|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
24-296 |
2.36e-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: 2.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 24 FTYSQVLTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGstqytplnsysyqddeqqkswsqyenpMVRGGHGCGH 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGE----PGPERYCKLVG---------------------------HTEQGKKCDY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 104 CNAGNE-NSHPAANMVDGNN----SWWMSPPLSRGLQhnEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERStDHGKT 178
Cdd:smart00136 50 CDARNPrRSHPAENLTDGNNpnnpTWWQSEPLSNGPQ--NVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 179 YQPWFNFAenaAECMRRFGMESLSPISE--DDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNV 256
Cdd:smart00136 126 WQPWQYFS---SDCRRTFGRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71991177 257 RLRLLGTRTLQGHLMDMNewrdPTVTRRYFYAIKEIMIGG 296
Cdd:smart00136 203 RVRLTRLRTLGDELMDDR----PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
30-296 |
8.37e-75 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 249.42 E-value: 8.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 30 LTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGSTqytplnsysyqddeqqkswsqyenpmvrGGHGCGHCNAGNE 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGL----NGPERYCILSGLE----------------------------GGKKCFICDSRDP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 110 -NSHPAANMVDGNN----SWWMSPPLSrgLQHNEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERSTDHGKTYQPWFN 184
Cdd:pfam00055 49 hNSHPPSNLTDSNNgtneTWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 185 FAenaAECMRRFGM-ESLSPISEDDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNVRLRLLGT 263
Cdd:pfam00055 126 FA---SDCRRTFGRpSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRL 202
|
250 260 270
....*....|....*....|....*....|...
gi 71991177 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 ... |
2578-2719 |
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 71991177 2578 SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKK 2657
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2658 LSSARSakvdSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAAHADI 2719
Cdd:pfam06009 81 LEVNSS----SLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1658-1782 |
2.03e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 146.64 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1658 SVYFNVPIEKK-DYTTSYGLKLTFKLSTVP-RGGRKSMNADadVRLTGANMTIEYWAsEQPTNPEEQFTVKCKLVPENFL 1735
Cdd:smart00281 4 PVYWVAPEQFLgDKVTSYGGKLRYTLSFDGrRGGTHVSAPD--VILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71991177 1736 TAEGKTVTREELMKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEP 1782
Cdd:smart00281 81 YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3342-3499 |
7.06e-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: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3342 GFNFGSQQYSRIEydiLPEAIDKSGEFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSI 3420
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSFRTTSPNGLLLyAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991177 3421 IDGRWHTIKVSRRGKSAHLIVDDNSYEsEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLN 3499
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVV-ESGSPGGSALLNLDGPLYLGGLPEDL----KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2898-3046 |
3.05e-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: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2898 VVSLDGEGYTSYKPSHwNPRKATKISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGqWITESSNYN 2975
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGsqNGGDFLALELEDGRLVLRYDLGSGSL-VLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991177 2976 DGKWHTVSIVREEKHVKIMIDGETeVLEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3046
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGER-VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVspGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
3367-3501 |
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 71991177 3367 EFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSII-DGRWHTIKVSRRGKSAHLIVDDn 3444
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLnDGQWHRVAVERNGRSVTLSVDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 3445 SYESEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3501
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDL----KLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2921-3046 |
3.33e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2921 KISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGE 2998
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGskGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71991177 2999 TEVlEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3046
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 ... |
3372-3501 |
5.08e-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: 5.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3372 IRPTSDNGIIFIATNKRTDHIAVMLEHGRVVFTYDTGSG-QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDnSYESEG 3450
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG-QTVVSS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 3451 AANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3501
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLL----LLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2693-2864 |
1.57e-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: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2693 GAHFEKGSSLDLNIPQRVTRsaaHADISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAP 2772
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPNGLLLYAGSQ---------NGGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2773 AVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAETKSSVAggnksvLNLNqqiSRLFVGGVPTSARISKDLYNR 2852
Cdd:cd00110 69 LVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAL------LNLD---GPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 71991177 2853 DFVGDIESLKLH 2864
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2926-3048 |
3.88e-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: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2926 FLTFSPHGLLFFVG-KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGETeVLEG 3004
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT-VVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71991177 3005 DVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKLGS 3048
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVraGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3521-3671 |
8.03e-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: 8.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3521 GMYFGKDGGYAIVQKDyEVGLTFGLEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGgeELWHHPDieN 3597
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSG--SLVLSSK--T 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 3598 QYCDGQWQSFKISKKRNLLTVAVNGKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3671
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLnLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2718-2866 |
1.10e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2718 DISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAPAVVKLD-TPVNDGLWRRLNIERIGK 2796
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSK---------GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2797 TVSVTLSKPNSVETaetkssVAGGNKSVLNLNqqiSRLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2866
Cdd:smart00282 72 SVTLSVDGGNRVSG------ESPGGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3545-3671 |
4.11e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3545 LEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGGEELWHHPdieNQYCDGQWQSFKISKKRNLLTVAVN 3621
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgggDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 3622 GKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3671
Cdd:smart00282 79 GGNRVSGESPGGLTILnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1669-1795 |
7.96e-25 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 102.73 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1669 DYTTSYGLKLTFKLSTVPRGGRKSMNADADVRLTGANMTIEYWASEQPT-NPEEQFTVKCKLVPENFLTAEGKTVTREEL 1747
Cdd:pfam00052 11 NKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPpDPGQEQTYSVRLHEENWRDSDGAPVSREDF 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71991177 1748 MKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEPNGVDSVikASSVE 1795
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 ... |
3549-3672 |
3.42e-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: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3549 MRPRMKNGILFSVGVL--EYITVEFVNGSIKTTVESGSGGEELWHHpdiENQYCDGQWQSFKISKKRNLLTVAVNGKAHL 3626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgsDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71991177 3627 KILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSFG 3672
Cdd:pfam02210 78 SSLPPGESLLLnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2278-2906 |
6.79e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK------- 2350
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkke 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2351 ESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAvttlNETR 2424
Cdd:PTZ00121 1375 EAKKKADaakkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKA----DEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2425 NDVAEALEA--AKKRVRRDEKSVDMQlvnAKAHELHlQATTLRQTFDNNKDNTDQAVEAANAfSNLTDTLKNAKaQIDNA 2502
Cdd:PTZ00121 1451 KKAEEAKKAeeAKKKAEEAKKADEAK---KKAEEAK-KADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAE-EAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2503 YEALSAEPAF-AESVQNARDKPFPDETKeKIDALSKtvSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNT 2581
Cdd:PTZ00121 1525 DEAKKAEEAKkADEAKKAEEKKKADELK-KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2582 LDSIDEKVQEV-----EKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELK 2656
Cdd:PTZ00121 1602 EEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2657 KLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAahadisfyfRTEQEHGIPLFFG 2736
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---------EEDKKKAEEAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2737 NEETAVGSRAVPTADYVAAEIEYGRPKIT---VDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAET 2813
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2814 KsSVAGGNKSVLNLNQQISRLFVGGVPTS-------ARISKDLYNR-DFVGDIESLKLHgEPIGLwNSREKGNTNVNGAQ 2885
Cdd:PTZ00121 1833 K-EVADSKNMQLEEADAFEKHKFNKNNENgedgnkeADFNKEKDLKeDDEEEIEEADEI-EKIDK-DDIEREIPNNNMAG 1909
|
650 660
....*....|....*....|.
gi 71991177 2886 KKPKITDNadelvvSLDGEGY 2906
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 ... |
2723-2866 |
3.52e-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: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2723 FRTEQEHGIPLFFGNEETavgsravptaDYVAAEIEYGRPKITVDLGDAPAVVK-LDTPVNDGLWRRLNIERIGKTVSVt 2801
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS----------DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTL- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2802 lskpnSVETAETKSSVAGGNKSVLNLNQQisrLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2866
Cdd:pfam02210 70 -----SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2306-2620 |
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 71991177 2306 KLEEIQKKIQEETEKLDKQKetfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQ--LTKVENLVAAITDDLE 2383
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEAAKGEFQKLNVAIGNITENLKDKREEMthavTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHElhlQATT 2463
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQLKEELKALREAL--DELRAELTLLNEEAAN---LRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2464 LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFP--DETKEKIDALSKTVSQ 2541
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2542 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKA 2617
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 71991177 2618 EEI 2620
Cdd:TIGR02168 982 KEL 984
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2404-2704 |
4.96e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2404 ENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvrRDEKsvdmqlvNAKAHELHLQATTLRQTFD--NNKdntdqavea 2481
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK--RDEL-------NAQVKELREEAQELREKRDelNEK--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2482 anaFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNARDKPFPDETKEKIDALSKTVsqdlkETEKL-----KKQLEQL 2556
Cdd:COG1340 73 ---VKELKEERDELNEKLNELREEL--DELRKELAELNKAGGSIDKLRKEIERLEWRQ-----QTEVLspeeeKELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2557 TELSEKLRKRKEAVKAGipKYSKNTLDSIDEKVQEVEKLKAEIDA---NIEETRAKISEIAGKAEEITEKANSAMEGIRL 2633
Cdd:COG1340 143 KELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2634 ARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQiKEMIAVARDAANRiklgahFEKGSSLDL 2704
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. |
1415-1463 |
5.13e-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: 68.53 E-value: 5.13e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1415 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPECIKCQC 1463
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1414-1457 |
5.97e-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: 5.97e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1414 SCDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPE 1457
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 |
9.22e-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: 67.76 E-value: 9.22e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 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. |
1506-1556 |
1.11e-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: 1.11e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 1506 CGCHPQGSEGGNlvCDPESGQCLCRESMGGRQCDRCLAGFYGFPHCYGCSC 1556
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1415-1458 |
1.32e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.32e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 1415 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYY--NFPEC 1458
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2182-2682 |
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 71991177 2182 EITKMLNDEENSfgnvfgdAQDILTNSTQIQNKLvrtkthsqnsvssaKNITlngteFLQEvmkraqRARQSVRSLAE-I 2260
Cdd:pfam05483 230 EYKKEINDKEKQ-------VSLLLIQITEKENKM--------------KDLT-----FLLE------ESRDKANQLEEkT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2261 ALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQypekaQTVPGKLEEIQKKIQEETEKLDKQKEtfEAQKKRAE---- 2336
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-----KALEEDLQIATKTICQLTEEKEAQME--ELNKAKAAhsfv 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2337 --ELAAYLNSAQQLLKESKSKADKSNNIAKML--QLTKVENLVAAITD-------DLERVEAAKGEFQKL---NVAIGNI 2402
Cdd:pfam05483 351 vtEFEATTCSLEELLRTEQQRLEKNEDQLKIItmELQKKSSELEEMTKfknnkevELEELKKILAEDEKLldeKKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2403 TENLKDKREEMTHAVTTLNETRNDV---AEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK---DNTD 2476
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2477 QAVEAANAFSNLTDTLKNAK---AQIDNAYEAlsaEPAFAESVQNARD--KPFPDETKEKIDALSKTVSQDLKETEKLKK 2551
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEErmlKQIENLEEK---EMNLRDELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2552 QLEQLTELSEKLRKRKEavkagipkyskNTLDSIDEKVQEVEKLKAEIDA-----NIEETRA-----KISEIAGKAEEIT 2621
Cdd:pfam05483 588 QMKILENKCNNLKKQIE-----------NKNKNIEELHQENKALKKKGSAenkqlNAYEIKVnklelELASAKQKFEEII 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2622 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKvdsvsdkvsQIKEMIAV 2682
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 |
2.87e-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: 2.87e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 756 CDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRLNSYNQMGC 806
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
564-605 |
4.06e-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: 4.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-658 |
4.28e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 4.28e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCRGCEC 658
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
609-657 |
8.78e-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: 8.78e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 609 ACACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCR-GCE 657
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
755-807 |
1.24e-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: 1.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 71991177 755 SCDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRlNSYNQMGCE 807
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
656-703 |
1.32e-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: 1.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 656 CECLLSGAKGQTCDSN-GQCYCKGNFEGERCDRCKPNFYNFPICEECNC 703
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1506-1549 |
1.42e-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: 61.60 E-value: 1.42e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1506 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYGFP 1549
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
756-799 |
2.38e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 756 CDCNVNGTISglNTCDLKTGQCMCKKNADGRRCDQCADGFYRLN 799
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
519-564 |
2.52e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.52e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFC 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
564-605 |
2.54e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.54e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1506-1551 |
9.25e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.25e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 1506 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYG--FPHC 1551
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2037-2081 |
9.61e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.61e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 2037 CHCGTA-AFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHGC 2081
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2483-2691 |
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 71991177 2483 NAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTEL 2559
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL--EEVLREINEISSelpELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2560 SEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKlkaeidaNIEETRAKISEIAGKAEEITEKANSAMEGIRlarrnsv 2639
Cdd:PRK03918 240 IEELEKELESLEG--------SKRKLEEKIRELEE-------RIEELKKEIEELEEKVKELKELKEKAEEYIK------- 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2640 qLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:PRK03918 298 -LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2084-2129 |
2.08e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGC 2129
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
519-566 |
2.79e-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: 2.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 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 |
4.83e-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: 4.83e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 471 PCECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTAGCVECV 520
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-656 |
5.17e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 5.17e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 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 |
5.54e-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: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 855 QYEAEDAHTEDQKPVRFA---VDPEQFADFSWRGYAVFSPiqdkilidVDITKATVYRLLFRYRNPTSVPV-TATVTINP 930
Cdd:cd02795 1 RIEAEDATLTGGTAVSTAagaSGGGYVIGFSSGGDSVTFT--------VTVPKAGTYRLAVRYASPNGNGSrSVSLDGNG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 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 |
9.03e-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: 9.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFP 696
Cdd:cd00055 2 CDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2037-2080 |
9.21e-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: 9.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71991177 2037 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHG 2080
Cdd:cd00055 2 CDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1829-1872 |
1.25e-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: 1.25e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1829 PCECNGHSA---TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1872
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
808-854 |
1.92e-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: 1.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 808 SCHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHYFPTLWHN 854
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
656-701 |
2.09e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFPiCEEC 701
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2248-2758 |
3.68e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2248 QRARQSVRSLAEIALAIGSSSKAV--NVDPRLLKEAE---ETLMTLEAASADQYPEKAQTVPGKLEEiqkkiqEETEKLD 2322
Cdd:NF041483 629 AQAEQEAERLRTEAAADASAARAEgeNVAVRLRSEAAaeaERLKSEAQESADRVRAEAAAAAERVGT------EAAEALA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2323 KQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAITDdleRVEAAKGEFQKLnvaignI 2402
Cdd:NF041483 703 AAQE--EAARRRRE--------AEETLGSARAEADQERERAR----EQSEELLASARK---RVEEAQAEAQRL------V 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2403 TEnlKDKR--EEMTHAVTTLNETRNDVA--------------EALEAAKKRVRRdEKSVDMQLVNAKAHelhlqATTLRQ 2466
Cdd:NF041483 760 EE--ADRRatELVSAAEQTAQQVRDSVAglqeqaeeeiaglrSAAEHAAERTRT-EAQEEADRVRSDAY-----AERERA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2467 TFDNNK--DNTDQAVEAANAFSNLT-------------DTLKNAKAQIDNAYEAL-SAEPAFAESVQNARDkpfpDETKE 2530
Cdd:NF041483 832 SEDANRlrREAQEETEAAKALAERTvseaiaeaerlrsDASEYAQRVRTEASDTLaSAEQDAARTRADARE----DANRI 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALSKT---VSQDLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAgipkyskntldsidEKVQEVEKLKAEIDANIEET 2606
Cdd:NF041483 908 RSDAAAQAdrlIGEATSEAERLTAEARAEAErLRDEARAEAERVRA--------------DAAAQAEQLIAEATGEAERL 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2607 RAKISEIAGKAEEITE---------KANSAMEGIRL-------------------ARRNSVQLNKLAPVIVSKFEELKKL 2658
Cdd:NF041483 974 RAEAAETVGSAQQHAErirteaervKAEAAAEAERLrteareeadrtldearkdaNKRRSEAAEQADTLITEAAAEADQL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2659 -SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEkGSSLdlnipqrVTRSAAHADisfyfrteqehgiPLFFG- 2736
Cdd:NF041483 1054 tAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVE-GNSL-------VEKARTDAD-------------ELLVGa 1112
|
570 580
....*....|....*....|...
gi 71991177 2737 -NEETAVGSRAVPTADYVAAEIE 2758
Cdd:NF041483 1113 rRDATAIRERAEELRDRITGEIE 1135
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1990-2034 |
3.84e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1990 CECSQCGS--QYCDNKSGGCECKINVEGDSCDRCKPDHWGFSkCQGC 2034
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. |
1830-1877 |
3.94e-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: 3.94e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 1830 CECNGH---SATCDPDTGICtDCEHNTNGDHCEFCNEGHYGNAtNGSPYDC 1877
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2084-2130 |
4.63e-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: 4.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPT--YGCR 2130
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
472-516 |
5.30e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 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. |
1554-1602 |
5.33e-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: 5.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLSAENPLGC 1602
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
519-559 |
6.12e-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: 6.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 71991177 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGD 559
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1936-1987 |
1.27e-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: 1.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 1936 PCQCNGNNNLtdSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVTAKNC 1987
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. |
2037-2086 |
1.71e-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: 1.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2037 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYgeHGCDKCDC 2086
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL--PSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2526-2658 |
1.74e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2526 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLR-KRKEAVKagipkyskntldSIDEKVQEVEKLKAEIDANIE 2604
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNA------------QVKELREEAQELREKRDELNE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2605 etraKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2658
Cdd:COG1340 72 ----KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL 121
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1989-2035 |
1.97e-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: 52.74 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1989 SCECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGF-SKCQGCQ 2035
Cdd:cd00055 1 PCDCNGHGSLsgQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1554-1603 |
3.15e-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: 3.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLsAENPLGCV 1603
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 |
4.13e-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: 4.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 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. |
2084-2132 |
4.74e-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: 51.59 E-value: 4.74e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGCRRC 2132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2308-2694 |
7.18e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2308 EEIQKKIQEETEkLDKQKETFEAQKKR----AEELAAYLNS-AQQLLKESKSKADKSnniakmlqltkvenLVAAitddl 2382
Cdd:NF041483 124 EAVQRRQQLDQE-LAERRQTVESHVNEnvawAEQLRARTESqARRLLDESRAEAEQA--------------LAAA----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2383 eRVEAAKgefqklnvaignITEnlkDKREEMThavttlNETRNDVAEAlEAAKKRVRRDEKsvdmQLVNA---KAHELHL 2459
Cdd:NF041483 184 -RAEAER------------LAE---EARQRLG------SEAESARAEA-EAILRRARKDAE----RLLNAastQAQEATD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2460 QATTLRQTFDNNKDNT-DQAVEAANA----FSNLTDTLKNAKAQIDN----AYEALSAEPAFAESVQNARDKpfpdETKE 2530
Cdd:NF041483 237 HAEQLRSSTAAESDQArRQAAELSRAaeqrMQEAEEALREARAEAEKvvaeAKEAAAKQLASAESANEQRTR----TAKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALsktVSQDLKETEKLKKQLEQL------------TELSEKLR-KRKEAVKAGIPKYSKNTLD-----SIDEK---- 2588
Cdd:NF041483 313 EIARL---VGEATKEAEALKAEAEQAladaraeaeklvAEAAEKARtVAAEDTAAQLAKAARTAEEvltkaSEDAKattr 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2589 --VQEVEKLKAEIDANIEETRAKISEIA----GKAEEITE----KANSAMEGIRLARRNSVQLNKLApviVSKFEELKkl 2658
Cdd:NF041483 390 aaAEEAERIRREAEAEADRLRGEAADQAeqlkGAAKDDTKeyraKTVELQEEARRLRGEAEQLRAEA---VAEGERIR-- 464
|
410 420 430
....*....|....*....|....*....|....*.
