLIENVTSHNEKIKSElliiNDALRRVKEKKDEmnklfnsltennnNNN 2523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2594 DSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEK----------ANSAMEGIRLAR------RNSVQLNKLAP 2657
Cdd:PTZ00440 2524 NSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENEklkllekakiEESRKERERIESetqednTDEEQINRQQQ 2603
|
570 580
....*....|....*....|....*
gi 808356960 2658 VIVSKFEELKKLSSARSAKVDSVSD 2682
Cdd:PTZ00440 2604 ERLQKEEEQKAYSQERLNREVSGTD 2628
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2317-2558 |
4.73e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.48 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK---------ESKSKADKSNNiakmlQLTKVENlva 2387
Cdd:pfam15818 223 KFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQqqtqantemEAELKALKENN-----QTLERDN--- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2388 aitdDLERVEAAKGEFQKLNV------AIG---NITENLKDKREEMTHAVTTLNETRNDVAEALE--AAKKRVRRDEKSV 2456
Cdd:pfam15818 295 ----ELQREKVKENEEKFLNLqnehekALGtwkKHVEELNGEINEIKNELSSLKETHIKLQEHYNklCNQKKFEEDKKFQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2457 DMQLVNAKAHELHLQATtlrQTFDNNKDNTDQAVEAANA--FSNLTDTLKNAKAqidnayEALSAEPAFAESVQnardkP 2534
Cdd:pfam15818 371 NVPEVNNENSEMSTEKS---ENLIIQKYNSEQEIREENTksFCSDTEYRETEKK------KGPPVEEIIIEDLQ-----V 436
|
250 260
....*....|....*....|....
gi 808356960 2535 FPDETKEKIDAlskTVSQDLKETE 2558
Cdd:pfam15818 437 LEKSFKNEIDT---SVPQDKNQSE 457
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2249-2620 |
4.83e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2249 EFLQEVMKRAQRARQSV---RSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASAdQYPEKAQTVPGKL--EEIQK 2323
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIeeqETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA-QQAAKLQGSDLDRtvQQVNQ 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2324 KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKS-KADKSNNIAKMLQL--------TKVENLVAAITDDLE 2394
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeKLQIGTNLQRRQQFeeqlvelsTEVQSLIREIKDAKE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2395 RV---EAAKGEFQKLNVAIGNI--TEN------LKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNA 2463
Cdd:TIGR00606 910 QDsplETFLEKDQQEKEELISSkeTSNkkaqdkVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2464 KAHELHLQAT--TLRQTFDNNK-------DN-TDQAVEaaNAFSNLTDTLKNAKAQID--------NAYEALSAEPAF-- 2523
Cdd:TIGR00606 990 EKHQEKINEDmrLMRQDIDTQKiqerwlqDNlTLRKRE--NELKEVEEELKQHLKEMGqmqvlqmkQEHQKLEENIDLik 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2524 -AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEK-LRKRKEAVKAGIPKYSKNTLDSIDEKV- 2600
Cdd:TIGR00606 1068 rNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKdLDIYYKTLDQAIMKFHSMKMEEINKIIr 1147
|
410 420
....*....|....*....|....*....
gi 808356960 2601 ---------QEVEKLKAEIDANiEETRAK 2620
Cdd:TIGR00606 1148 dlwrstyrgQDIEYIEIRSDAD-ENVSAS 1175
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
2463-2687 |
5.33e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2463 AKAHELHLQATTLRQTFDNNKDNTDQAVE---AANAFSNLTDTLKNaKAQIDNAYEALSaEPAFAESVqnardkpfpdET 2539
Cdd:COG5325 8 AQSKGNSVRFTDEYKNQHRKEDDALTPTFilsAASVDQELTAVRRS-ISRLGKVYAKHT-EPSFSDKS----------EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2540 KEKIDALSKTVSQDLKETEKLKKqlEQLTELSEKLRKRKEAVKAGIPK---YSKNTLdSIDEKVQEVEKLKAEIDANI-- 2614
Cdd:COG5325 76 EDEIDELSKKVNQDLQRCEKILK--TKYKNLQSSFLQSKLLRDLNTECmegQRIQQK-SAQFRKYQVLQAKFLRNKNNdq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2615 ----EETRAKISEIAGKAEEITEKANSAMEG---IRLARRNSVQLNKLAPVIV---SKFEELKKLSSARSAKVDSVSDKV 2684
Cdd:COG5325 153 hpleEEEDEESLSSLGSQQTLQQQGLSNEELeyqQILITERDEEIKNLARGIYelnEIFRDLGSLVGEQGELVDRIDFNI 232
|
...