gi 71991177 2659 SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGA 2694
Cdd:NF041483 465 GEARREAVQQIEEAARTAEELLTKAKADADELRSTA 500
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
472-509 |
8.86e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 8.86e-08
10 20 30
....*....|....*....|....*....|....*...
gi 71991177 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGY 509
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1880-1934 |
9.13e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 9.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 1880 CACPFAPTNNfaKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHPQISGESC 1934
Cdd:pfam00053 1 CDCNPHGSLS--DTCD-PETGQ---CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
427-467 |
9.44e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 427 CDCDPDKH-TGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
809-847 |
9.72e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.72e-08
10 20 30
....*....|....*....|....*....|....*....
gi 71991177 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1461-1504 |
1.07e-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: 1.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDPLI-GCQ 1504
Cdd:cd00055 2 CDCNghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1461-1499 |
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 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDP 1499
Cdd:smart00180 1 CDCDpggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-467 |
1.68e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 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. |
1461-1503 |
2.25e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 2.25e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGY--DPLIGC 1503
Cdd:pfam00053 1 CDCNphgsLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1554-1602 |
2.56e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDlsaENPLGC 1602
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1880-1927 |
2.56e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 1880 CACPfaPTNNFAKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHP 1927
Cdd:smart00180 1 CDCD--PGGSASGTCD-PDTGQ---CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2530-2698 |
8.60e-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: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2530 EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAK 2609
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2610 ISEIAGKAEEITEKANSAMEGIRLARRN-----SVQLNKLAPVIVSKFEELKKLsSARSAKVDSVSDKVSQIKEMI--AV 2682
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigelEAEIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEELerEI 345
|
170
....*....|....*.
gi 71991177 2683 ARDAANRIKLGAHFEK 2698
Cdd:TIGR02169 346 EEERKRRDKLTEEYAE 361
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1879-1934 |
1.12e-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: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 1879 ACACPFAPTNNFakSCDVseegQLLQCNCKPGYTGDRCDRCASGFFGHPqISGESC 1934
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 |
1.37e-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: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 71991177 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEDGC 753
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPET-GQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1830-1872 |
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 71991177 1830 CECN--GHSA-TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1872
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1990-2037 |
1.69e-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: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1990 CECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGFSKCQGcQGC 2037
Cdd:pfam00053 1 CDCNPHGSLsdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP-QGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1937-1980 |
3.22e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 3.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1937 CQCNGNNNLTDSrsCHPNSGDCyLCEQNTDGRHCESCAAWFYGD 1980
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
297-345 |
3.32e-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: 3.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 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 |
4.10e-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: 4.10e-06
10 20 30
....*....|....*....|....*....|....*....
gi 71991177 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 |
4.20e-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: 46.19 E-value: 4.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 71991177 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEdGCR 754
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGT-GQ-CECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2200-2573 |
9.31e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2200 DAQDILTNSTQIQNKLVRTKTHSQNSVSSAknITLNGTEFLQEVMKRAQRARQSVRSLAE--IALAIGSSSkavnvdpRL 2277
Cdd:NF041483 903 DANRIRSDAAAQADRLIGEATSEAERLTAE--ARAEAERLRDEARAEAERVRADAAAQAEqlIAEATGEAE-------RL 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLmtleaASADQYPEKAQTVPGKL--------EEIQKKIQEETEK-LDKQKEtfEAQKKRAE--ELAAYLNS-- 2344
Cdd:NF041483 974 RAEAAETV-----GSAQQHAERIRTEAERVkaeaaaeaERLRTEAREEADRtLDEARK--DANKRRSEaaEQADTLITea 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2345 ---AQQLLKESKSKADKSNNIAKMLQLTKV-------ENLVA-AITDDLERVEAAKGEFQKLNV-------AIGNITENL 2406
Cdd:NF041483 1047 aaeADQLTAKAQEEALRTTTEAEAQADTMVgaarkeaERIVAeATVEGNSLVEKARTDADELLVgarrdatAIRERAEEL 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2407 kdkREEMTHAVTTLNE-TRNDVAEALEAAKKRVRRDEKSVDMQLVNA--KAHEL----HLQATTLRQTfdnnkdntdqAV 2479
Cdd:NF041483 1127 ---RDRITGEIEELHErARRESAEQMKSAGERCDALVKAAEEQLAEAeaKAKELvsdaNSEASKVRIA----------AV 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2480 EAANAFsnltdtLKNA---KAQIDNAYEALSAEpAFAESVQNArdkpfpDETKEKIDALSKTvSQDLK-ETEKLKKQLEQ 2555
Cdd:NF041483 1194 KKAEGL------LKEAeqkKAELVREAEKIKAE-AEAEAKRTV------EEGKRELDVLVRR-REDINaEISRVQDVLEA 1259
|
410
....*....|....*....
gi 71991177 2556 LTEL-SEKLRKRKEAVKAG 2573
Cdd:NF041483 1260 LESFeAPSGGGKGNGVKAG 1278
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1937-1983 |
2.54e-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: 43.88 E-value: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1937 CQCNGNNnlTDSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVT 1983
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2499-2624 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2499 IDNAYEALSAepaFAESVQNARDKPFPDET-----------KEKIDALSKTVSQDLKE-TEKLKKQLEQ----LTELSEK 2562
Cdd:cd13769 7 IQKAQEAINN---LAQQVQKQLGLQNPEEVvntlkeqsdnfANNLQEVSSSLKEEAKKkQGEVEEAWNEfktkLSETVPE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2563 LRKRKEAVKAgipkySKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2624
Cdd:cd13769 84 LRKSLPVEEK-----AQELQAKLQSGLQtlvtESQKLAKAISENSQKAQEELQKATKQAYDIAVEA 144
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
701-749 |
1.77e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 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 ... |
2271-2378 |
3.45e-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: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2271 VNVDpRLLKEAEETlmtlEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKKRAEELAAYLNSAQQL 2348
Cdd:smart00935 4 VDVQ-KILQESPAG----KAAQK-QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseAAREKKEKELQKKVQEFQRK 77
|
90 100 110
....*....|....*....|....*....|..
gi 71991177 2349 LKESKSKADKSNN--IAKMLQltKVENLVAAI 2378
Cdd:smart00935 78 QQKLQQDLQKRQQeeLQKILD--KINKAIKEV 107
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2493-2698 |
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 71991177 2493 KNAKAQIDNAYEALSAEpafAESVQNARDKPFPDETKEKI----DALSKTVSQDLKETEKLKKQL----EQLTELSEKLR 2564
Cdd:cd22656 83 QNAGGTIDSYYAEILEL---IDDLADATDDEELEEAKKTIkallDDLLKEAKKYQDKAAKVVDKLtdfeNQTEKDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2565 KRKEAVKAGIPKYSK-NTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQL-N 2642
Cdd:cd22656 160 TLEKALKDLLTDEGGaIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLlA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2643 KLAPVIVSkFEELKKLSSARSAKVDSVSDKVSQIkemiavARDAANRIKLGAHFEK 2698
Cdd:cd22656 240 LIGPAIPA-LEKLQGAWQAIATDLDSLKDLLEDD------ISKIPAAILAKLELEK 288
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
298-344 |
1.67e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 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 |
2.36e-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: 2.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 24 FTYSQVLTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGstqytplnsysyqddeqqkswsqyenpMVRGGHGCGH 103
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGE----PGPERYCKLVG---------------------------HTEQGKKCDY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 104 CNAGNE-NSHPAANMVDGNN----SWWMSPPLSRGLQhnEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERStDHGKT 178
Cdd:smart00136 50 CDARNPrRSHPAENLTDGNNpnnpTWWQSEPLSNGPQ--NVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 179 YQPWFNFAenaAECMRRFGMESLSPISE--DDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNV 256
Cdd:smart00136 126 WQPWQYFS---SDCRRTFGRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71991177 257 RLRLLGTRTLQGHLMDMNewrdPTVTRRYFYAIKEIMIGG 296
Cdd:smart00136 203 RVRLTRLRTLGDELMDDR----PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
30-296 |
8.37e-75 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 249.42 E-value: 8.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 30 LTPSQITISHRKPITATSTCGEiqgqPVTEIYCSLTGSTqytplnsysyqddeqqkswsqyenpmvrGGHGCGHCNAGNE 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGL----NGPERYCILSGLE----------------------------GGKKCFICDSRDP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 110 -NSHPAANMVDGNN----SWWMSPPLSrgLQHNEVNITIDLEQEFHVAYVWIQMAnSPRPGSWVLERSTDHGKTYQPWFN 184
Cdd:pfam00055 49 hNSHPPSNLTDSNNgtneTWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 185 FAenaAECMRRFGM-ESLSPISEDDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNVRLRLLGT 263
Cdd:pfam00055 126 FA---SDCRRTFGRpSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRL 202
|
250 260 270
....*....|....*....|....*....|...
gi 71991177 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 ... |
2578-2719 |
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 71991177 2578 SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKK 2657
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2658 LSSARSakvdSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAAHADI 2719
Cdd:pfam06009 81 LEVNSS----SLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1658-1782 |
2.03e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 146.64 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1658 SVYFNVPIEKK-DYTTSYGLKLTFKLSTVP-RGGRKSMNADadVRLTGANMTIEYWAsEQPTNPEEQFTVKCKLVPENFL 1735
Cdd:smart00281 4 PVYWVAPEQFLgDKVTSYGGKLRYTLSFDGrRGGTHVSAPD--VILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71991177 1736 TAEGKTVTREELMKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEP 1782
Cdd:smart00281 81 YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3342-3499 |
7.06e-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: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3342 GFNFGSQQYSRIEydiLPEAIDKSGEFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSI 3420
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSFRTTSPNGLLLyAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991177 3421 IDGRWHTIKVSRRGKSAHLIVDDNSYEsEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLN 3499
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVV-ESGSPGGSALLNLDGPLYLGGLPEDL----KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2898-3046 |
3.05e-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: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2898 VVSLDGEGYTSYKPSHwNPRKATKISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGqWITESSNYN 2975
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGsqNGGDFLALELEDGRLVLRYDLGSGSL-VLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991177 2976 DGKWHTVSIVREEKHVKIMIDGETeVLEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3046
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGER-VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVspGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
3367-3501 |
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 71991177 3367 EFTFKIRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSII-DGRWHTIKVSRRGKSAHLIVDDn 3444
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLnDGQWHRVAVERNGRSVTLSVDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 3445 SYESEGAANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3501
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDL----KLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2921-3046 |
3.33e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2921 KISLSFLTFSPHGLLFFVG--KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGE 2998
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGskGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71991177 2999 TEVlEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKL 3046
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 ... |
3372-3501 |
5.08e-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: 5.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3372 IRPTSDNGIIFIATNKRTDHIAVMLEHGRVVFTYDTGSG-QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDnSYESEG 3450
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG-QTVVSS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 3451 AANQNEDLIETQPPFYVGGVPADLagfaRNLVVGVRSQFSGCIKDFKLNGK 3501
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLL----LLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2693-2864 |
1.57e-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: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2693 GAHFEKGSSLDLNIPQRVTRsaaHADISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAP 2772
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPNGLLLYAGSQ---------NGGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2773 AVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAETKSSVAggnksvLNLNqqiSRLFVGGVPTSARISKDLYNR 2852
Cdd:cd00110 69 LVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAL------LNLD---GPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 71991177 2853 DFVGDIESLKLH 2864
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2926-3048 |
3.88e-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: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2926 FLTFSPHGLLFFVG-KDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGETeVLEG 3004
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT-VVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71991177 3005 DVPGKDSEMSVTEFLYIGGTPSGLSVRTTIV--PLRGCIKSVKLGS 3048
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVraGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3521-3671 |
8.03e-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: 8.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3521 GMYFGKDGGYAIVQKDyEVGLTFGLEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGgeELWHHPDieN 3597
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQnggDFLALELEDGRLVLRYDLGSG--SLVLSSK--T 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 3598 QYCDGQWQSFKISKKRNLLTVAVNGKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3671
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLnLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2718-2866 |
1.10e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2718 DISFYFRTEQEHGIPLFFGNEetavgsravPTADYVAAEIEYGRPKITVDLGDAPAVVKLD-TPVNDGLWRRLNIERIGK 2796
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSK---------GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2797 TVSVTLSKPNSVETaetkssVAGGNKSVLNLNqqiSRLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2866
Cdd:smart00282 72 SVTLSVDGGNRVSG------ESPGGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3545-3671 |
4.11e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3545 LEVEMRPRMKNGILFSVGVL---EYITVEFVNGSIKTTVESGSGGEELWHHPdieNQYCDGQWQSFKISKKRNLLTVAVN 3621
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgggDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 3622 GKAHLKILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSF 3671
Cdd:smart00282 79 GGNRVSGESPGGLTILnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1669-1795 |
7.96e-25 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 102.73 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1669 DYTTSYGLKLTFKLSTVPRGGRKSMNADADVRLTGANMTIEYWASEQPT-NPEEQFTVKCKLVPENFLTAEGKTVTREEL 1747
Cdd:pfam00052 11 NKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPpDPGQEQTYSVRLHEENWRDSDGAPVSREDF 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71991177 1748 MKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEPNGVDSVikASSVE 1795
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 ... |
3549-3672 |
3.42e-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: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3549 MRPRMKNGILFSVGVL--EYITVEFVNGSIKTTVESGSGGEELWHHpdiENQYCDGQWQSFKISKKRNLLTVAVNGKAHL 3626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgsDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71991177 3627 KILKKAKTDVL-TKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSFG 3672
Cdd:pfam02210 78 SSLPPGESLLLnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2926-3052 |
1.49e-23 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.93 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2926 FLTFSPHGLLFFVGK--DKDFMALELSDGGVKLSVDLGSGVGQwITESSNYNDGKWHTVSIVREEKHVKIMIDGETEVLE 3003
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGRLEVSYDLGSGAAV-VRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 3004 GDVPGKDSEMSVTEFLYIGGTPSGLSVR--TTIVP-LRGCIKSVKLGSDNVD 3052
Cdd:pfam00054 80 ESPLGATTDLDVDGPLYVGGLPSLGVKKrrLAISPsFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3372-3504 |
1.86e-23 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.54 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3372 IRPTSDNGIIF-IATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDN---SYE 3447
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEarpTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 3448 SEGAANQNEDLIEtqpPFYVGGVPADLAGfARNLVVGVRsqFSGCIKDFKLNGKSLD 3504
Cdd:pfam00054 81 SPLGATTDLDVDG---PLYVGGLPSLGVK-KRRLAISPS--FDGCIRDVIVNGKPLD 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2278-2906 |
6.79e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK------- 2350
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkke 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2351 ESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAvttlNETR 2424
Cdd:PTZ00121 1375 EAKKKADaakkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKA----DEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2425 NDVAEALEA--AKKRVRRDEKSVDMQlvnAKAHELHlQATTLRQTFDNNKDNTDQAVEAANAfSNLTDTLKNAKaQIDNA 2502
Cdd:PTZ00121 1451 KKAEEAKKAeeAKKKAEEAKKADEAK---KKAEEAK-KADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAE-EAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2503 YEALSAEPAF-AESVQNARDKPFPDETKeKIDALSKtvSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNT 2581
Cdd:PTZ00121 1525 DEAKKAEEAKkADEAKKAEEKKKADELK-KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2582 LDSIDEKVQEV-----EKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELK 2656
Cdd:PTZ00121 1602 EEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2657 KLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAahadisfyfRTEQEHGIPLFFG 2736
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---------EEDKKKAEEAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2737 NEETAVGSRAVPTADYVAAEIEYGRPKIT---VDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAET 2813
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2814 KsSVAGGNKSVLNLNQQISRLFVGGVPTS-------ARISKDLYNR-DFVGDIESLKLHgEPIGLwNSREKGNTNVNGAQ 2885
Cdd:PTZ00121 1833 K-EVADSKNMQLEEADAFEKHKFNKNNENgedgnkeADFNKEKDLKeDDEEEIEEADEI-EKIDK-DDIEREIPNNNMAG 1909
|
650 660
....*....|....*....|.
gi 71991177 2886 KKPKITDNadelvvSLDGEGY 2906
Cdd:PTZ00121 1910 KNNDIIDD------KLDKDEY 1924
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2241-2698 |
2.13e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2241 QEVMKRAQRARQSvrslAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPgKLEEIQKKIQEETEK 2320
Cdd:PTZ00121 1332 DAAKKKAEEAKKA----AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2321 LDKQKETfEAQKKRAEEL---AAYLNSAQQLLK--ESKSKADKSNNIAKmlQLTKVENLVAAITddlervEAAKGEFQKL 2395
Cdd:PTZ00121 1407 ADELKKA-AAAKKKADEAkkkAEEKKKADEAKKkaEEAKKADEAKKKAE--EAKKAEEAKKKAE------EAKKADEAKK 1477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2396 NVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHlQATTLRQTFDNNKDNT 2475
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2476 DQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQnardKPFPDETKEKIDALSK-----TVSQDLKETEKLK 2550
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM----KLYEEEKKMKAEEAKKaeeakIKAEELKKAEEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2551 KQLEQLTELSEKLRKRKEAVKagipkyskntldsideKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEG 2630
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELK----------------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 2631 IRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEK 2698
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2723-2866 |
3.52e-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: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2723 FRTEQEHGIPLFFGNEETavgsravptaDYVAAEIEYGRPKITVDLGDAPAVVK-LDTPVNDGLWRRLNIERIGKTVSVt 2801
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS----------DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTL- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2802 lskpnSVETAETKSSVAGGNKSVLNLNQQisrLFVGGVPTSARISKDLYNRDFVGDIESLKLHGE 2866
Cdd:pfam02210 70 -----SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2157-2684 |
1.27e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2157 IANISSATIVgARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSsakniTLNG 2236
Cdd:PRK02224 196 IEEKEEKDLH-ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE-----TIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2237 TEFLQEVMKRAQRARQSVRSlaeialaigssskavnvdpRLLKEAEETLMTLEAASADqypekAQTVPGKLEEIQKKIQE 2316
Cdd:PRK02224 270 TEREREELAEEVRDLRERLE-------------------ELEEERDDLLAEAGLDDAD-----AEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2317 ETEKLDKQKETFEAQKKRAEELAAylnSAQQLLKESKSKADKSNNIAKMLQLTK--VENLVAAITDDLERVEAAKGEFQK 2394
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE---DADDLEERAEELREEAAELESELEEAReaVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2395 LNVAIGN-------ITENLKDKREEMTHAVTTLNETRNDVAEA---LEAAK-------------------KRVRRDE--- 2442
Cdd:PRK02224 403 APVDLGNaedfleeLREERDELREREAELEATLRTARERVEEAealLEAGKcpecgqpvegsphvetieeDRERVEElea 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2443 ---------KSVDMQLVNAK-AHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNayEALSAEPAF 2512
Cdd:PRK02224 483 eledleeevEEVEERLERAEdLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA--EAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2513 AESVQNArdkpfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTELS---EKLRKRKEAvKAGIPKYSKNTLDSID 2586
Cdd:PRK02224 561 AEAEEEA------EEAREEVAELNSklaELKERIESLERIRTLLAAIADAEdeiERLREKREA-LAELNDERRERLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2587 EKVQEvekLKAEID-ANIEETRAK-------ISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLApvivskfEELKKL 2658
Cdd:PRK02224 634 ERKRE---LEAEFDeARIEEAREDkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELR-------ERREAL 703
|
570 580
....*....|....*....|....*.
gi 71991177 2659 sSARSAKVDSVSDKVSQIKEMIAVAR 2684
Cdd:PRK02224 704 -ENRVEALEALYDEAEELESMYGDLR 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2306-2620 |
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 71991177 2306 KLEEIQKKIQEETEKLDKQKetfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQ--LTKVENLVAAITDDLE 2383
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEAAKGEFQKLNVAIGNITENLKDKREEMthavTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHElhlQATT 2463
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQLKEELKALREAL--DELRAELTLLNEEAAN---LRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2464 LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFP--DETKEKIDALSKTVSQ 2541
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2542 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKA 2617
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 71991177 2618 EEI 2620
Cdd:TIGR02168 982 KEL 984
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2404-2704 |
4.96e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2404 ENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvrRDEKsvdmqlvNAKAHELHLQATTLRQTFD--NNKdntdqavea 2481
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK--RDEL-------NAQVKELREEAQELREKRDelNEK--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2482 anaFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNARDKPFPDETKEKIDALSKTVsqdlkETEKL-----KKQLEQL 2556
Cdd:COG1340 73 ---VKELKEERDELNEKLNELREEL--DELRKELAELNKAGGSIDKLRKEIERLEWRQ-----QTEVLspeeeKELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2557 TELSEKLRKRKEAVKAGipKYSKNTLDSIDEKVQEVEKLKAEIDA---NIEETRAKISEIAGKAEEITEKANSAMEGIRL 2633
Cdd:COG1340 143 KELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2634 ARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQiKEMIAVARDAANRiklgahFEKGSSLDL 2704
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 ... |
2306-2691 |
7.25e-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: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQLLKE-----------SKSKADKSNNIAKM-LQLTKVE 2372
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkYNDLKKQkeelenelnllEKEKLNIQKNIDKIkNKLLKLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2373 ----NLVAAITD---------DLER--------VEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDvaeaL 2431
Cdd:TIGR04523 201 lllsNLKKKIQKnkslesqisELKKqnnqlkdnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----L 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2432 EAAKKRVrrDEKSVDMQLVNAKAHELhlqattlrqtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSaepa 2511
Cdd:TIGR04523 277 EQNNKKI--KELEKQLNQLKSEISDL------------NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2512 faesvqnardkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIP--KYSKNTLDS----- 2584
Cdd:TIGR04523 339 ---------------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlESQINDLESkiqnq 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2585 ------IDEKVQEVEKLKAEIDANIEETRAKI----SEIAGKAEEITEKANSAMEgirLARRNSVQLNKLapvivSKFE- 2653
Cdd:TIGR04523 404 eklnqqKDEQIKKLQQEKELLEKEIERLKETIiknnSEIKDLTNQDSVKELIIKN---LDNTRESLETQL-----KVLSr 475
|
410 420 430
....*....|....*....|....*....|....*...
gi 71991177 2654 ELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2174-2698 |
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 71991177 2174 KKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVM--------K 2245
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseisdlnnQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2246 RAQRARQSVRS--------LAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEA--ASADQYPEKAQTvpgKLEEIQKKIQ 2315
Cdd:TIGR04523 304 KEQDWNKELKSelknqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESenSEKQRELEEKQN---EIEKLKKENQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2316 ---EETEKLDKQKETFEAQKKRAEELAaylnsaQQLLKESKSKADKSNNIAKMLQLTKVENLVAAIT-DDLERVEAAKGe 2391
Cdd:TIGR04523 381 sykQEIKNLESQINDLESKIQNQEKLN------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKE- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2392 fqklnvaigNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMqlvnakaheLHLQATTLRQTFDNN 2471
Cdd:TIGR04523 454 ---------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK---------LNEEKKELEEKVKDL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2472 KDNTDQaveaanaFSNLTDTLKNAKAQIDNayealsaepafaesvqnardkpfpdETKEKIDALSKtvsqdlKETEKLKK 2551
Cdd:TIGR04523 516 TKKISS-------LKEKIEKLESEKKEKES-------------------------KISDLEDELNK------DDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2552 QLE-QLTELSEKLRKRKEAVKAgipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEItEKANSAMEG 2630
Cdd:TIGR04523 558 NLEkEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA-KKENEKLSS 631
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 2631 IRLARRNSvqLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANriKLGAHFEK 2698
Cdd:TIGR04523 632 IIKNIKSK--KNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK--ELSLHYKK 695
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2171-2641 |
2.99e-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: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2171 ARNKKEFNDINEITKMLNDEENSFGNV-FGDAQDILTNSTQIQNKLvrtkthsqnsvssaKNITLNGTEFLQEvmkraqr 2249
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGEVeTGIIKDIFGKLTQELNQN--------------LKKLEIFGLTLGL------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2250 aRQSVRSLAEIALAIGSSSKAVNVDPRL-----LKEAEETLMTLEAA-----SADQYPEKAQTVPGKLEEIQKKIQE-ET 2318
Cdd:COG5185 189 -LKGISELKKAEPSGTVNSIKESETGNLgsestLLEKAKEIINIEEAlkgfqDPESELEDLAQTSDKLEKLVEQNTDlRL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2319 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlqltkvenlvaaiTDDLERVEAAKGEFQKLNVA 2398
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA-----------------TESLEEQLAAAEAEQELEES 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2399 IGNITENLKDKREEmthavttLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNnkDNTDQA 2478
Cdd:COG5185 331 KRETETGIQNLTAE-------IEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE--IPQNQR 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2479 VEAANAFSNLTDTLKNAKAQIDN----------AYEALSAEPAFAESVQNARDKPFPDETKEKID-ALSKTVSQDLKETE 2547
Cdd:COG5185 402 GYAQEILATLEDTLKAADRQIEElqrqieqatsSNEEVSKLLNELISELNKVMREADEESQSRLEeAYDEINRSVRSKKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2548 KLKKQLEQlteLSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANiEETRAKISEIAGKAEEITEKANSA 2627
Cdd:COG5185 482 DLNEELTQ---IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRAR-GYAHILALENLIPASELIQASNAK 557
|
490
....*....|....
gi 71991177 2628 MEGIRLARRNSVQL 2641
Cdd:COG5185 558 TDGQAANLRTAVID 571
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1415-1463 |
5.13e-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: 68.53 E-value: 5.13e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1415 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPECIKCQC 1463
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1414-1457 |
5.97e-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: 5.97e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1414 SCDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPE 1457
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 |
9.22e-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: 67.76 E-value: 9.22e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYPNCKACAC 612
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2238-2681 |
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 71991177 2238 EFLQEVMKRAQRARQSVRS--------LAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEE 2309
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAelqeleekLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2310 IQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQlTKVENLVAAITDDLERVEAAK 2389
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2390 GEFQK-------LNVAIGNITENLKDKREEMTHA--------VTTLNETRNDVAEALEA-----AKKRVRRDEKSVDMQL 2449
Cdd:TIGR02168 400 NEIERlearlerLEDRRERLQQEIEELLKKLEEAelkelqaeLEELEEELEELQEELERleealEELREELEEAEQALDA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2450 VNAKAHELHLQATTLRQTFDNNKDNTD---QAVEAANAFSNLTDTLKNaKAQIDNAYEAlSAEPAFAESVQNA--RDKpf 2524
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILGVLSE-LISVDEGYEA-AIEAALGGRLQAVvvENL-- 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2525 pDETKEKIDALSKT--------VSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGiPKYSK--NTL-------DSIDE 2587
Cdd:TIGR02168 556 -NAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD-PKLRKalSYLlggvlvvDDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2588 KVQEVEKLKA------------------------------EIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRN 2637
Cdd:TIGR02168 634 ALELAKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 71991177 2638 SVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIA 2681
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1506-1556 |
1.11e-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: 1.11e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 1506 CGCHPQGSEGGNlvCDPESGQCLCRESMGGRQCDRCLAGFYGFPHCYGCSC 1556
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2298-2585 |
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 71991177 2298 EKAQTVPGKLEEIQKKIQE---ETEKLDKQKETFEAQ-KKRAEELAAYLNSAQQL---LKESKSKADKSNNIAKMLQLTK 2370
Cdd:COG1340 1 SKTDELSSSLEELEEKIEElreEIEELKEKRDELNEElKELAEKRDELNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2371 vENLVAAITDDLERVEAAKGEFQKLNVAIGNItENLKDK--REEMTH--AVTTLNETR------NDVAEALEAAKKRVRR 2440
Cdd:COG1340 81 -DELNEKLNELREELDELRKELAELNKAGGSI-DKLRKEieRLEWRQqtEVLSPEEEKelvekiKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2441 DEKSVDMQlvnAKAHELHLQATTLRQtfdnnkdntdQAVEAANAFSNLTDTLKNAKAQIDNAYEalSAEPAFAEsVQNAR 2520
Cdd:COG1340 159 NEKLKELR---AELKELRKEAEEIHK----------KIKELAEEAQELHEEMIELYKEADELRK--EADELHKE-IVEAQ 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2521 DKpfPDETKEKIDALSKTVSQDLKETEKLKKQLE--QLTELSEKLRKRKEAVKAGIPKYSKNTLDSI 2585
Cdd:COG1340 223 EK--ADELHEEIIELQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKKGEKLTTEEL 287
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1415-1458 |
1.32e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.32e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 1415 CDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYY--NFPEC 1458
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2306-2607 |
2.39e-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: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQE--------ETEKLDKQKETFEAQ-----------KKRAEELAAYLNSAQQLLKE-----SKSKADKSNN 2361
Cdd:TIGR02169 212 RYQALLKEKREyegyellkEKEALERQKEAIERQlasleeeleklTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2362 I-AKMLQLT-KVENLVAAITDDLERVEAAKGEFQKLNVAIgnitENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvr 2439
Cdd:TIGR02169 292 VkEKIGELEaEIASLERSIAEKERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2440 rdeksvdMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNA 2519
Cdd:TIGR02169 366 -------LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2520 rdkpFPDETKEKIDalsktvsqdlkETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSkntlDSIDEKVQEVEKLKAEI 2599
Cdd:TIGR02169 439 ----LEEEKEDKAL-----------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE----KELSKLQRELAEAEAQA 499
|
....*...
gi 71991177 2600 DANIEETR 2607
Cdd:TIGR02169 500 RASEERVR 507
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2278-2629 |
4.09e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKAD 2357
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2358 KSNNiakmlQLTKVENLVAAITDDLERVEAakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEaLEAAKKR 2437
Cdd:COG4372 98 QAQE-----ELESLQEEAEELQEELEELQK---ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-LQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2438 VRRDEKSVDMQLVNAKAHELHLQAttlRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKaqIDNAYEALSAEPAFAESVQ 2517
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEA---NRNAEKEEELAEAEKLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2518 NARDKPFPDETKEKIDALSKTVsQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKA 2597
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELEL-AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350
....*....|....*....|....*....|..
gi 71991177 2598 EIDANIEETRAKISEIAGKAEEITEKANSAME 2629
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2278-2655 |
5.93e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASaDQYPEKAQTVP---GKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELA---AYLNSAQQLLKE 2351
Cdd:PRK03918 288 LKEKAEEYIKLSEFY-EEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2352 SKSKADKSNNIAKMLQLTKVENLVAaitdDLERVEAAKGEFQKlnvAIGNITE---NLKDKREEMTHAVTTL-------- 2420
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEK----ELEELEKAKEEIEE---EISKITArigELKKEIKELKKAIEELkkakgkcp 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2421 ----------------------NETRNDVAEaLEAAKKRVRRDEKSVDMQLvnAKAHELhlqaTTLRQTFDN-------- 2470
Cdd:PRK03918 440 vcgrelteehrkelleeytaelKRIEKELKE-IEEKERKLRKELRELEKVL--KKESEL----IKLKELAEQlkeleekl 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2471 NKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALS------------------AEPAFAESVQNARDKPFP--DETKE 2530
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleelkkklaelekkldeLEEELAELLKELEELGFEsvEELEE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALS---------KTVSQDLKETEK--------LKKQLEQLTELS---EKLRKRKEAVKAgipKYSKNT--------- 2581
Cdd:PRK03918 593 RLKELEpfyneylelKDAEKELEREEKelkkleeeLDKAFEELAETEkrlEELRKELEELEK---KYSEEEyeelreeyl 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2582 -----LDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIT--EKANSAMEGIR---LARRNSVQLNKLAPV--IV 2649
Cdd:PRK03918 670 elsreLAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELRekvKKYKALLKERALSKVgeIA 749
|
....*..
gi 71991177 2650 SK-FEEL 2655
Cdd:PRK03918 750 SEiFEEL 756
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2182-2682 |
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 71991177 2182 EITKMLNDEENSfgnvfgdAQDILTNSTQIQNKLvrtkthsqnsvssaKNITlngteFLQEvmkraqRARQSVRSLAE-I 2260
Cdd:pfam05483 230 EYKKEINDKEKQ-------VSLLLIQITEKENKM--------------KDLT-----FLLE------ESRDKANQLEEkT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2261 ALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQypekaQTVPGKLEEIQKKIQEETEKLDKQKEtfEAQKKRAE---- 2336
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-----KALEEDLQIATKTICQLTEEKEAQME--ELNKAKAAhsfv 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2337 --ELAAYLNSAQQLLKESKSKADKSNNIAKML--QLTKVENLVAAITD-------DLERVEAAKGEFQKL---NVAIGNI 2402
Cdd:pfam05483 351 vtEFEATTCSLEELLRTEQQRLEKNEDQLKIItmELQKKSSELEEMTKfknnkevELEELKKILAEDEKLldeKKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2403 TENLKDKREEMTHAVTTLNETRNDV---AEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK---DNTD 2476
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2477 QAVEAANAFSNLTDTLKNAK---AQIDNAYEAlsaEPAFAESVQNARD--KPFPDETKEKIDALSKTVSQDLKETEKLKK 2551
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEErmlKQIENLEEK---EMNLRDELESVREefIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2552 QLEQLTELSEKLRKRKEavkagipkyskNTLDSIDEKVQEVEKLKAEIDA-----NIEETRA-----KISEIAGKAEEIT 2621
Cdd:pfam05483 588 QMKILENKCNNLKKQIE-----------NKNKNIEELHQENKALKKKGSAenkqlNAYEIKVnklelELASAKQKFEEII 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2622 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKvdsvsdkvsQIKEMIAV 2682
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH---------KIAEMVAL 708
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2723-2869 |
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 71991177 2723 FRTEQEHGIPLFFGNeetavgsraVPTADYVAAEIEYGRPKITVDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTL 2802
Cdd:pfam00054 1 FRTTEPSGLLLYNGT---------QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 2803 SKpNSVETAETKSsvagGNKSVLNLNQQisrLFVGGVPTSARISKDL-YNRDFVGDIESLKLHGEPIG 2869
Cdd:pfam00054 72 DG-EARPTGESPL----GATTDLDVDGP---LYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
756-806 |
2.87e-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: 2.87e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 756 CDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRLNSYNQMGC 806
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2282-2834 |
3.20e-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: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2282 EETLMTLEAASADqypekaqtvpgkLEEIQKKIQEetekLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNN 2361
Cdd:COG1196 175 EEAERKLEATEEN------------LERLEDILGE----LERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2362 iakmLQLTKVENLVAAITDDLERVEAakgEFQKLNVAIgnitENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRD 2441
Cdd:COG1196 239 ----AELEELEAELEELEAELEELEA---ELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2442 EKsvdmQLVNAKAHELHLQATTLRQTFDNNKDNTDQAvEAANAFSNLTDTLKNAKAQIDNAYEALSAEpafaesvQNARd 2521
Cdd:COG1196 308 EE----RRRELEERLEELEEELAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEA-------EAEL- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2522 kpfpDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKLKAEIDA 2601
Cdd:COG1196 375 ----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE--------ELEELEEALAELEEEEEEEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2602 NIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSdKVSQIKEMIA 2681
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2682 VARDAANRIKLGAHFEK--GSSLDLNIPQRVTRSAAHADISFYFRTEQEHGIPLFFgnEETAVGSRAVPTADYVAAEIEY 2759
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGA 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2760 GRPKITVDLGDAPAVVKLDtpVNDGLWRRLNIERI--GKTVSVTLSKPNSVETAETKSSVAGGNKSVLNLNQQISRL 2834
Cdd:COG1196 600 AVDLVASDLREADARYYVL--GDTLLGRTLVAARLeaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2305-2677 |
3.75e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2305 GKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKmlQLTKVENLVAAIT---DD 2381
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK--RLSRLEEEINGIEeriKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2382 LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRN-----------DVAEALEAAKKrvRRDEKSVDMQLV 2450
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeKLEKELEELEK--AKEEIEEEISKI 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2451 NAKAHELHLQATTLRQTFDN-----------NKDNTDQavEAANAFSNLTDTLKNA---KAQIDNAYEALSAEPAFAESV 2516
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEElkkakgkcpvcGRELTEE--HRKELLEEYTAELKRIekeLKEIEEKERKLRKELRELEKV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2517 QNARDKPFP-DETKEKIDAL-SKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYS--KNTLDSIDEKVQEV 2592
Cdd:PRK03918 489 LKKESELIKlKELAEQLKELeEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2593 EKLKAEID--------ANIEETRAKISEIagkaEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLssarSA 2664
Cdd:PRK03918 569 EEELAELLkeleelgfESVEELEERLKEL----EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET----EK 640
|
410
....*....|...