gi 808356960 2685 SQI 2687
Cdd:COG5325 233 ENT 235
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2266-2423 |
5.93e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2266 RSLA-EIALAIGssskavnVDPRLLKEA-----------EETLMTLEAASADQyPEKAQTVPGKLEEIQKKIQEETEKLD 2333
Cdd:PRK00409 487 KSNAfEIAKRLG-------LPENIIEEAkkligedkeklNELIASLEELEREL-EQKAEEAEALLKEAEKLKEELEEKKE 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2334 KQKETFEAQKKRAEElaaylnSAQQLLKESKSKADKSnnIAKMLQLTKVENlvAAITDdlERVEAAKgefQKLNVAIGNI 2413
Cdd:PRK00409 559 KLQEEEDKLLEEAEK------EAQQAIKEAKKEADEI--IKELRQLQKGGY--ASVKA--HELIEAR---KRLNKANEKK 623
|
170
....*....|
gi 808356960 2414 TENLKDKREE 2423
Cdd:PRK00409 624 EKKKKKQKEK 633
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
2529-2673 |
5.99e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 42.68 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2529 NARDKPfpDETKEKIdalsKTVSQDLKETEKLKKQL--------EQLTELSEKLRKRKEAVKAGIPKYSKNtlDSIDEKV 2600
Cdd:pfam12718 11 NAQERA--EELEEKV----KELEQENLEKEQEIKSLthknqqleEEVEKLEEQLKEAKEKAEESEKLKTNN--ENLTRKI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2601 QEVEKLKAEIDANIEETRAKISEIAGKAEEiTEKANSAMEgirlARRNsvQLNKlapvivsKFEEL-KKLSSAR 2673
Cdd:pfam12718 83 QLLEEELEESDKRLKETTEKLRETDVKAEH-LERKVQALE----QERD--EWEK-------KYEELeEKYKEAK 142
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
2541-2640 |
6.29e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 43.74 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2541 EKI-DALSKTVSQdlkeTEKLKKQLEQLTELSEKLRKR-KEAVKAG------IPKYSKNTLDSIDEKVQEVEKLKAeida 2612
Cdd:pfam10368 4 EKIyDHLEEAVEL----EKPFEEQQEPLVELEKKEQELyEEIIELGmdefdeIKKLSDEALENVEEREELLEKEKE---- 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 808356960 2613 NIEETRAKISEIAGKAEEI--------TEKANSAME 2640
Cdd:pfam10368 76 SIEEAKEEFKKIKEIIEEIedeelkkeAEELIDAME 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2259-2645 |
6.84e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2259 QRARQSVRSLAEIALAIgssskAVNVDPR-LLKEAEETLMTLEAASADQYpEKAQTVPGKLEEIQKKIQE---------- 2327
Cdd:PRK04863 813 QRLHQAFSRFIGSHLAV-----AFEADPEaELRQLNRRRVELERALADHE-SQEQQQRSQLEQAKEGLSAlnrllprlnl 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2328 -ETEKLDKQKETFEAQKKRAEELAAYLNSAQQllkeskskadksnniakmlQLTKVENLVAAITDDLERVEAAKGEFQKL 2406
Cdd:PRK04863 887 lADETLADRVEEIREQLDEAEEAKRFVQQHGN-------------------ALAQLEPIVSVLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2407 NVAIGNITEN---LKDKREEMTH-----AVTTLNETrNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHelHLQATTLRQT 2478
Cdd:PRK04863 948 QQTQRDAKQQafaLTEVVQRRAHfsyedAAEMLAKN-SDLNEKLRQRLEQAEQERTRAREQLRQAQAQ--LAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2479 FDNNKDNTDQAV-EAANAFSNLT-----DTLKNAKAQIDNAYEALSAepafaesvqnardkpfpdeTKEKIDALSKTVSQ 2552
Cdd:PRK04863 1025 LKSSYDAKRQMLqELKQELQDLGvpadsGAEERARARRDELHARLSA-------------------NRSRRNQLEKQLTF 1085
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2553 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKvqeveKLKAEIDANIEetrakiseiAGKAEEIT 2632
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVER-----RLHRRELAYLS---------ADELRSMS 1151
|
410
....*....|...