gi 71991177 2665 KVDSVSDKVSQIK 2677
Cdd:PRK03918 641 RLEELRKELEELE 653
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
564-605 |
4.06e-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: 4.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-658 |
4.28e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 4.28e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 610 CACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCRGCEC 658
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2144-2686 |
5.97e-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: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2144 DNLELEIDVLGTAIANI-SSATIVGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNS-------------- 2208
Cdd:TIGR02168 312 ANLERQLEELEAQLEELeSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskvaql 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2209 ----TQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEvMKRAQRARQSvRSLAEIALAIGSSSKAVNVDPRLLKEAEET 2284
Cdd:TIGR02168 392 elqiASLNNEIERLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQ-AELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2285 LMTLEAAsADQYPEKAQTVPGKLEEIQKkIQEETEKLDkqkETFEAQKKRAEELAAYLNSAQQLLK-ESKSKADKSNNIA 2363
Cdd:TIGR02168 470 LEEAEQA-LDAAERELAQLQARLDSLER-LQENLEGFS---EGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAALG 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2364 KMLQLTKVENLVAAIT--DDLERVEAAKGEFQKLNVAIGN-ITENLKDKREEMTHAVTTLNETR---------------- 2424
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllgg 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2425 ----NDVAEALEAAKKrVRRDEKSV--DMQLVNA------KAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTL 2492
Cdd:TIGR02168 625 vlvvDDLDNALELAKK-LRPGYRIVtlDGDLVRPggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2493 KNAKAQIDNAYEALSAEPAFAESVQNARDKPFPDETKEkIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKA 2572
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2573 GIpkyskntlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANS-----AMEGIRL------ARRNSVQL 2641
Cdd:TIGR02168 783 EI--------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerriAATERRLedleeqIEELSEDI 854
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 71991177 2642 NKLAPVIvskfEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA 2686
Cdd:TIGR02168 855 ESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSE 895
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
609-657 |
8.78e-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: 8.78e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 609 ACACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCR-GCE 657
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
755-807 |
1.24e-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: 1.24e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 71991177 755 SCDCNVNGTISGlnTCDLKTGQCMCKKNADGRRCDQCADGFYRlNSYNQMGCE 807
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
656-703 |
1.32e-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: 1.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 656 CECLLSGAKGQTCDSN-GQCYCKGNFEGERCDRCKPNFYNFPICEECNC 703
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2306-2636 |
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 71991177 2306 KLEEIQKKIQ---EETEKLDKQKETFEAQKKRAE-ELAAYLNSAQQLLKESKSKADKSNNIAKMLQltKVENLVAAITDD 2381
Cdd:PRK03918 166 NLGEVIKEIKrriERLEKFIKRTENIEELIKEKEkELEEVLREINEISSELPELREELEKLEKEVK--ELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2382 LERVEAAKGEFQKLNVAIGNITENLKDKREEMthavttlnetrndvaEALEAAKKRVRRDEKSvdmqlvnAKAHElhlqa 2461
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEI---------------EELEEKVKELKELKEK-------AEEYI----- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2462 tTLRQTFDNNKDNTdQAVEaaNAFSNLTDTLKNAKAQIDNAyealsaepafaesvqnardkpfpDETKEKIDALSKTVSQ 2541
Cdd:PRK03918 297 -KLSEFYEEYLDEL-REIE--KRLSRLEEEINGIEERIKEL-----------------------EEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2542 DLKETEKLKKQLEQLTELSEKLrKRKEAVKAgipKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIt 2621
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKK-EELERLKK---RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL- 424
|
330
....*....|....*
gi 71991177 2622 ekaNSAMEGIRLARR 2636
Cdd:PRK03918 425 ---KKAIEELKKAKG 436
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1506-1549 |
1.42e-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: 61.60 E-value: 1.42e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1506 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYGFP 1549
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2277-2674 |
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 71991177 2277 LLKEAEETLMTLE--AASADQYPE-KAQtvpgkLEEIQK-----KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQL 2348
Cdd:TIGR02168 194 ILNELERQLKSLErqAEKAERYKElKAE-----LRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2349 LKEskskadksnniaKMLQLTKVEnlvaaitddlERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNEtrndVA 2428
Cdd:TIGR02168 269 LEE------------LRLEVSELE----------EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----LE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2429 EALEAAKKrvRRDEKSVDMQLVNAKAHELhlqattlrqtfdnnkdnTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALsa 2508
Cdd:TIGR02168 323 AQLEELES--KLDELAEELAELEEKLEEL-----------------KEELESLEAELEELEAELEELESRLEELEEQL-- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2509 epafaESVQNARdkpfpDETKEKIDALSKTVSQdlketekLKKQLEQLTELSEKLRKRKEAVKagiPKYSKNTLDSIDEK 2588
Cdd:TIGR02168 382 -----ETLRSKV-----AQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELL---KKLEEAELKELQAE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2589 VQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGI-----RLARRNSVQLNKLapvivSKFEELKKL---SS 2660
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLE-----GFSEGVKALlknQS 516
|
410
....*....|....
gi 71991177 2661 ARSAKVDSVSDKVS 2674
Cdd:TIGR02168 517 GLSGILGVLSELIS 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2311-2691 |
2.09e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2311 QKKIQEETEKLDKQKETFEAQKK----RAEElaaylnsaQQLLKESKSKAD---KSNNIAKMLQLTKVENlvAAITDDLE 2383
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKtetgKAEE--------ARKAEEAKKKAEdarKAEEARKAEDARKAEE--ARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEAAKGEFQKLNVAIGNITENLKdKREEMTHA--VTTLNETRN-DVAEALEAAKK--------RVRRDEKSVDMQLVNa 2452
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEDAK-KAEAARKAeeVRKAEELRKaEDARKAEAARKaeeerkaeEARKAEDAKKAEAVK- 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2453 KAHELHLQATTLRQTFD--NNKDNTDQAVEAANAFSNLTDTLKNAKA----QIDNAYEALSAEPAF-AESVQNARDKPFP 2525
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEerNNEEIRKFEEARMAHFARRQAAIKAEEArkadELKKAEEKKKADEAKkAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2526 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTldSIDEKVQEVEKLKAEIDANIEE 2605
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2606 TRAKISEIAGKAEEITEKANSaMEGIRLARRNSVQLNKLAPViVSKFEELKKlsSARSAKvdsvsdKVSQIKEMIAVARD 2685
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE-KKKADEAKK--KAEEAK------KADEAKKKAEEAKK 1458
|
....*.
gi 71991177 2686 AANRIK 2691
Cdd:PTZ00121 1459 AEEAKK 1464
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
756-799 |
2.38e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 756 CDCNVNGTISglNTCDLKTGQCMCKKNADGRRCDQCADGFYRLN 799
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
519-564 |
2.52e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.52e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFC 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
564-605 |
2.54e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.54e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 564 CNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYP 605
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2298-2685 |
2.55e-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: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2298 EKAQTVPGKLEEIQKKIQEETEKldkqKETFEAQKKRAEELAAYLNSAQQ-LLKESKSKADKSNNI----AKMLQLTKVE 2372
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLEI----FGLTLGLLKGISELKKAEPSGTVnSIKESETGNLGSESTllekAKEIINIEEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2373 NLV-AAITDDLERVEAAKGEFQKLNVAIGNI-TENLKDKREEMTHavttLNETRNDVAEALEAAKKRVRRDEKSVDMQLV 2450
Cdd:COG5185 235 LKGfQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKR----LNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2451 NAKAHELhLQATTLRQTFDNNKDNTDQAVEaanafsNLTDTLKNAKAQIDNAYEALSAEpafAESVQNARDKPfpdETKE 2530
Cdd:COG5185 311 TESLEEQ-LAAAEAEQELEESKRETETGIQ------NLTAEIEQGQESLTENLEAIKEE---IENIVGEVELS---KSSE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALSKTVsqdlketEKLKKQLEQLtelseklrkrkeavkagipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKI 2610
Cdd:COG5185 378 ELDSFKDTI-------ESTKESLDEI---------------------PQNQRGYAQEILATLEDTLKAADRQIEELQRQI 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2611 SEIAGKAEEITEKANSAMEGIRLARRnSVQLNKLAPVIvskfEELKKLSSARSAKVDSVSDKVSQIKEMIAVARD 2685
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 ... |
2298-2668 |
2.95e-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: 69.82 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2298 EKAQTVPGKLEEIQKKIQ---EE----TEKLDKQKETF-EAQKKRA---------EELAAYLNS--------AQQLLKES 2352
Cdd:pfam01576 19 ERQQKAESELKELEKKHQqlcEEknalQEQLQAETELCaEAEEMRArlaarkqelEEILHELESrleeeeerSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2353 K----------SKADKSNNIAKMLQLTKV--ENLVAAITDDLERVEAAKGEFQK----LNVAIGNITENLKDKREEmtha 2416
Cdd:pfam01576 99 KkmqqhiqdleEQLDEEEAARQKLQLEKVttEAKIKKLEEDILLLEDQNSKLSKerklLEERISEFTSNLAEEEEK---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2417 VTTLNETRNDVAEALEAAKKRVRRDEKSvDMQLVNAK------AHELHLQATTLRQTFDN------NKDNTDQAV----- 2479
Cdd:pfam01576 175 AKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKrklegeSTDLQEQIAELQAQIAElraqlaKKEEELQAAlarle 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2480 EAANAFSNLTDTLKNAKAQIDNAYEALSAEPAfaesvqnARDKpfpdETKEKidalsktvsQDL-KETEKLKKQLEQL-- 2556
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERA-------ARNK----AEKQR---------RDLgEELEALKTELEDTld 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2557 -TELSEKLRKRKEavkagipkyskntldsidekvQEVEKLKAEIDaniEETRAKISEIAgkaeEITEKANSAM----EGI 2631
Cdd:pfam01576 314 tTAAQQELRSKRE---------------------QEVTELKKALE---EETRSHEAQLQ----EMRQKHTQALeeltEQL 365
|
410 420 430
....*....|....*....|....*....|....*...
gi 71991177 2632 RLARRNSVQLNKLAPVIVSKFEELKK-LSSARSAKVDS 2668
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAeLRTLQQAKQDS 403
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2240-2697 |
2.99e-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: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2240 LQEvMKRAQRARQSVRSLAEIALAIGSSSKAVNvDPRLLKEAEETL---MTLEAASADQYPEKAQTVPGKLEEIQKKIQE 2316
Cdd:pfam05701 107 VEE-MEQGIADEASVAAKAQLEVAKARHAAAVA-ELKSVKEELESLrkeYASLVSERDIAIKRAEEAVSASKEIEKTVEE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2317 ETEKLDKQKETFEAQKkraeelAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVE------NLVAAitDDLE-RVEAAK 2389
Cdd:pfam05701 185 LTIELIATKESLESAH------AAHLEAEEHRIGAALAREQDKLNWEKELKQAEEElqrlnqQLLSA--KDLKsKLETAS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2390 GEFQKLNVAIGNITENlkdKREEMTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHELHLQATTLRQTFD 2469
Cdd:pfam05701 257 ALLLDLKAELAAYMES---KLKEEADGEGNEKKTSTSIQAALASAKKEL--EEVKANIEKAKDEVNCLRVAAASLRSELE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2470 NNKDNTD----QAVEAANAFSNLTDTLKNAKAQIdnayealsaepafaESVQnARDKpfpdETKEKIDALSKTVSQDLKE 2545
Cdd:pfam05701 332 KEKAELAslrqREGMASIAVSSLEAELNRTKSEI--------------ALVQ-AKEK----EAREKMVELPKQLQQAAQE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2546 TEKLKKqLEQLTElsEKLRKRKEavKAGIPKYSKNTLDSIDEKVQ-EVEKLKAE-------IDANIE-ETRAKISEIAGK 2616
Cdd:pfam05701 393 AEEAKS-LAQAAR--EELRKAKE--EAEQAKAAASTVESRLEAVLkEIEAAKASeklalaaIKALQEsESSAESTNQEDS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2617 AEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKlSSARS-AKVDSVSDKVSQIKEMIAVARDAANRI---KL 2692
Cdd:pfam05701 468 PRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKE-SELRSlEKLEEVNREMEERKEALKIALEKAEKAkegKL 546
|
....*
gi 71991177 2693 GAHFE 2697
Cdd:pfam05701 547 AAEQE 551
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2149-2605 |
4.37e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2149 EIDVLGTAIANISsATIVGARLARN--KKEFNDINEITKMLNDEENSF--GNVFGDA--------QDILTNS-TQIQNKL 2215
Cdd:PRK02224 252 ELETLEAEIEDLR-ETIAETEREREelAEEVRDLRERLEELEEERDDLlaEAGLDDAdaeavearREELEDRdEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2216 VRTKTHSQNSVSSAKNITLNGTEfLQEvmkRAQRARQSVRSL-AEIALAigssskAVNVDPR--LLKEAEETLMTLEAAS 2292
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADD-LEE---RAEELREEAAELeSELEEA------REAVEDRreEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2293 ADqypekAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELaayLNSAQQLLKESK---------------SKAD 2357
Cdd:PRK02224 401 GD-----APVDLGNAEDFLEELREERDELREREAELEATLRTARER---VEEAEALLEAGKcpecgqpvegsphveTIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2358 KSNNIAKM-LQLTKVENLVAAITDDLERVEAAK---GEFQKLNVAIGNITENLKDKREemthavtTLNETRndvaeaLEA 2433
Cdd:PRK02224 473 DRERVEELeAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRE-------TIEEKR------ERA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2434 AKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQ---TFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSA-- 2508
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAla 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2509 --------------------EPAFAES-VQNARDK-----PFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTElsek 2562
Cdd:PRK02224 620 elnderrerlaekrerkrelEAEFDEArIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE---- 695
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 71991177 2563 LRKRKEAVKAgipkySKNTLDSIDEKVQEVE----KLKAEIDA-NIEE 2605
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 ... |
2145-2613 |
4.94e-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: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2145 NLELEIDVLGTAIANISSATIVGARLaRNKKEfNDINEITKMLNDEENSFgnvfgdaqdiltnSTQIQNklVRTKtHSQn 2224
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQEL-RSKRE-QEVTELKKALEEETRSH-------------EAQLQE--MRQK-HTQ- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2225 svssaknitlnGTEFLQEVMKRAQRARQSvrsLAEIALAIGSSSKAVNVDPRLL-----------KEAEETLMTLEAASA 2293
Cdd:pfam01576 357 -----------ALEELTEQLEQAKRNKAN---LEKAKQALESENAELQAELRTLqqakqdsehkrKKLEGQLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2294 DQYPEKAQtvpgkLEEIQKKIQEETEKLDKQKETFEAQ----KKRAEELAAYLNSAQQLLKESKSKadKSNNIAKMLQLt 2369
Cdd:pfam01576 423 ESERQRAE-----LAEKLSKLQSELESVSSLLNEAEGKniklSKDVSSLESQLQDTQELLQEETRQ--KLNLSTRLRQL- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2370 kvENLVAAITDDLERVEAAKGEFQK----LNVAIgnitENLKDKREEMTHAVttlnetrndvaEALEAAKKRVRRDEKSV 2445
Cdd:pfam01576 495 --EDERNSLQEQLEEEEEAKRNVERqlstLQAQL----SDMKKKLEEDAGTL-----------EALEEGKKRLQRELEAL 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2446 DMQLVN--AKAHELHLQATTLRQTFDN---NKDNTDQAVEA----ANAFSNLTDTLKNAKAQidNAYEALSAEpafAEsv 2516
Cdd:pfam01576 558 TQQLEEkaAAYDKLEKTKNRLQQELDDllvDLDHQRQLVSNlekkQKKFDQMLAEEKAISAR--YAEERDRAE---AE-- 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2517 qnARDKpfpdETKekidALSktvsqdlketekLKKQLEQLTELSEKLRKRKEAVKAGIPKY--SKntlDSIDEKVQEVEK 2594
Cdd:pfam01576 631 --AREK----ETR----ALS------------LARALEEALEAKEELERTNKQLRAEMEDLvsSK---DDVGKNVHELER 685
|
490
....*....|....*....
gi 71991177 2595 LKAEIDANIEETRAKISEI 2613
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEEL 704
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1506-1551 |
9.25e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.25e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 1506 CGCHPQGSEGGnlVCDPESGQCLCRESMGGRQCDRCLAGFYG--FPHC 1551
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2037-2081 |
9.61e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.61e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 2037 CHCGTA-AFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHGC 2081
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2483-2691 |
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 71991177 2483 NAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPfpDETKEKIDALSK---TVSQDLKETEKLKKQLEQLTEL 2559
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL--EEVLREINEISSelpELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2560 SEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKlkaeidaNIEETRAKISEIAGKAEEITEKANSAMEGIRlarrnsv 2639
Cdd:PRK03918 240 IEELEKELESLEG--------SKRKLEEKIRELEE-------RIEELKKEIEELEEKVKELKELKEKAEEYIK------- 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2640 qLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:PRK03918 298 -LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2198-2691 |
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 71991177 2198 FGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSvrsLAEIALAIGSSSKAVNVDPRL 2277
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYpEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKAD 2357
Cdd:TIGR02168 360 LEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2358 KSN--NIAKML-----QLTKVENLVAAITDDLERVE----AAKGEFQKLNVAIgNITENLKDKREEMTHAVTTLNETRND 2426
Cdd:TIGR02168 439 QAEleELEEELeelqeELERLEEALEELREELEEAEqaldAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2427 VAEALEAAKKRVRRDEK-----------SVDMQLVN-----AKAHELHLQATTLRQTF---DNNKDNTDQA--------- 2478
Cdd:TIGR02168 518 LSGILGVLSELISVDEGyeaaieaalggRLQAVVVEnlnaaKKAIAFLKQNELGRVTFlplDSIKGTEIQGndreilkni 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2479 ----------VEAANAFSNL----------TDTLKNAKAQIDNAYE----------------ALSAEPAFAESVQNARDK 2522
Cdd:TIGR02168 598 egflgvakdlVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPgyrivtldgdlvrpggVITGGSAKTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2523 PFpDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpKYSKNTLDSIDEKVQEVEKLKAEIDAN 2602
Cdd:TIGR02168 678 EI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2603 IEETRAKISEIAGKAEEITEKANSAMEGI-----RLARRNSvQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIK 2677
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIeeleaQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
570
....*....|....
gi 71991177 2678 EMIAVARDAANRIK 2691
Cdd:TIGR02168 835 ATERRLEDLEEQIE 848
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2278-2691 |
1.31e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 68.32 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAaSADQYPEKAQTVPGKLEEiqKKIQEETEKlDKQKETFEAQKKRAEELaayLNSAQQLLKESKSKAD 2357
Cdd:PTZ00440 1079 IKLLEEKVEALLK-KIDENKNKLIEIKNKSHE--HVVNADKEK-NKQTEHYNKKKKSLEKI---YKQMEKTLKELENMNL 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2358 ---KSNNIAKM-LQLTK--VENLVAAITDDLERveaAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETR-NDVAEA 2430
Cdd:PTZ00440 1152 ediTLNEVNEIeIEYERilIDHIVEQINNEAKK---SKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAyYDKATA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2431 LEAakkrvrrdeksvdmqlvnaKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNL------TDTLKNAKAQIDNAYE 2504
Cdd:PTZ00440 1229 SYE-------------------NIEELTTEAKGLKGEANRSTNVDELKEIKLQVFSYLqqvikeNNKMENALHEIKNMYE 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2505 ALsaepafaesvqnardkpfpdeTKEKIDALSKTVSQDLKETE----KLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKN 2580
Cdd:PTZ00440 1290 FL---------------------ISIDSEKILKEILNSTKKAEefsnDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGS 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2581 TLD-SIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARrnsvqlnklapvIVSKFEELKKlS 2659
Cdd:PTZ00440 1349 LEDkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKID------------FLNKHEAIEP-S 1415
|
410 420 430
....*....|....*....|....*....|..
gi 71991177 2660 SARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:PTZ00440 1416 NSKEVNIIKITDNINKCKQYSNEAMETENKAD 1447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2330-2575 |
1.72e-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: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2330 AQKKRAEELAAYLNSAQQLLKESKSKADKsnniakmlQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDK 2409
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2410 REEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVdmqLVNAK-AHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNL 2488
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL---LLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2489 TDTLKNAKAQIDNAYEALSAEPAFAESVQNARdkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKE 2568
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER--------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*..