gi 808356960 2633 EKANSAMegiRLA 2645
Cdd:PRK04863 1152 DKALGAL---RLA 1161
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
2548-2624 |
7.16e-04 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 41.03 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2548 KTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSknTLDSIDEkvqEVEKLKAEID---ANIEETRAKISEI 2624
Cdd:cd22248 3 QTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDES--VLRDLEE---EIDSLKANIDyvqENITECQSNIMQM 77
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
2400-2652 |
7.22e-04 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 45.05 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2400 KGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAE-------ALEAAKK-----RVRRDEKSVDMQLVNAKAHE 2467
Cdd:smart00806 84 DDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARpaaspspVLASSSSaislaNNPDKLNKEQRAELKSLQRE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2468 LhlqaTTLRQTFDNNkdntdqaveaanaFSNLTDTLKNAKAQIDNAYEAlsaepafAESVQNARDKPFPDETKEKIDALS 2547
Cdd:smart00806 164 L----AVLRQTHNSF-------------FTEIKESIKDILEKIDKFKSS-------SLSASGSSNRAYVESSKKKLSEDS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2548 KTVS------QDLKETEK----------LKKQLEQLTELSEKLRKR----KEAVKAGIPKYSK---NTLDSIDEKVQEVe 2604
Cdd:smart00806 220 DSLLtkvddlQDIIEALRkdvaqrgvrpSKKQLETVQKELETARKElkkmEEYIDIEKPIWKKiweAELDKVCEEQQFL- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 808356960 2605 KLKAEIDANIEETRAKISEIAGKAEEITEKansAMEGIRLARRNSVQL 2652
Cdd:smart00806 299 TLQEDLIADLKEDLEKAEETFDLVEQCCEE---QEKGPSKNRNKPVSL 343
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2283-2419 |
8.48e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.67 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2283 NVDPRLLKEAEETLMTL---EAASADQYPEKAQTV--------------PGKLEEIQKKIQE---------ETEKLDK-Q 2335
Cdd:cd22656 106 ATDDEELEEAKKTIKALlddLLKEAKKYQDKAAKVvdkltdfenqtekdQTALETLEKALKDlltdeggaiARKEIKDlQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2336 KETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTK--VENLVAAITDDLERVEAAKGEFQKLNVAIGNI 2413
Cdd:cd22656 186 KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADtdLDNLLALIGPAIPALEKLQGAWQAIATDLDSL 265
|
....*.