gi 71991177 2569 AVKAGIP 2575
Cdd:COG4942 238 AAAERTP 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2084-2129 |
2.08e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGC 2129
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 ... |
2276-2678 |
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 71991177 2276 RLLKEaEETLMTLEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKEsksk 2355
Cdd:pfam01576 195 RLKKE-EKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE---- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2356 adksnniakmlqltkVENLVAAITDDL--ERVEAAKGEFQKlnvaignitenlKDKREEMTHAVTTLNETRNDVAEALEA 2433
Cdd:pfam01576 269 ---------------LEAQISELQEDLesERAARNKAEKQR------------RDLGEELEALKTELEDTLDTTAAQQEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2434 AKKR---VRRDEKSVDMQlvnAKAHELHLQATTLRQTfdnnkdntdQAVEaanAFSNLTDTLKNAKAQIDNAYEALSAEP 2510
Cdd:pfam01576 322 RSKReqeVTELKKALEEE---TRSHEAQLQEMRQKHT---------QALE---ELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2511 AfaesvqnardkpfpdETKEKIdalsKTVSQDLKETEKLKKQLE-QLTELSEKL----RKRKEAVKagipKYSK--NTLD 2583
Cdd:pfam01576 387 A---------------ELQAEL----RTLQQAKQDSEHKRKKLEgQLQELQARLseseRQRAELAE----KLSKlqSELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2584 SIDEKVQEVEK--LKAEIDANI-------------EETRAKISeIAGKAEEITEKANSAMEgiRL-----ARRNsvqLNK 2643
Cdd:pfam01576 444 SVSSLLNEAEGknIKLSKDVSSlesqlqdtqellqEETRQKLN-LSTRLRQLEDERNSLQE--QLeeeeeAKRN---VER 517
|
410 420 430
....*....|....*....|....*....|....*
gi 71991177 2644 LAPVIVSKFEELKKlssarsaKVDSVSDKVSQIKE 2678
Cdd:pfam01576 518 QLSTLQAQLSDMKK-------KLEEDAGTLEALEE 545
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2144-2592 |
2.18e-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: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2144 DNLELEIDVLGTAIANISsativgARLARNKKEFNDINEITKMLNDEEnsfgnvfgdaQDILTNSTQIQNKLVRtkthsq 2223
Cdd:TIGR02168 680 EELEEKIEELEEKIAELE------KALAELRKELEELEEELEQLRKEL----------EELSRQISALRKDLAR------ 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2224 nsvssaknitlngteFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTV 2303
Cdd:TIGR02168 738 ---------------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2304 PGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQllkeskSKADKSNNIAKM-LQLTKVENLVAAITDDL 2382
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE------QIEELSEDIESLaAEIEELEELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2383 ERVEAAKGEFQklnvaignitENLKDKREEMTHAVTTLNETRNDVAEALEaakkrvrrdeksvDMQLVNAKAHELHLQAT 2462
Cdd:TIGR02168 876 EALLNERASLE----------EALALLRSELEELSEELRELESKRSELRR-------------ELEELREKLAQLELRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2463 TLRQTFDNNKDntdqaveaanAFSNLtdtlknakaQIDNAYEALSAEPAFAESVQNARDKpfPDETKEKIDALSK---TV 2539
Cdd:TIGR02168 933 GLEVRIDNLQE----------RLSEE---------YSLTLEEAEALENKIEDDEEEARRR--LKRLENKIKELGPvnlAA 991
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2540 SQDLKETEK----LKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEV 2592
Cdd:TIGR02168 992 IEEYEELKErydfLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
519-566 |
2.79e-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: 2.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 519 CVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFCNC 566
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2306-2632 |
2.99e-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: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADksnniakmlqLTKVENLVAAITDDLERV 2385
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID----------VASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2386 EAAKGEFQKLnvaigniTENLKDKREEMTHAVTTLNETRNDVAEaLEAAKKRVRRDEKSVDMQLVNAKAhelhLQATTLR 2465
Cdd:COG4913 681 DASSDDLAAL-------EEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAED----LARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2466 QTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALsaEPAFAESVQNardkpFPDETKEKIDALSktvsqDLKE 2545
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL--ERAMRAFNRE-----WPAETADLDADLE-----SLPE 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2546 TEKLKKQLEQ--LTELSEKLRKRKEavkagipkysKNTldsidekVQEVEKLKAEIDANIEETRAKISEIagkaeeitek 2623
Cdd:COG4913 817 YLALLDRLEEdgLPEYEERFKELLN----------ENS-------IEFVADLLSKLRRAIREIKERIDPL---------- 869
|
....*....
gi 71991177 2624 aNSAMEGIR 2632
Cdd:COG4913 870 -NDSLKRIP 877
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2282-2622 |
3.07e-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: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2282 EETLMTLEAAsaDQYPEKAQTVPGKLEEIQKKIQEETEKL----DKQKETFEAQKKRAEELAAYLNSAQQLLKE------ 2351
Cdd:pfam12128 460 PELLLQLENF--DERIERAREEQEAANAEVERLQSELRQArkrrDQASEALRQASRRLEERQSALDELELQLFPqagtll 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2352 ---SKSKADKSNNIAKML---QLTKvenlvaaiTD-DLERVEAAKGefQKLNVaiGNITENLKDKREEMTHAVT-TLNET 2423
Cdd:pfam12128 538 hflRKEAPDWEQSIGKVIspeLLHR--------TDlDPEVWDGSVG--GELNL--YGVKLDLKRIDVPEWAASEeELRER 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2424 RNDVAEALEAAKKRVRRDEKSvdMQLVNAKAHELHLQATTLRQTFDNNKDNTDQaveaanafsnLTDTLKNAKAQIDnay 2503
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQ--LVQANGELEKASREETFARTALKNARLDLRR----------LFDEKQSEKDKKN--- 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2504 EALSAEPAFAESVQNARD----------KPFPDETKEKIDALSKTVSQDLKETEKLKKqlEQLTELSEKLRKRKEAVKA- 2572
Cdd:pfam12128 671 KALAERKDSANERLNSLEaqlkqldkkhQAWLEEQKEQKREARTEKQAYWQVVEGALD--AQLALLKAAIAARRSGAKAe 748
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2573 --GIPKYSKNTLDSIDEKVQEVEKLKAEidanIEETRAKISEIAGKAEEITE 2622
Cdd:pfam12128 749 lkALETWYKRDLASLGVDPDVIAKLKRE----IRTLERKIERIAVRRQEVLR 796
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3555-3672 |
3.78e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 60.41 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3555 NGILFSVGV---LEYITVEFVNGSIKTTVESGSGGEELWHHPDIenqyCDGQWQSFKISKKRNLLTVAVNGKAHLKI--L 3629
Cdd:pfam00054 7 SGLLLYNGTqteRDFLALELRDGRLEVSYDLGSGAAVVRSGDKL----NDGKWHSVELERNGRSGTLSVDGEARPTGesP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 71991177 3630 KKAKTDVLTKDPLYFGGLPEGVTNKGIKTN-KPFVGCIRFVSFG 3672
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2314-2691 |
4.09e-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: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2314 IQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQL--LKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKG 2390
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEkRQQLerLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2391 EFQKLNVAIGNITENLKDKREEMthavttlnetrNDVAEALEAAKKRVRrDEKSVDMQLVNAKAHELHLQATTLRQTFDN 2470
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRL-----------EEIEQLLEELNKKIK-DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2471 NKDNTDQAVEaanafsnltdTLKNAKAQIDNayealsaepafaesvqnardkpfpdeTKEKIDALSKtvsqdlkETEKLK 2550
Cdd:TIGR02169 313 KERELEDAEE----------RLAKLEAEIDK--------------------------LLAEIEELER-------EIEEER 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2551 KQLEQLTELSEKLRKRKEavkagipkyskntldsidEKVQEVEklkaEIDANIEETRAKISEIAGKAEEITEKANSAMEG 2630
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELE------------------DLRAELE----EVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 2631 IR----LARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSD---KVSQIKEMIAVARDAANRIK 2691
Cdd:TIGR02169 408 LDrlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewKLEQLAADLSKYEQELYDLK 475
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
471-520 |
4.83e-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: 4.83e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 471 PCECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTAGCVECV 520
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2242-2676 |
5.01e-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: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2242 EVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLE---AASADQYPEKAQTVPGKL----EEIQKKi 2314
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNGELsaadAAVAKD- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2315 QEETEKLDKQKETFeaQKKRAEELAAYLNSAQQ-------LLKESKSKADKSNNIAK---MLQLTKVENLVAAITDDLER 2384
Cdd:pfam12128 321 RSELEALEDQHGAF--LDADIETAAADQEQLPSwqselenLEERLKALTGKHQDVTAkynRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2385 VEAAKGEFQKLNVAIGNITENLKDK-REEMTHAVTTLNETRNDVAEALEAAKKRVRRdeksvdmqlVNAKAHELhlqaTT 2463
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ---------ATATPELL----LQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2464 LRQtFDNNKDNTDQAVEAANA-FSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARdkpfpDETKEKIDALSKTVSQD 2542
Cdd:pfam12128 466 LEN-FDERIERAREEQEAANAeVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-----DELELQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2543 L-KETEKLKKQLEQLteLSEKLRKR--------KEAVKAGIPKYSKN-TLDSID--EKVQEVEKLKAEIDA--------- 2601
Cdd:pfam12128 540 LrKEAPDWEQSIGKV--ISPELLHRtdldpevwDGSVGGELNLYGVKlDLKRIDvpEWAASEEELRERLDKaeealqsar 617
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2602 -NIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNklapviVSKFEELKKLSSARSAKVDSVSDKVSQI 2676
Cdd:pfam12128 618 eKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLF------DEKQSEKDKKNKALAERKDSANERLNSL 687
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-656 |
5.17e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 5.17e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 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 ... |
2168-2739 |
5.27e-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: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2168 ARLARNKKEFND-----INEITKMLNDEENSFGNVFGDAQDILTNSTQI---QNKLVRTKTHSQNSVSSAKNITLNGTEF 2239
Cdd:pfam02463 179 IEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2240 LQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETE 2319
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2320 KLDKQKEtfEAQKKRAEELAAYLNSAQQLLKESKSKAD----KSNNIAKMLQLTKVENLVAAITDDLER-VEAAKGEFQK 2394
Cdd:pfam02463 339 ELEKELK--ELEIKREAEEEEEEELEKLQEKLEQLEEEllakKKLESERLSSAAKLKEEELELKSEEEKeAQLLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2395 LNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQtfdnnKDN 2474
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-----LLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2475 TDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSaepafaESVQNARDKPFPDETKEKIDALSKTVSQDlketEKLKKQLE 2554
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRI------ISAHGRLGDLGVAVENYKVAISTAVIVEV----SATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2555 QltelseklRKRKEAVKAGIPKYsKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLA 2634
Cdd:pfam02463 562 E--------RQKLVRALTELPLG-ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2635 RRNSVQLNKLAPVIVS-KFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA---ANRIKLGAHFEKGSSLDLNIPQRV 2710
Cdd:pfam02463 633 ELTKLKESAKAKESGLrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAeseLAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590
....*....|....*....|....*....|
gi 71991177 2711 TRSAAHADISF-YFRTEQEHGIPLFFGNEE 2739
Cdd:pfam02463 713 KKLKLEAEELLaDRVQEAQDKINEELKLLK 742
|
|
| CBM6-CBM35-CBM36_like |
cd02795 |
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ... |
855-988 |
5.54e-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: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 855 QYEAEDAHTEDQKPVRFA---VDPEQFADFSWRGYAVFSPiqdkilidVDITKATVYRLLFRYRNPTSVPV-TATVTINP 930
Cdd:cd02795 1 RIEAEDATLTGGTAVSTAagaSGGGYVIGFSSGGDSVTFT--------VTVPKAGTYRLAVRYASPNGNGSrSVSLDGNG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 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 ... |
2141-2729 |
5.70e-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: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2141 GDVDNL--ELEIDVLGTAIANISSATivgaRLARNKKEFNdiNEITKMLNDEENSfgnVFGDAQDILTNSTQIQNKLVRT 2218
Cdd:TIGR01612 671 DDIDALynELSSIVKENAIDNTEDKA----KLDDLKSKID--KEYDKIQNMETAT---VELHLSNIENKKNELLDIIVEI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2219 KTHSQNSVSSAKNITLNG-----TEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLmtleaasa 2293
Cdd:TIGR01612 742 KKHIHGEINKDLNKILEDfknkeKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNY-------- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2294 DQYPEKAQTVPGKLEEIQKKIQE---------------------ETEKLDKQKETFE--AQKKRAEELAAYLNSAQQLLK 2350
Cdd:TIGR01612 814 DKSKEYIKTISIKEDEIFKIINEmkfmkddflnkvdkfinfennCKEKIDSEHEQFAelTNKIKAEISDDKLNDYEKKFN 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2351 ESKSKADKSNN-IAKMLQ----LTKVENLVAAITDDLERVEAAKGEFQKLNvaignitenlkdkrEEMTHAVTTLNET-- 2423
Cdd:TIGR01612 894 DSKSLINEINKsIEEEYQnintLKKVDEYIKICENTKESIEKFHNKQNILK--------------EILNKNIDTIKESnl 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2424 -----RNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNT--DQAVEAANAFSNLTDTLKNAK 2496
Cdd:TIGR01612 960 ieksyKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyHQFDEKEKATNDIEQKIEDAN 1039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2497 AQIDNAyealsaEPAFAESVQNARDKpFPDETKEKIDALSKTVsqdlkeTEKLKKQLEQLTELSEKLRKRK--EAVKAGI 2574
Cdd:TIGR01612 1040 KNIPNI------EIAIHTSIYNIIDE-IEKEIGKNIELLNKEI------LEEAEINITNFNEIKEKLKHYNfdDFGKEEN 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2575 PKYS----------KNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIagkaEEITEKA--NSAMEGIRLARRNSV--- 2639
Cdd:TIGR01612 1107 IKYAdeinkikddiKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDL----EDVADKAisNDDPEEIEKKIENIVtki 1182
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2640 --------QLNKLAPVIV------SKFEELK--KLSSARS------AKVDSVSDKVSQ-IKEMIAVARDAANRIKLGAHF 2696
Cdd:TIGR01612 1183 dkkkniydEIKKLLNEIAeiekdkTSLEEVKgiNLSYGKNlgklflEKIDEEKKKSEHmIKAMEAYIEDLDEIKEKSPEI 1262
|
650 660 670
....*....|....*....|....*....|....
gi 71991177 2697 EKGSSLDLNIPQRV-TRSAAHADISFYFRTEQEH 2729
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMeTFNISHDDDKDHHIISKKH 1296
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2528-2831 |
8.35e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.77 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2528 TKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpKYSKNTLDSIDEKVQEVEKLKAEIDANIEETR 2607
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL-EQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2608 AKISEIAGKAEEITEKANSamegirlARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAA 2687
Cdd:COG4372 101 EELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2688 NRIKLGAHFEKGSSLDLNIPQRVTRSAAHAD-----ISFYFRTEQEHGIPLFFGNEETAVGSRAVPTADY---VAAEIEY 2759
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEaekliESLPRELAEELLEAKDSLEAKLGLALSALLDALEleeDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2760 GRPKITVDLGDAPAVVKLDTPVNDGLWRRL-----------NIERIGKTVSVTLSKPNSVETAETKSSVAGGNKSVLNLN 2828
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALelealeeaaleLKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
...
gi 71991177 2829 QQI 2831
Cdd:COG4372 334 ILL 336
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
656-696 |
9.03e-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: 9.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFP 696
Cdd:cd00055 2 CDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2037-2080 |
9.21e-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: 9.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71991177 2037 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHG 2080
Cdd:cd00055 2 CDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2306-2685 |
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 71991177 2306 KLEEIQKKIQEetekLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADK----SNNIAKMLQLTKVENLVAAITDD 2381
Cdd:COG4717 72 ELKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleklLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2382 LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLN-ETRNDV------AEALEAAKKRVRRDEKSVDMQLVNAKA 2454
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELqdlaeeLEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2455 HELHLQATTLRQtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYE-----ALSAEPAFAESVQNARDKPFPDETK 2529
Cdd:COG4717 228 ELEQLENELEAA---ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2530 EKIDALSKtvSQDLKEteklkkqlEQLTELSEKLRKRKEAVKAGIPKYSKnTLDSIDEKVQEVEKLKAEIDanIEETRAK 2609
Cdd:COG4717 305 EELQALPA--LEELEE--------EELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEELQ--LEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2610 ISEIAGKA-----EEITEKANSAMEGIRLARRNSV---QLNKLAPVIVS------------KFEELKKLSSARSAKVDSV 2669
Cdd:COG4717 372 IAALLAEAgvedeEELRAALEQAEEYQELKEELEEleeQLEELLGELEEllealdeeeleeELEELEEELEELEEELEEL 451
|
410
....*....|....*.
gi 71991177 2670 SDKVSQIKEMIAVARD 2685
Cdd:COG4717 452 REELAELEAELEQLEE 467
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1829-1872 |
1.25e-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: 1.25e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1829 PCECNGHSA---TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1872
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2172-2680 |
1.72e-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: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2172 RNKKEFNDI-NEITKMLN-----DEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKN--ITLNgteflQEV 2243
Cdd:TIGR01612 1511 KNKELFEQYkKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKekFRIE-----DDA 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2244 MK--RAQRA----RQSVRSLAEIALAIGSSSKAVNvdpRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEeiqkKIQEE 2317
Cdd:TIGR01612 1586 AKndKSNKAaidiQLSLENFENKFLKISDIKKKIN---DCLKETESIEKKISSFSIDSQDTELKENGDNLN----SLQEF 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2318 TEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSK-----ADKSNNIAKM----LQLTK------VENLVAAI-TDD 2381
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIAnkeeIESIKelieptIENLISSFnTND 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2382 LERVEAAKgEFQKLNVAIGNITENLKDKREEMTHAVTTL-------NETRNDVAEALEAAKKRVRRDEKSvDMQLVNAKA 2454
Cdd:TIGR01612 1739 LEGIDPNE-KLEEYNTEIGDIYEEFIELYNIIAGCLETVskepityDEIKNTRINAQNEFLKIIEIEKKS-KSYLDDIEA 1816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2455 HELHLQATTLRQTFDNNKDN-TDQAVEAANAFSNLTDTLKNAKAQID------------NAYEAL----------SAEPA 2511
Cdd:TIGR01612 1817 KEFDRIINHFKKKLDHVNDKfTKEYSKINEGFDDISKSIENVKNSTDenllfdilnktkDAYAGIigkkyysykdEAEKI 1896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2512 F------AES----VQNARDKPFPDETkeKIDALSkTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAV------KAGIP 2575
Cdd:TIGR01612 1897 FinisklANSiniqIQNNSGIDLFDNI--NIAILS-SLDSEKEDTLKFIPSPEKEPEIYTKIRDSYDTLldifkkSQDLH 1973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2576 KYSKNTLDSIDEKVQEVEKLKAEidaniEETRAKISEIAGKAEEITekansamegirlarrNSVQLnklapvIVSKFEEL 2655
Cdd:TIGR01612 1974 KKEQDTLNIIFENQQLYEKIQAS-----NELKDTLSDLKYKKEKIL---------------NDVKL------LLHKFDEL 2027
|
570 580
....*....|....*....|....*..