gi 808356960 2414 TENLKD 2419
Cdd:cd22656 266 KDLLED 271
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2504-2709 |
1.01e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2504 KNAKAQIDNAYEALSAEpafAESVQNARDKPFPDETKEKI----DALSKTVSQDLKETEKLKKQL----EQLTELSEKLR 2575
Cdd:cd22656 83 QNAGGTIDSYYAEILEL---IDDLADATDDEELEEAKKTIkallDDLLKEAKKYQDKAAKVVDKLtdfeNQTEKDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2576 KRKEAVKAGIPKYSK-NTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQL-N 2653
Cdd:cd22656 160 TLEKALKDLLTDEGGaIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLlA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2654 KLAPVIVSkFEELKKLSSARSAKVDSVSDKVSQIkemiavARDAANRIKLGAHFEK 2709
Cdd:cd22656 240 LIGPAIPA-LEKLQGAWQAIATDLDSLKDLLEDD------ISKIPAAILAKLELEK 288
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
2263-2511 |
1.07e-03 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 43.81 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2263 QSVRSLAEIALAIGSSSKAVNvdprllKEAEETLMTLE--AASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFE 2340
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELA------ERMEELSASIEevAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2341 AQKKRAEELAAYLNSAQQLLKESKSKADKSNniakMLQLtkveNlvAAItddlervEAA------KG------EFQKL-- 2406
Cdd:smart00283 78 EAVSAVEELEESSDEIGEIVSVIDDIADQTN----LLAL----N--AAI-------EAArageagRGfavvadEVRKLae 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2407 NVA---------IGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDM-QLVNAKAHElhlQATTLR 2476
Cdd:smart00283 141 RSAesakeieslIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLvQEIAAATDE---QAAGSE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 808356960 2477 Q---TFDN----NKDNTDQAVEAANAFSNLTDTLKNAKAQID 2511
Cdd:smart00283 218 EvnaAIDEiaqvTQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
2289-2447 |
1.34e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 43.93 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVP----GKLEEIQKKI---QEETEKLDKQKETFEAQKKRA----EELAAYLNSAQ 2357
Cdd:pfam15294 95 IAEFEEREFTSSNKKPNFELNKPKLEPlnegGGSALLHMEIerlKEENEKLKERLKTLESQATQAldekSKLEKALKDLQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2358 QLLKESKSKADKSNNIAKMlqltkvENLVAAITDDLErveaakgefQKLNvaigNITENLKDKREEMThavttlnETRND 2437
Cdd:pfam15294 175 KEQGAKKDVKSNLKEISDL------EEKMAALKSDLE---------KTLN----ASTALQKSLEEDLA-------STKHE 228
|
170
....*....|...
gi 808356960 2438 ---VAEALEAAKK 2447
Cdd:pfam15294 229 llkVQEQLEMAEK 241
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
298-344 |
1.69e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808356960 298 CVCN--GHA-VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQ 344
Cdd:smart00180 1 CDCDpgGSAsGTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2590-2687 |
1.70e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 41.60 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2590 KNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKA-EEITEKANSAMEGIR--LARRNSVQLNKLApvivSKFEEL 2666
Cdd:PRK08476 44 KNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKAiAKAKEEAEKKIEAKKaeLESKYEAFAKQLA----NQKQEL 119
|
90 100
....*....|....*....|..
gi 808356960 2667 K-KLSSARSAKVDSVSDKVSQI 2687
Cdd:PRK08476 120 KeQLLSQMPEFKEALNAKLSKI 141
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2537-2686 |
1.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2537 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRK-------EAVKAGIPKYSKNtLDSI-DEKvqEVEKLKA 2608
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrleleiEEVEARIKKYEEQ-LGNVrNNK--EYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2609 EIDAN---IEETRAKISEIAGKAEEITEKANSAMEgiRLARRNSvQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVS 2685
Cdd:COG1579 97 EIESLkrrISDLEDEILELMERIEELEEELAELEA--ELAELEA-ELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 808356960 2686 Q 2686
Cdd:COG1579 174 P 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2538-2697 |
1.86e-03 |
|
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: 44.28 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2538 ETKEKIDALSKTVSqdLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNtLDSIDEKVQEVEKLKAEIDANIEET 2617
Cdd:TIGR02168 217 ELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2618 RAKISEIAGKAEEITEKANSAMEGIrlaRRNSVQLNKLApvivSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA 2697
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQL---EELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
2358-2455 |
2.23e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2358 QLLKESKSKAD----KSNNIAKMLQLTKvENLVAAITDdlerVEAAKGEFQKLNVAIGNITENLKDkreeMTHAVTTLNE 2433
Cdd:pfam10473 10 EKLKESERKADslkdKVENLERELEMSE-ENQELAILE----AENSKAEVETLKAEIEEMAQNLRD----LELDLVTLRS 80
|
90 100
....*....|....*....|..
gi 808356960 2434 TRNDVAEALEAAKKRVRRDEKS 2455
Cdd:pfam10473 81 EKENLTKELQKKQERVSELESL 102
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2317-2451 |
2.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2317 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKsnNIAKmlQLTKVENlVAAITddlerV 2396
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE--LIEE--QLQELER-ISGLT-----A 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2397 EAAKGEfqklnvaignITENLKDK-REEMTHAVttlnetRNDVAEALEAAKKRVRR 2451
Cdd:PRK12704 153 EEAKEI----------LLEKVEEEaRHEAAVLI------KEIEEEAKEEADKKAKE 192
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2318-2468 |
3.31e-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: 40.93 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKLDKQKEtfEAQKKRAEelaaylnsAQQLLKESKSKAdksnniAKMLQLTK--VENLVAAITDDLER 2395
Cdd:COG0711 29 LDERQEKIADGLAEAERAKE--EAEAALAE--------YEEKLAEARAEA------AEIIAEARkeAEAIAEEAKAEAEA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356960 2396 vEAAKgefqklnvaignITENLKDKREEMTHAVttLNETRNDVAE-ALEAAKKRVRR--DEKSVDmQLVNAKAHEL 2468
Cdd:COG0711 93 -EAER------------IIAQAEAEIEQERAKA--LAELRAEVADlAVAIAEKILGKelDAAAQA-ALVDRFIAEL 152
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
2944-3038 |
3.35e-03 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 40.83 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2944 GLLFFVGKDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGeteVLEGDVPGKDSE 3023
Cdd:pfam13385 35 RAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRLYVNG---VLVGSSTLTGGP 111
|
90
....*....|....*.
gi 808356960 3024 MSVTEF-LYIGGTPSG 3038
Cdd:pfam13385 112 PPGTGGpLYIGRSPGG 127
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
2554-2643 |
4.97e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 40.18 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2554 LKETEKLKKQLEQLTELSEKLRKRKEAVkagipkyskntldsidekVQEVEKLKAEIDANIEETRA----KISEIAGKAE 2629
Cdd:cd21759 71 LRKIRALEKQLKEMEEIASQLKKDKDKW------------------TKQVKELKKEIDALIKKIKTndmiTRKEIDKLYN 132
|
90
....*....|....
gi 808356960 2630 EITEKANSAMEGIR 2643
Cdd:cd21759 133 ALVKKVDKQLAELQ 146
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2378-2533 |
5.12e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2378 QLTKVENLVAAITDDL-----ERVEAAKGEFQKlnvAIGNITENLKDKREEMTHAVT-TLNETRNDVAEALEAAKKRVRR 2451
Cdd:pfam01442 12 YAEELQEQLGPVAQELvdrleKETEALRERLQK---DLEEVRAKLEPYLEELQAKLGqNVEELRQRLEPYTEELRKRLNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2452 DEKSVdMQLVNAKAHELHLQA----TTLRQTF----DNNKDNTDQAVEAANAfsNLTDTLKNAKAQIDNAYEALSAepAF 2523
Cdd:pfam01442 89 DAEEL-QEKLAPYGEELRERLeqnvDALRARLapyaEELRQKLAERLEELKE--SLAPYAEEVQAQLSQRLQELRE--KL 163
|
170
....*....|
gi 808356960 2524 AESVQNARDK 2533
Cdd:pfam01442 164 EPQAEDLREK 173
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2289-2446 |
5.42e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2289 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKK---RAEELAAYLNSAQQLLKES 2363
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYleELQAKlgqNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2364 KSKAdksnniAKMLQlTKVENLVAAITDDLER-VEAAKGEF--------QKLNVAIGNITENLKDKREEM-THAVTTLNE 2433
Cdd:pfam01442 86 LNAD------AEELQ-EKLAPYGEELRERLEQnVDALRARLapyaeelrQKLAERLEELKESLAPYAEEVqAQLSQRLQE 158
|
170
....*....|...
gi 808356960 2434 TRNDVAEALEAAK 2446
Cdd:pfam01442 159 LREKLEPQAEDLR 171
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
2555-2616 |
5.53e-03 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 38.22 E-value: 5.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356960 2555 KETEKLKKQLEQLTELSEKLRKRKEAVKAgipKYSKNTLDSIDEKVQEVEKLKAEIDANIEE 2616
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEA---QLADPELYSDYEKLQELSAELEELEAELEE 59
|
|
| 3keto-disac_hyd |
pfam06439 |
3-keto-disaccharide hydrolase; This family has structural similarity to an endo-1,3-1,4-beta ... |
3510-3634 |
5.75e-03 |
|
3-keto-disaccharide hydrolase; This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. A member containing this domain, BT2157 from B. thetaiotaomicron, hydrolyses 3-ketotrehalose during trehalose degradation that proceeds through a 3-keto-glycoside intermediate. Other members containing this domain are involved in disaccharide catabolism with 3-ketoglycoside intermediates.