gi 71991177 2656 KKLsSARSAKVDSV--SDKVSQIKEMI 2680
Cdd:TIGR01612 2028 NKL-SCDSQNYDTIleLSKQDKIKEKI 2053
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
808-854 |
1.92e-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: 1.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 808 SCHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHYFPTLWHN 854
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
656-701 |
2.09e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 656 CECLLSGAKGQTCDS-NGQCYCKGNFEGERCDRCKPNFYNFPiCEEC 701
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2279-2629 |
3.21e-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: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2279 KEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEelaaylNSAQQLLKESKSKADK 2358
Cdd:pfam09731 102 AEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAV------KAHTDSLKEASDTAEI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2359 SNNIAKMLQLTKVEnlvAAITDDLERVEAAK-GEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRnDVAEALEAAKKR 2437
Cdd:pfam09731 176 SREKATDSALQKAE---ALAEKLKEVINLAKqSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQ-SLAKLVDQYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2438 VRRDEKSVDMQLV--------NAKAHELhLQATTLRQTFDNNKDNTDQAVEA-----ANAFSNLTDTLKNAKAQIDNAYE 2504
Cdd:pfam09731 252 VASERIVFQQELVsifpdiipVLKEDNL-LSNDDLNSLIAHAHREIDQLSKKlaelkKREEKHIERALEKQKEELDKLAE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2505 ALSAEpafAESVQNARDKPFPDETKEKIDALSKtvsqdlKETEKLKKQLEQLTE-LSEKLRKRkeavkagipkyskntld 2583
Cdd:pfam09731 331 ELSAR---LEEVRAADEAQLRLEFEREREEIRE------SYEEKLRTELERQAEaHEEHLKDV----------------- 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2584 sidEKVQEVE---KLKAEIDANIEETRA----KISEIAGKAEEItEKA---NSAME 2629
Cdd:pfam09731 385 ---LVEQEIElqrEFLQDIKEKVEEERAgrllKLNELLANLKGL-EKAtssHSEVE 436
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2246-2679 |
3.49e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 62.58 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2246 RAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQ---YPEKAQtvpgKLEE-IQKKIQEEtekL 2321
Cdd:pfam02029 11 RRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeaFLDRTA----KREErRQKRLQEA---L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2322 DKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlqltkveNLVAAITDDLERVEAakgEFQKLNVAIGN 2401
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDS-----------RLGRYKEEETEIREK---EYQENKWSTEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2402 ITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRvRRDEKSVDMqlvnakahelhlqattlRQTFDNNKDNTDQAVEA 2481
Cdd:pfam02029 150 RQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIK-KEKKVKYES-----------------KVFLDQKRGHPEVKSQN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2482 ANAFSNLTDTLKNAKAQIDNAYEALSAEpafAESVQNARDKpfpdetKEKID-ALSKTVSQdlkETEKLK-KQLEQLTEL 2559
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQEREEE---AEVFLEAEQK------LEELRrRRQEKESE---EFEKLRqKQQEAELEL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2560 SEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVE---KLKAEID---ANIEETRAKISEIaGKAEE-------------- 2619
Cdd:pfam02029 280 EELKKKREERRKLLEEEEQRRKQEEAERKLREEEekrRMKEEIErrrAEAAEKRQKLPED-SSSEGkkpfkcfspkgssl 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2620 -ITEKANSAMEGirLARRNSVQLNKlAPVIVSKFE------------ELKKLSSARSAKVD--SVSDKVSQIKEM 2679
Cdd:pfam02029 359 kITERAEFLNKS--LQKSSSVKKTH-PPAVVSKIDsrleqytsaiesSTKEAKPTKPAASDlpVPAEGVRNIKSM 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2284-2522 |
3.59e-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: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2284 TLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQketfeaqkkrAEELAAYLNSAQQLLKESKSKADKSNNia 2363
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAE----------LEELNEEYNELQAELEALQAEIDKLQA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2364 kmlQLTKVENLVAAITDDL-ERVEAAK---GEFQKLNVAIGNitENLKD--KReemTHAVTTLNETRNDVAEALEAAKKR 2437
Cdd:COG3883 73 ---EIAEAEAEIEERREELgERARALYrsgGSVSYLDVLLGS--ESFSDflDR---LSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2438 VRRDEKSVDMQLVNAKAhelhlqattLRQTFDNNKDNTDQAVEAANAfsnLTDTLKNAKAQIDNAYEALSAEPAFAESVQ 2517
Cdd:COG3883 145 LEAKKAELEAKLAELEA---------LKAELEAAKAELEAQQAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
....*
gi 71991177 2518 NARDK 2522
Cdd:COG3883 213 AAAAA 217
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2248-2758 |
3.68e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2248 QRARQSVRSLAEIALAIGSSSKAV--NVDPRLLKEAE---ETLMTLEAASADQYPEKAQTVPGKLEEiqkkiqEETEKLD 2322
Cdd:NF041483 629 AQAEQEAERLRTEAAADASAARAEgeNVAVRLRSEAAaeaERLKSEAQESADRVRAEAAAAAERVGT------EAAEALA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2323 KQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAITDdleRVEAAKGEFQKLnvaignI 2402
Cdd:NF041483 703 AAQE--EAARRRRE--------AEETLGSARAEADQERERAR----EQSEELLASARK---RVEEAQAEAQRL------V 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2403 TEnlKDKR--EEMTHAVTTLNETRNDVA--------------EALEAAKKRVRRdEKSVDMQLVNAKAHelhlqATTLRQ 2466
Cdd:NF041483 760 EE--ADRRatELVSAAEQTAQQVRDSVAglqeqaeeeiaglrSAAEHAAERTRT-EAQEEADRVRSDAY-----AERERA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2467 TFDNNK--DNTDQAVEAANAFSNLT-------------DTLKNAKAQIDNAYEAL-SAEPAFAESVQNARDkpfpDETKE 2530
Cdd:NF041483 832 SEDANRlrREAQEETEAAKALAERTvseaiaeaerlrsDASEYAQRVRTEASDTLaSAEQDAARTRADARE----DANRI 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALSKT---VSQDLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAgipkyskntldsidEKVQEVEKLKAEIDANIEET 2606
Cdd:NF041483 908 RSDAAAQAdrlIGEATSEAERLTAEARAEAErLRDEARAEAERVRA--------------DAAAQAEQLIAEATGEAERL 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2607 RAKISEIAGKAEEITE---------KANSAMEGIRL-------------------ARRNSVQLNKLAPVIVSKFEELKKL 2658
Cdd:NF041483 974 RAEAAETVGSAQQHAErirteaervKAEAAAEAERLrteareeadrtldearkdaNKRRSEAAEQADTLITEAAAEADQL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2659 -SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEkGSSLdlnipqrVTRSAAHADisfyfrteqehgiPLFFG- 2736
Cdd:NF041483 1054 tAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVE-GNSL-------VEKARTDAD-------------ELLVGa 1112
|
570 580
....*....|....*....|...
gi 71991177 2737 -NEETAVGSRAVPTADYVAAEIE 2758
Cdd:NF041483 1113 rRDATAIRERAEELRDRITGEIE 1135
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2306-2762 |
3.79e-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: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQ---KETFEAQKKRaeelaaylnsaqqLLKESKSKADKsnniaKMLQLTKVENLVAAITDDL 2382
Cdd:pfam02463 170 KKKEALKKLIEETENLAELiidLEELKLQELK-------------LKEQAKKALEY-----YQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2383 ERVEAakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKrvrrdEKSVDMQLVNAKAHELHLQAT 2462
Cdd:pfam02463 232 LKLNE---ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-----LQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2463 TLRQtfdNNKDNTDQAVEAANAFSNLTDTLKNAKAQIdnayEALSAEPAFAESVQNARdkpfpdetKEKIDALSKtvsqd 2542
Cdd:pfam02463 304 KLER---RKVDDEEKLKESEKEKKKAEKELKKEKEEI----EELEKELKELEIKREAE--------EEEEEELEK----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2543 lketeKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDsIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITE 2622
Cdd:pfam02463 364 -----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL-KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2623 KANSAMEGIRLarrNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVsdKVSQIKEMIAVARDAANRIKLGAHFEKGSSL 2702
Cdd:pfam02463 438 SIELKQGKLTE---EKEELEKQELKLLKDELELKKSEDLLKETQLVK--LQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2703 DLNIPQRVTRSAAHADIsfyFRTEQEHGIPLFFGNEETAVGSRAVPTADYVAAEIEYGRP 2762
Cdd:pfam02463 513 LALIKDGVGGRIISAHG---RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1990-2034 |
3.84e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1990 CECSQCGS--QYCDNKSGGCECKINVEGDSCDRCKPDHWGFSkCQGC 2034
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. |
1830-1877 |
3.94e-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: 3.94e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 1830 CECNGH---SATCDPDTGICtDCEHNTNGDHCEFCNEGHYGNAtNGSPYDC 1877
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2084-2130 |
4.63e-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: 4.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPT--YGCR 2130
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
2156-2658 |
5.11e-09 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 61.96 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2156 AIANISSATIVGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLN 2235
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2236 GTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQ 2315
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2316 EETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAitDDL-ERVEA-AKGEFQ 2393
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAE--GDLtVRIDVdSKDEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2394 KLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVNAKAHELhlqattlRQTFDNNKD 2473
Cdd:COG0840 239 QLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA--EEQAASLEETAAAMEEL-------SATVQEVAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2474 NTDQAVEAAN-----------AFSNLTDTLKNAKAQIDNAYE-----------------------------ALSA--EPA 2511
Cdd:COG0840 310 NAQQAAELAEeaselaeeggeVVEEAVEGIEEIRESVEETAEtieelgessqeigeivdviddiaeqtnllALNAaiEAA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2512 --------FA-----------ESVQNARdkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKlrkrkeavka 2572
Cdd:COG0840 390 rageagrgFAvvadevrklaeRSAEATK------EIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEE---------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2573 gipkySKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLApvivskf 2652
Cdd:COG0840 454 -----AGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELA------- 521
|
....*.
gi 71991177 2653 EELKKL 2658
Cdd:COG0840 522 EELQEL 527
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2140-2634 |
5.27e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2140 IGDVDNLELEIDVLGTAI----ANISSATIVGARLarnKKEFNDINEITKMLNDEENSFGNVFgdaQDILTNSTQIQNKl 2215
Cdd:PRK01156 158 ILEINSLERNYDKLKDVIdmlrAEISNIDYLEEKL---KSSNLELENIKKQIADDEKSHSITL---KEIERLSIEYNNA- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2216 vrtkthsqnsvsSAKNITLNGTefLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVdprlLKEAEETLMTLEAASA-- 2293
Cdd:PRK01156 231 ------------MDDYNNLKSA--LNELSSLEDMKNRYESEIKTAESDLSMELEKNNY----YKELEERHMKIINDPVyk 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2294 ------------DQYPEKAQTVPGKLEEIQK--KIQEETEKLDKQKETFEAQKKRAEEL--------------AAYLNSA 2345
Cdd:PRK01156 293 nrnyindyfkykNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDLnnqilelegyemdyNSYLKSI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2346 QQLLK----ESKSKADKSNNIAKMLQLTKVE-----NLVAAITDDLERVEaakGEFQKLNVAIGNITENLKDKREEMT-- 2414
Cdd:PRK01156 373 ESLKKkieeYSKNIERMSAFISEILKIQEIDpdaikKELNEINVKLQDIS---SKVSSLNQRIRALRENLDELSRNMEml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2415 --HAV-----TTL-----NETRNDVAE---ALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQ--TFDNN------ 2471
Cdd:PRK01156 450 ngQSVcpvcgTTLgeeksNHIINHYNEkksRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKsiNEYNKiesara 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2472 ------------KDNTDQAVEAANAFSNL---------TDTLkNAKAQIDN--------AYEALSAEPAFAESVQNARDK 2522
Cdd:PRK01156 530 dledikikinelKDKHDKYEEIKNRYKSLkledldskrTSWL-NALAVISLidietnrsRSNEIKKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2523 PFPDETK------EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPkySKNTLDS----IDEKVQEV 2592
Cdd:PRK01156 609 GFPDDKSyidksiREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP--DLKEITSrindIEDNLKKS 686
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 71991177 2593 EKL-------KAEIDANIEETRAKISEIAGKAEEITEKANSaMEGIRLA 2634
Cdd:PRK01156 687 RKAlddakanRARLESTIEILRTRINELSDRINDINETLES-MKKIKKA 734
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
472-516 |
5.30e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 71991177 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. |
1554-1602 |
5.33e-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: 5.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLSAENPLGC 1602
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
519-559 |
6.12e-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: 6.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 71991177 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 ... |
2316-2658 |
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 71991177 2316 EETEKLDKQKETFEAQKKRAEELAAYLNSAQQL----LKESKSKADKSNNIAKML---------QLTKVENLVAAITDDL 2382
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVksleLKKKSQKNLKESKDQKELekeiralvqERGEQDKRLQALEEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2383 ERVEAakgefqKLNVAIgnitenlKDKREeMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQAT 2462
Cdd:pfam15905 104 EKVEA------KLNAAV-------REKTS-LSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2463 TLRQTFDNNKDNTDQAVEAANafsnltDTLKNAKAQIDNAYEALSaepafaesvqnardkpfpDETKEKIDALSktvsqd 2542
Cdd:pfam15905 170 AKMKEVMAKQEGMEGKLQVTQ------KNLEHSKGKVAQLEEKLV------------------STEKEKIEEKS------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2543 lkETEKLKKQLEQLTELSEKLRKRKEAVkagipKYSKNTLdsiDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEI-T 2621
Cdd:pfam15905 220 --ETEKLLEYITELSCVSEQVEKYKLDI-----AQLEELL---KEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLeS 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 71991177 2622 EKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2658
Cdd:pfam15905 290 EKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2228-2676 |
1.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2228 SAKNITLNGTEfLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASA--DQYPEKAQT--- 2302
Cdd:COG4717 62 QGRKPELNLKE-LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALeae 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2303 ---VPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNS-AQQLLKESKSKADKSNNIAKmlQLTKVENLVAAI 2378
Cdd:COG4717 141 laeLPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQ--RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2379 TDDLERVEAAKGEFQKlNVAIGNITENLKDKRE---------EMTHAVTTLNETRNDVAEAL---------EAAKKRVRR 2440
Cdd:COG4717 219 QEELEELEEELEQLEN-ELEAAALEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLflvlgllalLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2441 DEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAEsvqnaR 2520
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-----I 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2521 DKPFPDETKEKIDALSKTVSQdLKETEKLKKQLEQLTE-LSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEI 2599
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEqLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2600 DANIEETRAKISEIA--GKAEEITEKANSAMEGIR-LARRNSVqlNKLAPVIVSKFEELkklssARSAKVDSVSDKVSQI 2676
Cdd:COG4717 452 REELAELEAELEQLEedGELAELLQELEELKAELReLAEEWAA--LKLALELLEEAREE-----YREERLPPVLERASEY 524
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1936-1987 |
1.27e-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: 1.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 1936 PCQCNGNNNLtdSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVTAKNC 1987
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2139-2506 |
1.29e-08 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 60.78 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2139 LIGDVDNLELEIDVLGTAIANISSATIVGARLARNKKEFNDINEITKMLNDEENSF--GNVFGDAQDILTNSTQIQNKLV 2216
Cdd:COG5281 50 AAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAAAEAALAALAAAalALAAAALAEAALAAAAAAAAAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2217 RTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQY 2296
Cdd:COG5281 130 AAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2297 PEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLL--KESKSKADKSNNIAKMLQLTKVENL 2374
Cdd:COG5281 210 AAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAAAAAALALAaaAELALTAQAEAAAAAAAAAAAAAQA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2375 VAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQL---VN 2451
Cdd:COG5281 290 AEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALeaaAA 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991177 2452 AKAHELHLQATTLRQTFDNNKDNTDQAVEAA--------NAFSNLTDTLKNAKAQIDNAYEAL 2506
Cdd:COG5281 370 AAAAELAAAGDWAAGAKAALAEYADSATNVAaqvaqaatSAFSGLTDALAGAVTTGKLLFDAL 432
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2245-2662 |
1.35e-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: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2245 KRAQRARQSVRSLAEIAlaigssskavnvdpRLLKEAEETLMTLEAASADqypEKAQtvpgKLEEIQKKIQEETEKLDKQ 2324
Cdd:COG3064 60 AKAEAEQRAAELAAEAA--------------KKLAEAEKAAAEAEKKAAA---EKAK----AAKEAEAAAAAEKAAAAAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2325 KETFEAQKKRAEElaaylnSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITE 2404
Cdd:COG3064 119 KEKAEEAKRKAEE------EAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2405 NLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANA 2484
Cdd:COG3064 193 ADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2485 FSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFPDETkekidalSKTVSQDLKETEKLKKQLEQLTELSEKLR 2564
Cdd:COG3064 273 ALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA-------VLAAAAAAGALVVRGGGAASLEAALSLLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2565 KRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKL 2644
Cdd:COG3064 346 AGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLA 425
|
410
....*....|....*...
gi 71991177 2645 APVIVSKFEELKKLSSAR 2662
Cdd:COG3064 426 LAGAAGAVVALLVKLVAD 443
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2178-2677 |
1.43e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 61.39 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2178 NDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKL--VRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVR 2255
Cdd:PTZ00440 536 NEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIkyIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFI 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2256 SLAEIaLAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTvpGKLEEIQKKIQEETEKLDKQKETFEAQ--KK 2333
Cdd:PTZ00440 616 NEKND-LQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSK--EDLQTLLNTSKNEYEKLEFMKSDNIDNiiKN 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2334 RAEELAAYLNSAQQLLKEskskadKSNNIAKMLQ--LTKVENLVAAITDDLERVEAAKGEF--------QKLNVAIGNIT 2403
Cdd:PTZ00440 693 LKKELQNLLSLKENIIKK------QLNNIEQDISnsLNQYTIKYNDLKSSIEEYKEEEEKLevykhqiiNRKNEFILHLY 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2404 ENLKD-------KREEMTHAVTTLNETR--NDVAEALEAAKKRVRRDEKSVDMQLVNAKAH-ELHLQAT-TLRQTFDNNK 2472
Cdd:PTZ00440 767 ENDKDlpdgkntYEEFLQYKDTILNKENkiSNDINILKENKKNNQDLLNSYNILIQKLEAHtEKNDEELkQLLQKFPTED 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2473 DNTDQAvEAANAFSNLTDTLKNAKAQIDNAYEALSAepafAESVQNARD------------KPFPDETKEKIDALSKTVS 2540
Cdd:PTZ00440 847 ENLNLK-ELEKEFNENNQIVDNIIKDIENMNKNINI----IKTLNIAINrsnsnkqlvehlLNNKIDLKNKLEQHMKIIN 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2541 QDL---------------KETEKLKKQL--EQLTELS---EKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEID 2600
Cdd:PTZ00440 922 TDNiiqkneklnllnnlnKEKEKIEKQLsdTKINNLKmqiEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEID 1001
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2601 ----------ANIEETRAK---------ISEIAGKAEEITEKAN---SAMEGIR-----LARRNSVQLNKlAPVIVSKFE 2653
Cdd:PTZ00440 1002 klnvnynilnKKIDDLIKKqhddiieliDKLIKEKGKEIEEKVDqyiSLLEKMKtklssFHFNIDIKKYK-NPKIKEEIK 1080
|
570 580
....*....|....*....|....