Pssm-ID: 399445 Cd Length: 182 Bit Score: 40.82 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 3510 NGKSLDNGKEFGTEQCSQFS-EPGM----YFGKDGGYAIVQKDYEvglTFGLEVEMR--PRMKNGILF----SVGVLEYI 3578
Cdd:pfam06439 7 NGKDLDGWKGAGGGGVGGWKvEDGVlvdgSSGKGGGFLITKKKFG---DFELHLEFKitPGGNSGVFFrsqpEEGQDFVK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 808356960 3579 TVEF-VNGSIKTTVESGSGGEELWHHPDIENQYC-DGQWQSFKISKKRNLLTVAVNGK 3634
Cdd:pfam06439 84 GYEVqILDSGGDLGLNRGTGSLYGEIAPSANATFpPGEWNTYEIIVKGNRITVWLNGV 141
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
2540-2637 |
5.98e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 39.78 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2540 KEKIDALSK---TVSQDLKETEKLKKQLEQLTELSEKlrkrKEA---------VKAGIPKYSKNTLD---------SIDE 2598
Cdd:cd23160 13 EQQAEALQQqieLLQASINELNRAKETLEELKKLKEG----TEIlvpigggsfVKAKIKDTDKVLVNigagvvvekTIDE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 808356960 2599 KVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANS 2637
Cdd:cd23160 89 AIEILEKRIKELEKALEKLQEQLQQIAQRLEELEAELQE 127
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
2536-2643 |
6.85e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 39.47 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2536 PDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVkagipkysKNTL---DSIDEKVQEVEKLKAEIda 2612
Cdd:pfam05103 20 PDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETL--------QNTLilaQETAEEVKANAQKEAEL-- 89
|
90 100 110
....*....|....*....|....*....|.
gi 808356960 2613 NIEETRAKISEIAGKAEEITEKANSAMEGIR 2643
Cdd:pfam05103 90 IIKEAEAKAERIVDDANNEVKKINDEIEELK 120
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2552-2702 |
7.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2552 QDL-KETEKLKKQLEQLTELSEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEE 2630
Cdd:COG1579 13 QELdSELDRLEHRLKELPAELAELEDELAALEA--------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356960 2631 I-TEKANSAMEG-IRLARRNSVQLNKlapVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2702
Cdd:COG1579 85 VrNNKEYEALQKeIESLKRRISDLED---EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2318-2450 |
7.70e-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: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2318 LEEIQKKIQEETEKLDKQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAItddlerVE 2397
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKE--EAEELLAE--------YEEKLAEARAEAQEIIEEAR----KEAEKIKEEI------LA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 808356960 2398 AAKGEFQKLnvaignitenLKDKREEMTHAVT-TLNETRNDVAE-ALEAAKKRVR 2450
Cdd:cd06503 88 EAKEEAERI----------LEQAKAEIEQEKEkALAELRKEVADlAVEAAEKILG 132
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
2615-2699 |
7.96e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356960 2615 EETRAKISEiagKAEEITEKANSAMEGIRLarrnsvQLNKLAPVIVSKFEELKK-LSSARSAKVDSVSDKVSQIKEMIAV 2693
Cdd:COG4980 30 KETRKKLKD---KADDLKDKAEDLKDELKE------KASELSEEAKEKLDELIEeIKEKIEELKEEVEPKIEELKEEAEK 100
|
....*.
gi 808356960 2694 ARDAAN 2699
Cdd:COG4980 101 LQKEVE 106
|
|
| |