gi 71991177 2654 ELKKLSSARSAKVDSVSDKVSQIK 2677
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKLIEIK 1104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2227-2646 |
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 71991177 2227 SSAKNITLNGTEFLQEVMKRAQRARQSVRSLaeialaigssskavnvdprllkEAEETLMTLEAASADQY-PEKAQTVPG 2305
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSL----------------------HGKAELLTLRSQLLTLCtPCMPDTYHE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETfEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiakmlQLTKVENLVAAItdDLERV 2385
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRA-----QEAVLEETQERI--NRARK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2386 EAAKGEFQKlnvAIGNItenlkDKREEMTHavTTLNETRNDVAEALeAAKKRVRRDEKSVDMQLV-----------NAKA 2454
Cdd:TIGR00618 292 AAPLAAHIK---AVTQI-----EQQAQRIH--TELQSKMRSRAKLL-MKRAAHVKQQSSIEEQRRllqtlhsqeihIRDA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2455 HELHL-------QATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQID---NAYEALSAEPAFAESVQNARDKPF 2524
Cdd:TIGR00618 361 HEVATsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtSAFRDLQGQLAHAKKQQELQQRYA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2525 P----------DETKEKIDALSKtVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVK----------------------- 2571
Cdd:TIGR00618 441 ElcaaaitctaQCEKLEKIHLQE-SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepcplcgscihpnparqd 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2572 AGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEI-------TEKANSAMEGIRLARRNSVQLNKL 2644
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLQDL 599
|
..
gi 71991177 2645 AP 2646
Cdd:TIGR00618 600 TE 601
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2037-2086 |
1.71e-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: 1.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2037 CHC-GTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYgeHGCDKCDC 2086
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL--PSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2526-2658 |
1.74e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2526 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLR-KRKEAVKagipkyskntldSIDEKVQEVEKLKAEIDANIE 2604
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNA------------QVKELREEAQELREKRDELNE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2605 etraKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKL 2658
Cdd:COG1340 72 ----KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL 121
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1989-2035 |
1.97e-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: 52.74 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1989 SCECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGF-SKCQGCQ 2035
Cdd:cd00055 1 PCDCNGHGSLsgQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1554-1603 |
3.15e-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: 3.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLsAENPLGCV 1603
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2319-2691 |
3.39e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2319 EKLDKQKETFEAQKKRAEELAAYLNSAqqlLKESKSKADKSNNiakmlQLTKVENLVAAITDDLERVEA----AKGEFQK 2394
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQ---LRKALFELDKLQE-----ELEQLREELEQAREELEQLEEeleqARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2395 LNvaignitENLKDKREEMTHAVTTLNETRndvaEALEAAKKRVRRDEKSVDmqlvnakahELHLQATTLRQTfdnNKDN 2474
Cdd:COG4372 78 LE-------EELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELE---------ELQKERQDLEQQ---RKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2475 TDQAVEAANAFSNLTDTLKNAKAQIDNayeaLSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKETEKLKKQLE 2554
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLES----LQEELAALEQELQALSE---AEAEQALDELLKEANRNAEKEEELAEAEK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2555 QLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRaKISEIAGKAEEITEKANSAMEGIRLA 2634
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI-EELELAILVEKDTEEEELEIAALELE 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2635 RRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
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 |
4.13e-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: 4.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 427 CDCDPD-KHTGACAEETGKCECLPRFVGEDCDQCASGYYDAPKCKPCEC 474
Cdd:pfam00053 1 CDCNPHgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2302-2438 |
4.45e-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: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2302 TVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNiAKMLQ-LTK-VENLVAAIT 2379
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEaLQKeIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2380 D--D-----LERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRV 2438
Cdd:COG1579 107 DleDeilelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2084-2132 |
4.74e-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: 51.59 E-value: 4.74e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 2084 CDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGCRRC 2132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2295-2657 |
5.65e-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: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2295 QYPEKAQTVPGKLEeiqkKIQEETEKLDKQKETFEAQKKRA-----------EELAAYLNSAQqlLKESKSKADksNNIA 2363
Cdd:pfam05701 32 QTVERRKLVELELE----KVQEEIPEYKKQSEAAEAAKAQVleelestkrliEELKLNLERAQ--TEEAQAKQD--SELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2364 KMlqltKVENLVAAITDDlERV------EAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKR 2437
Cdd:pfam05701 104 KL----RVEEMEQGIADE-ASVaakaqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2438 vrrdEKSVD---MQLVNAK-----AHELHLQA--------TTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDN 2501
Cdd:pfam05701 179 ----EKTVEeltIELIATKeslesAHAAHLEAeehrigaaLAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2502 AYE---ALSAEpaFAESVQNARDKPFPDETKEKIDALS--KTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPK 2576
Cdd:pfam05701 255 ASAlllDLKAE--LAAYMESKLKEEADGEGNEKKTSTSiqAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2577 ySKNTLDSIdeKVQE------VEKLKAEID----------ANIEETRAKISEIAGK-------AEEITEKANSAMEGIRL 2633
Cdd:pfam05701 333 -EKAELASL--RQREgmasiaVSSLEAELNrtkseialvqAKEKEAREKMVELPKQlqqaaqeAEEAKSLAQAAREELRK 409
|
410 420
....*....|....*....|....
gi 71991177 2634 ARRNSVQLNKLAPVIVSKFEELKK 2657
Cdd:pfam05701 410 AKEEAEQAKAAASTVESRLEAVLK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2240-2523 |
6.04e-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: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2240 LQEVMKRAQRARQSVRS-LAEIALAIGSSSKAVNvdpRLLKEAEETLMTLEAASADQYPEKAQTvpGKLEEIQKKIQEET 2318
Cdd:COG1196 251 LEAELEELEAELAELEAeLEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2319 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLvAAITDDLERVEAAKGEFQKLNVA 2398
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2399 IGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVdmqlvnAKAHELHLQATTLRQtfdnnkDNTDQA 2478
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE------AELEEEEEALLELLA------ELLEEA 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71991177 2479 VEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKP 2523
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2308-2694 |
7.18e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2308 EEIQKKIQEETEkLDKQKETFEAQKKR----AEELAAYLNS-AQQLLKESKSKADKSnniakmlqltkvenLVAAitddl 2382
Cdd:NF041483 124 EAVQRRQQLDQE-LAERRQTVESHVNEnvawAEQLRARTESqARRLLDESRAEAEQA--------------LAAA----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2383 eRVEAAKgefqklnvaignITEnlkDKREEMThavttlNETRNDVAEAlEAAKKRVRRDEKsvdmQLVNA---KAHELHL 2459
Cdd:NF041483 184 -RAEAER------------LAE---EARQRLG------SEAESARAEA-EAILRRARKDAE----RLLNAastQAQEATD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2460 QATTLRQTFDNNKDNT-DQAVEAANA----FSNLTDTLKNAKAQIDN----AYEALSAEPAFAESVQNARDKpfpdETKE 2530
Cdd:NF041483 237 HAEQLRSSTAAESDQArRQAAELSRAaeqrMQEAEEALREARAEAEKvvaeAKEAAAKQLASAESANEQRTR----TAKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2531 KIDALsktVSQDLKETEKLKKQLEQL------------TELSEKLR-KRKEAVKAGIPKYSKNTLD-----SIDEK---- 2588
Cdd:NF041483 313 EIARL---VGEATKEAEALKAEAEQAladaraeaeklvAEAAEKARtVAAEDTAAQLAKAARTAEEvltkaSEDAKattr 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2589 --VQEVEKLKAEIDANIEETRAKISEIA----GKAEEITE----KANSAMEGIRLARRNSVQLNKLApviVSKFEELKkl 2658
Cdd:NF041483 390 aaAEEAERIRREAEAEADRLRGEAADQAeqlkGAAKDDTKeyraKTVELQEEARRLRGEAEQLRAEA---VAEGERIR-- 464
|
410 420 430
....*....|....*....|....*....|....*.
gi 71991177 2659 SSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGA 2694
Cdd:NF041483 465 GEARREAVQQIEEAARTAEELLTKAKADADELRSTA 500
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
472-509 |
8.86e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 8.86e-08
10 20 30
....*....|....*....|....*....|....*...
gi 71991177 472 CECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGY 509
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1880-1934 |
9.13e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 9.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 1880 CACPFAPTNNfaKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHPQISGESC 1934
Cdd:pfam00053 1 CDCNPHGSLS--DTCD-PETGQ---CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
427-467 |
9.44e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 427 CDCDPDKH-TGACAEETGKCECLPRFVGEDCDQCASGYYDAP 467
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
809-847 |
9.72e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.72e-08
10 20 30
....*....|....*....|....*....|....*....
gi 71991177 809 CHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHY 847
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1461-1504 |
1.07e-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: 1.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDPLI-GCQ 1504
Cdd:cd00055 2 CDCNghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1461-1499 |
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 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDP 1499
Cdd:smart00180 1 CDCDpggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2306-2690 |
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 71991177 2306 KLEEIQKKIQE-ETEKLDKqketFEAQKKRAEELAAY--LNSAQQLLKESKSKADK-SNNIAKMLQltKVENLVAAITDD 2381
Cdd:pfam06160 46 KFEEWRKKWDDiVTKSLPD----IEELLFEAEELNDKyrFKKAKKALDEIEELLDDiEEDIKQILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2382 LERVEAAKGEFQKLN-----------VAIGNITENLKDKREEMTHAVTtLNETRNDVA--EALEAAKKRVRRDEKsvDMQ 2448
Cdd:pfam06160 120 REEVEELKDKYRELRktllanrfsygPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEarEVLEKLEEETDALEE--LME 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2449 LVNAKAHELHlqaTTLRQTFDNNKDNTDQAVEAANAFS--NLTDTLKNAKAQIDNAYEAL-SAEPAFAESVQnardkpfp 2525
Cdd:pfam06160 197 DIPPLYEELK---TELPDQLEELKEGYREMEEEGYALEhlNVDKEIQQLEEQLEENLALLeNLELDEAEEAL-------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2526 DETKEKIDALsktvsQDLKETE------------KLKKQLEQLTELSEKLRKRKEAVK---------AGIPKYSKNTLDS 2584
Cdd:pfam06160 266 EEIEERIDQL-----YDLLEKEvdakkyveknlpEIEDYLEHAEEQNKELKEELERVQqsytlneneLERVRGLEKQLEE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2585 IDEKVQE-VEKLKA------EIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNK-------------L 2644
Cdd:pfam06160 341 LEKRYDEiVERLEEkevaysELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLelreikrlveksnL 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2645 aPVIVSKFEELKKLSSARSAKV-----------DSVSDKVSQIKEMIAVARDAANRI 2690
Cdd:pfam06160 421 -PGLPESYLDYFFDVSDEIEDLadelnevplnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2147-2523 |
1.47e-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: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2147 ELEIDVLGTAIANISSATI---VGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNklVRTKTHSQ 2223
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGnlgSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTD--LRLEKLGE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2224 NsVSSAKNITLNGTEFLQEVmkraQRARQSVRSLAEIALAIGSSSKAVNVDPR--LLKEAEETLMTLEAASADQYPEKAQ 2301
Cdd:COG5185 273 N-AESSKRLNENANNLIKQF----ENTKEKIAEYTKSIDIKKATESLEEQLAAaeAEQELEESKRETETGIQNLTAEIEQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2302 TVPgKLEEIQKKIQEE------TEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLV 2375
Cdd:COG5185 348 GQE-SLTENLEAIKEEienivgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2376 AAITDDLERVEAAKgefQKLNVAIGNITENLKDKREEMTHAVT-TLNETRNDVAEALEAAKKRVRRDEKSVDmqlvnaka 2454
Cdd:COG5185 427 RQIEQATSSNEEVS---KLLNELISELNKVMREADEESQSRLEeAYDEINRSVRSKKEDLNEELTQIESRVS-------- 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2455 helhlqatTLRQTFDNNKDNTDQAVEAA-NAFSNLTDTLKNA-KAQIDNAYEALSAEPAFAESVQNARDKP 2523
Cdd:COG5185 496 --------TLKATLEKLRAKLERQLEGVrSKLDQVAESLKDFmRARGYAHILALENLIPASELIQASNAKT 558
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-467 |
1.68e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 71991177 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 ... |
2179-2422 |
1.74e-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: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2179 DINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNgtefLQEVMKRAQRARQSVRSLA 2258
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDN----IKEINEKVATLGENDFALP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2259 EIALaigsSSKAVNVDpRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLdkqketFEAQKKRAEEL 2338
Cdd:pfam06008 117 SSDL----SRMLAEAQ-RMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAL------ANALRDSLAEY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2339 AAYLNSAQQLLKESKSKADKSNniaKMLQLTKvenlvAAITDDLERVEAAKGefQKLnvaigNITENLKDKREEMTHAVT 2418
Cdd:pfam06008 186 EAKLSDLRELLREAAAKTRDAN---RLNLANQ-----ANLREFQRKKEEVSE--QKN-----QLEETLKTARDSLDAANL 250
|
....
gi 71991177 2419 TLNE 2422
Cdd:pfam06008 251 LLQE 254
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1461-1503 |
2.25e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 2.25e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1461 CQCN----AGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGY--DPLIGC 1503
Cdd:pfam00053 1 CDCNphgsLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2240-2563 |
2.33e-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: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2240 LQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVD-PRLLKEAEETLMTLEAASadqypEKAQTVPGKLEEIQKKIQEET 2318
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLS-----EAEDMLACEQHALLRKLQPEQ 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2319 EKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVA 2398
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2399 IGNITENLKD---KREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHElHLQATTLRQTFDNNKDNT 2475
Cdd:TIGR00618 706 LRELETHIEEydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN-NEEVTAALQTGAELSHLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2476 DQAVEAANAFSNLTDTLKNAKAQIDNayEALSAEPAF-AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLE 2554
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQ--EIPSDEDILnLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*....
gi 71991177 2555 QLTELSEKL 2563
Cdd:TIGR00618 863 QLTQEQAKI 871
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2335-2622 |
2.51e-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: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2335 AEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVE--NLVAAITDDLERVEAAKgefqKLNvAIGN--ITENLKDKR 2410
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKgsNVIEISYTSPDPELAAA----VAN-ALAEayLEQNLELRR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2411 EEMTHAVTTLNETRNDVAEALEAAKKRV---RRDEKSVDMQlvnakahelhlqattlrqtfDNNKDNTDQAVEAANAFSN 2487
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLS--------------------EEAKLLLQQLSELESQLAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2488 LTDTLKNAKAQIDNAYEALSAEPAFAESVQNardkpfpdetkekiDALSKTVSQDLKETE-KLKKQLEQLTELSEK---L 2563
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQ--------------SPVIQQLRAQLAELEaELAELSARYTPNHPDviaL 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71991177 2564 RKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITE 2622
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1554-1602 |
2.56e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 1554 CSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDlsaENPLGC 1602
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1880-1927 |
2.56e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 71991177 1880 CACPfaPTNNFAKSCDvSEEGQllqCNCKPGYTGDRCDRCASGFFGHP 1927
Cdd:smart00180 1 CDCD--PGGSASGTCD-PDTGQ---CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2312-2598 |
2.70e-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: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2312 KKIQEETEKLDKQ-------KETFEA----QKKRAEELAAYLNSAqqlLKESKSKADKSNNIAKMLQLTkvenlVAAITD 2380
Cdd:pfam05701 229 KQAEEELQRLNQQllsakdlKSKLETasalLLDLKAELAAYMESK---LKEEADGEGNEKKTSTSIQAA-----LASAKK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2381 DLERV----EAAKGEFQKLNVAIGNITENL-KDK--------REEMTH-AVTTLNETRNDVAEALEAAKKRVRRD-EKSV 2445
Cdd:pfam05701 301 ELEEVkaniEKAKDEVNCLRVAAASLRSELeKEKaelaslrqREGMASiAVSSLEAELNRTKSEIALVQAKEKEArEKMV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2446 DM--QLVNA--KAHELHLQATTLRQTFDNNKDNTDQAVEAANAF-SNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNAR 2520
Cdd:pfam05701 381 ELpkQLQQAaqEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVeSRLEAVLKEIEAAKASEKLALAAIKALQESESSAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2521 DKPFPDE------TKEKIDALSK---------------TVSQ--DLKETEKlkKQLEQLTELSEKLRKRKEAVKAGIPKY 2577
Cdd:pfam05701 461 STNQEDSprgvtlSLEEYYELSKraheaeelankrvaeAVSQieEAKESEL--RSLEKLEEVNREMEERKEALKIALEKA 538
|
330 340
....*....|....*....|....
gi 71991177 2578 SKNTldsiDEKV---QEVEKLKAE 2598
Cdd:pfam05701 539 EKAK----EGKLaaeQELRKWRAE 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2167-2708 |
2.88e-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: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2167 GARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQdiltnstqiqnklVRTKTHSQNSVSSAKNITLNGTEFLQEVMKR 2246
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ-------------LQADRHQEHIRARDSLIQSLATRLELDGFER 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2247 AQRARQSVRSLaeIALAIGSSSKAVNVDPRLLKEAEETLMTLEaasadqypEKAQTVPGKLEEIQKKIQEETEKLDKQKE 2326
Cdd:TIGR00606 385 GPFSERQIKNF--HTLVIERQEDEAKTAAQLCADLQSKERLKQ--------EQADEIRDEKKGLGRTIELKKEILEKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2327 TFEAQKKRAEELAA----YLNSAQQLLKESK--SKADKSNNI-AKMLQLTKVENLVAaitdDLERVEAAkgefqklnvai 2399
Cdd:TIGR00606 455 ELKFVIKELQQLEGssdrILELDQELRKAERelSKAEKNSLTeTLKKEVKSLQNEKA----DLDRKLRK----------- 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2400 gnitenLKDKREEMTHAVTTLNETrndvaeaLEAAKKRVRRDEksvdmqlvnakahelhlqattlrQTFDNNKDNTDQAV 2479
Cdd:TIGR00606 520 ------LDQEMEQLNHHTTTRTQM-------EMLTKDKMDKDE-----------------------QIRKIKSRHSDELT 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2480 EAANAFSN---LTDTL---KNAKAQIDNAYEALSAEPAFAESVQNARDKpfpdETKEKIDALSKTVSQ--DLKETEKLKK 2551
Cdd:TIGR00606 564 SLLGYFPNkkqLEDWLhskSKEINQTRDRLAKLNKELASLEQNKNHINN----ELESKEEQLSSYEDKlfDVCGSQDEES 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2552 QLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEK------VQEVEKLKAEIDANIEETRAKISEIAGKAEEIT---- 2621
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTEselk 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2622 --EKANSAMEGIRLARRNSVQL---------NKLAPV------IVSKFEELKKLSSARSAKVDSVSD---KVSQIKEMIA 2681
Cdd:TIGR00606 720 kkEKRRDEMLGLAPGRQSIIDLkekeipelrNKLQKVnrdiqrLKNDIEEQETLLGTIMPEEESAKVcltDVTIMERFQM 799
|
570 580
....*....|....*....|....*..
gi 71991177 2682 VARDAANRIKLGAHFEKGSSLDLNIPQ 2708
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGSDLDRTVQQ 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2273-2616 |
3.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2273 VDPRLLKEAEETlmtleaASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEEL---AAYLNSAQQLL 2349
Cdd:PTZ00121 1635 VEQLKKKEAEEK------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELK 1708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2350 KESKSKADKSNNIAKM--LQLTKVENLVAAITDDLERVEAAK-GEFQKLNVAignitenlKDKREEMTHAVTTLNETRND 2426
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAeeENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIA--------HLKKEEEKKAEEIRKEKEAV 1780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2427 VAEAL--EAAKKRVRRDEKSVDM----QLVNAKAHELHLQATTLRQTFDNnkdNTDQAVEAANAFSNLTDTLKNAKAQID 2500
Cdd:PTZ00121 1781 IEEELdeEDEKRRMEVDKKIKDIfdnfANIIEGGKEGNLVINDSKEMEDS---AIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2501 NayeaLSAEPAFAESVQNardkpfpdetkekidalsktvsqdlKETEKLKKQLEQLTELSEKLRKRKEAVKAGIP--KYS 2578
Cdd:PTZ00121 1858 N----ENGEDGNKEADFN-------------------------KEKDLKEDDEEEIEEADEIEKIDKDDIEREIPnnNMA 1908
|
330 340 350
....*....|....*....|....*....|....*...
gi 71991177 2579 KNTLDSIDEKVQEVEKLKaeidANIEETRAKISEIAGK 2616
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIK----RDAEETREEIIKISKK 1942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2476-2623 |
3.77e-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: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2476 DQAVEAANAFSNLTDTLKNAKAQIDNA------YEALSaepafaESVQNARDkpfpdetkekIDALSKTVSQDLKETEKL 2549
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVearikkYEEQL------GNVRNNKE----------YEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2550 KKQLEQLTELSEKLRKRKEAVKAgipkyskntldSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEK 2623
Cdd:COG1579 109 EDEILELMERIEELEEELAELEA-----------ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2306-2562 |
3.90e-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: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELaaylnsaQQLLKEsksKADKSNNIAKmlQLTKVENLVAAITDDLERV 2385
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK-------QELIDQ---KEKEKKDLIK--EIEEKEKKISSLEKELEKA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2386 EAakgEFQKLNVAIGNItENLKDKREEMTHAV-TTLNETRNDVAEaleaakkrvrrdeksvdmqlvnakahelhlqattl 2464
Cdd:TIGR04523 623 KK---ENEKLSSIIKNI-KSKKNKLKQEVKQIkETIKEIRNKWPE----------------------------------- 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2465 rqTFDNNKDntdqAVEAANAFSNLTDTLKNAKAqidnayeaLSAEPAFAESVqnaRDKPFPdetkeKIDALSKTVSQDLK 2544
Cdd:TIGR04523 664 --IIKKIKE----SKTKIDDIIELMKDWLKELS--------LHYKKYITRMI---RIKDLP-----KLEEKYKEIEKELK 721
|
250
....*....|....*...
gi 71991177 2545 ETEKLKKQLEQLTELSEK 2562
Cdd:TIGR04523 722 KLDEFSKELENIIKNFNK 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2233-2482 |
5.08e-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: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2233 TLNGTEflqevmKRAQRARQSVRSLAEIALAIGSsskavnvdprlLKEAEETLMTLEAASADQYPEKAQTvpgKLEEIQK 2312
Cdd:COG4913 236 DLERAH------EALEDAREQIELLEPIRELAER-----------YAAARERLAELEYLRAALRLWFAQR---RLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2313 KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKadksnniakmlQLTKVENLVAAITDDLERVEAAKGEF 2392
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-----------RLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2393 QK----LNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKsvdmqlvnaKAHELHLQATTLRQtf 2468
Cdd:COG4913 365 EAllaaLGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---------ELRELEAEIASLER-- 433
|
250
....*....|....
gi 71991177 2469 dnNKDNTDQAVEAA 2482
Cdd:COG4913 434 --RKSNIPARLLAL 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2333-2715 |
5.80e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2333 KRAEELAAYLNSAQQLLKESKSKADKSNN----IAKMLQLTKVENLVAAITD----------DLERVEAAKGEFQKLNVA 2398
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNhegkAEAKAHVGQDEGLKPSYKDfdfdakednrADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2399 IGNITENLKDKREEMTHAvttlnetrNDVAEALEAAK-KRVRRDEKSVDMQlvNAKAHELHLQATTLRQTFDNNKDNTDQ 2477
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKA--------EDARKAEEARKaEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2478 AVEAANAFSNLTDTLKNAKAQ-IDNAYEALSAEPAF-AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQ 2555
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEdARKAEAARKAEEERkAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2556 LTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEiAGKAEEITEKANSAMEGIRLAR 2635
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2636 RNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAA 2715
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2530-2698 |
8.60e-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: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2530 EKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAK 2609
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2610 ISEIAGKAEEITEKANSAMEGIRLARRN-----SVQLNKLAPVIVSKFEELKKLsSARSAKVDSVSDKVSQIKEMI--AV 2682
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLRVKEkigelEAEIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEELerEI 345
|
170
....*....|....*.
gi 71991177 2683 ARDAANRIKLGAHFEK 2698
Cdd:TIGR02169 346 EEERKRRDKLTEEYAE 361
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2202-2680 |
9.92e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.22 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2202 QDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRS-LAEIALAIGSSSKAVNVD------ 2274
Cdd:PTZ00440 1087 EALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKtLKELENMNLEDITLNEVNeieiey 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2275 PRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEET-EKLDkqkeTFEAQKKRAEELAAYlNSAQQLLKESK 2353
Cdd:PTZ00440 1167 ERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERnDHLT----TFEYNAYYDKATASY-ENIEELTTEAK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2354 SKADKSNNIAKM-------------------------------------LQLTKVENLVAAITDDLERVE----AAKGEF 2392
Cdd:PTZ00440 1242 GLKGEANRSTNVdelkeiklqvfsylqqvikennkmenalheiknmyefLISIDSEKILKEILNSTKKAEefsnDAKKEL 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2393 QKLNvaigNITENLKDKREEmthavttLNETRNDVAEALEaaKKRVrrDEKSVDMQLVNAKAHELHLQATTLRQTFDNNK 2472
Cdd:PTZ00440 1322 EKTD----NLIKQVEAKIEQ-------AKEHKNKIYGSLE--DKQI--DDEIKKIEQIKEEISNKRKEINKYLSNIKSNK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2473 DNTDQAVEAANAFSNLTDTLKNAKA------------QIDNAY---EALSAEPAFAESVQNARDKPFPdETKEKIDALSK 2537
Cdd:PTZ00440 1387 EKCDLHVRNASRGKDKIDFLNKHEAiepsnskevniiKITDNInkcKQYSNEAMETENKADENNDSII-KYEKEITNILN 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2538 TVSQDLKET--EKLKKQL---------------EQLTELSEKLRKRKEAvkagiPKYSKNTLDSIDEKVQeveKLKAEID 2600
Cdd:PTZ00440 1466 NSSILGKKTklEKKKKEAtnimddingehsiikTKLTKSSEKLNQLNEQ-----PNIKREGDVLNNDKST---IAYETIQ 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2601 ANIEETRAKISEI---AGKAEEITEKANSAMEGIR-----LARRNSVQLNKLAPVIVS---KFEELKKLSSARSAKVDSV 2669
Cdd:PTZ00440 1538 YNLGRVKHNLLNIlniKDEIETILNKAQDLMRDISkiskiVENKNLENLNDKEADYVKyldNILKEKQLMEAEYKKLNEI 1617
|
570
....*....|.
gi 71991177 2670 SDKVSQIKEMI 2680
Cdd:PTZ00440 1618 YSDVDNIEKEL 1628
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2174-2634 |
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 71991177 2174 KKEFNDINEITKMLNDEENsfgnvfgDAQDILTNSTQIqnklvrTKTHSQNSvssaknitlngtEFLQEVMKRAQRARqs 2253
Cdd:pfam06160 82 KKAKKALDEIEELLDDIEE-------DIKQILEELDEL------LESEEKNR------------EEVEELKDKYRELR-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2254 vRSLAEIALAIGSSSKAVNVDprlLKEAEETLMTLEAASADQYPEKAqtvpgklEEIQKKIQEETEKLDKQ--------- 2324
Cdd:pfam06160 135 -KTLLANRFSYGPAIDELEKQ---LAEIEEEFSQFEELTESGDYLEA-------REVLEKLEEETDALEELmedipplye 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2325 --KETFEAQkkrAEELAA---------YLNSAQQLLKESKSKADK-SNNIAKM--LQLTKVENLVAAIT-------DDLE 2383
Cdd:pfam06160 204 elKTELPDQ---LEELKEgyremeeegYALEHLNVDKEIQQLEEQlEENLALLenLELDEAEEALEEIEeridqlyDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEAAKGEFQKlNVA-----IGNITENLKDKREEMTHAVT--TLNEtrNDVAEALEAAKkrvrrdeksvdmQLvnakaHE 2456
Cdd:pfam06160 281 KEVDAKKYVEK-NLPeiedyLEHAEEQNKELKEELERVQQsyTLNE--NELERVRGLEK------------QL-----EE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2457 LHLQATTLRQTFDNNKdntdqaveaaNAFSNLTDTLKNAKAQIDNaYEALSAEpaFAESVQNARDkpfpDETKEKidals 2536
Cdd:pfam06160 341 LEKRYDEIVERLEEKE----------VAYSELQEELEEILEQLEE-IEEEQEE--FKESLQSLRK----DELEAR----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2537 ktvsqdlketeklkkqlEQLTELSEKLRKRKEAVKA----GIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISE 2612
Cdd:pfam06160 399 -----------------EKLDEFKLELREIKRLVEKsnlpGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDE 461
|
490 500
....*....|....*....|..
gi 71991177 2613 IAGKAEEITEKANSAMEGIRLA 2634
Cdd:pfam06160 462 AQDDVDTLYEKTEELIDNATLA 483
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1879-1934 |
1.12e-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: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 1879 ACACPFAPTNNFakSCDVseegQLLQCNCKPGYTGDRCDRCASGFFGHPqISGESC 1934
Cdd:cd00055 1 PCDCNGHGSLSG--QCDP----GTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2238-2457 |
1.14e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2238 EFLQEVMK-RAQR--ARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEaasaDQY------PEKAQTVPGKLE 2308
Cdd:COG1340 68 ELNEKVKElKEERdeLNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE----WRQqtevlsPEEEKELVEKIK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2309 EIQKKIqEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADK-SNNIAKMLQltKVENLVAAItddlervEA 2387
Cdd:COG1340 144 ELEKEL-EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQElHEEMIELYK--EADELRKEA-------DE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2388 AKGEFQKLNVAIGNITENLKDKREEMthavttlnetrNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHEL 2457
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKEL-----------RELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
2327-2687 |
1.18e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 54.26 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2327 TFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENL 2406
Cdd:COG0840 8 LALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2407 KDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFS 2486
Cdd:COG0840 88 LLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2487 NLTDTLKNAKAQIDNAYEALSAEP-----AFAESVQNARDKPFpDETKEKIDALSK---TVSQDLK---ETEKLKKQLEQ 2555
Cdd:COG0840 168 EAAALALAAAALALALLAAALLALvalaiILALLLSRSITRPL-RELLEVLERIAEgdlTVRIDVDskdEIGQLADAFNR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2556 LTElseKLRKRKEAVKAGIPKYSKNTlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLAR 2635
Cdd:COG0840 247 MIE---NLRELVGQVRESAEQVASAS-EELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2636 RNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAA 2687
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 |
1.37e-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: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 71991177 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHHEDGC 753
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPET-GQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1830-1872 |
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 71991177 1830 CECN--GHSA-TCDPDTGICtDCEHNTNGDHCEFCNEGHYGNATNG 1872
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1990-2037 |
1.69e-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: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 1990 CECSQCGSQ--YCDNKSGGCECKINVEGDSCDRCKPDHWGFSKCQGcQGC 2037
Cdd:pfam00053 1 CDCNPHGSLsdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP-QGC 49
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1808-2133 |
2.00e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 53.43 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1808 CQLCASGYHRVQSGSFLGACVPCECNGHSATCDPDTGICTDCEHNTNGDHCEFCNEghygnatngspyDCMACACPFAPT 1887
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCKTENCKACSNDKREVCEECNSNNYLTPTSQCID------------DCAKIGNYYYTT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1888 NNFAK-SCDVSEEGQLLQCNCKpgytgDRCDRCASGFFghpqISGESCSPCQCNgnnnltdSRSCH-PNSGDCylceqnt 1965
Cdd:pfam03302 69 NANNKkICKECTVANCKTCEDQ-----GQCQACNDGFY----KSGDACSPCHES-------CKTCSgGTASDC------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 1966 dgRHCESCAAWFYGDAVTAKNCSSCECSQCGSQYCDNksggceCKINVEGDS-CDRCKPDHwGFSKCQGCQGCHCGTAAF 2044
Cdd:pfam03302 126 --TECLTGKALRYGNDGTKGTCGEGCTTGTGAGACKT------CGLTIDGTSyCSECATET-EYPQNGVCTSTAARATAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2045 NTQCNVENGqctcrpgatgmRCEHCEHGYWNYgEHGC-------DKCDCEADLSMGTV-----------CDVRTGQCHCQ 2106
Cdd:pfam03302 197 CKASSVANG-----------MCSSCANGYFRM-NGGCyettkfpGKSVCEEANSGGTCqkeapgyklnnGDLVTCSPGCK 264
|
330 340
....*....|....*....|....*..
gi 71991177 2107 EGATGSRCDQCLPSYLRIpTYGCRRCD 2133
Cdd:pfam03302 265 TCTSNTVCTTCMDGYVKT-SDSCTKCD 290
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2278-2691 |
2.08e-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: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEaasadQYPEKAQTVPGKLeeIQKKIQEETEKldkqketfEAQKKRAEELAAyLNSAQQLLKESKSKAD 2357
Cdd:TIGR00606 202 VQEHQMELKYLK-----QYKEKACEIRDQI--TSKEAQLESSR--------EIVKSYENELDP-LKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2358 KSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEMT---HAVTTLNETRNDVAEALEAA 2434
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVdcqRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2435 KKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFsnltdTLKnAKAQIDNAYEALSAEPAFAE 2514
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFH-----TLV-IERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2515 SVQNARDKPfpDETKEKIDALSKTVSQDL----KETEKLK---KQLEQLTELSEKLRKRKEAVK---AGIPKYSKNTLds 2584
Cdd:TIGR00606 420 KERLKQEQA--DEIRDEKKGLGRTIELKKeileKKQEELKfviKELQQLEGSSDRILELDQELRkaeRELSKAEKNSL-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2585 IDEKVQEVEKLKAEiDANIEETRAKISE----------IAGKAEEITEKANSAMEGIR-LARRNSVQLNKLAPVIVSKfE 2653
Cdd:TIGR00606 496 TETLKKEVKSLQNE-KADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKDEQIRkIKSRHSDELTSLLGYFPNK-K 573
|
410 420 430
....*....|....*....|....*....|....*...
gi 71991177 2654 ELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2344-2627 |
2.18e-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: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2344 SAQQLLKESKSKADKSNNiakmlQLTKVENLVAAITDDLErveAAKGEFQKLNVAIGNITENLKDKREEmthavttLNET 2423
Cdd:COG3883 13 FADPQIQAKQKELSELQA-----ELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAE-------IAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2424 RNDVAEALEAAKKRVR---RDEKSVDM--QLVNAKahelhlqattlrqtfdnnkdNTDQAVEAANAFSNLTDtlknAKAQ 2498
Cdd:COG3883 78 EAEIEERREELGERARalyRSGGSVSYldVLLGSE--------------------SFSDFLDRLSALSKIAD----ADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2499 IDNAYEALsaepafaesvqnardkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVkagipkys 2578
Cdd:COG3883 134 LLEELKAD----------------------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL-------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71991177 2579 kntLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSA 2627
Cdd:COG3883 184 ---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2314-2655 |
2.67e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2314 IQEETEKLDKQKETFEAQKKRAEELaaYLNSAQQLLKESKSKADKSNNIAKMLqltkveNLVaaitddlerVEAAKGEFQ 2393
Cdd:PTZ00440 2192 LENTADKLKELYENLKKKKNIINNI--YKKINFIKLQEIENSSEKYNDISKLF------NNV---------VETQKKKLL 2254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2394 KLNVAIGNITENLKDKREEMTHAVTTLN-ETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATT----LRQTF 2468
Cdd:PTZ00440 2255 DNKNKINNIKDKINDKEKELINVDSSFTlESIKTFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENIThllnRINTL 2334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2469 DNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEpaFAESVQNARD----------KPFPDETKEKIDALSKT 2538
Cdd:PTZ00440 2335 INDLDNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKEE--FSKLLKNIKRnntlcnnnniKDFISNIGKSVETIKQR 2412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2539 VSQDLKETEKLKKQLEQLTELSEKLR--KRKEAVKAGIPKYSKN------------TLDSIDEKVQEVEKLKAEIDANIE 2604
Cdd:PTZ00440 2413 FSSNLPEKEKLHQIEENLNEIKNIMNetKRISNVDAFTNKILQDidneknkennnmNAEKIDDLIENVTSHNEKIKSELL 2492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 2605 ET-------RAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEEL 2655
Cdd:PTZ00440 2493 IIndalrrvKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYIINELESHVSKLNEL 2550
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2306-2690 |
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 71991177 2306 KLEEI-QKKIQEETEKLDK------QKETFEAQKKRAEEL-AAYLNSAQQLLKESKSKADKSNNI-AKML------QLTK 2370
Cdd:PRK04778 37 RKQELeNLPVNDELEKVKKlnltgqSEEKFEEWRQKWDEIvTNSLPDIEEQLFEAEELNDKFRFRkAKHEineiesLLDL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2371 VENLVAAITDDL-----------ERVEAAKGEFQKLN-----------VAIGNITENLKDKREEMTHAVTtLNETrNDVA 2428
Cdd:PRK04778 117 IEEDIEQILEELqelleseeknrEEVEQLKDLYRELRksllanrfsfgPALDELEKQLENLEEEFSQFVE-LTES-GDYV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2429 EA---LEAAKKRVRRDEKsvDMQLVNAKAHELhlqATTLRQTFDNNKDNTDQAVEAANAFS--NLTDTLKNAKAQIDNAY 2503
Cdd:PRK04778 195 EAreiLDQLEEELAALEQ--IMEEIPELLKEL---QTELPDQLQELKAGYRELVEEGYHLDhlDIEKEIQDLKEQIDENL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2504 EALSA-EPAFAEsVQNardkpfpDETKEKIDALsktvsQDLKETE-----KLKKQLEQLTELSEKLRKRKEAVKAGIPKY 2577
Cdd:PRK04778 270 ALLEElDLDEAE-EKN-------EEIQERIDQL-----YDILEREvkarkYVEKNSDTLPDFLEHAKEQNKELKEEIDRV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2578 SKN-TLD--------SIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIT----------EKANSAMEGIRL----A 2634
Cdd:PRK04778 337 KQSyTLNeselesvrQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILkqleeiekeqEKLSEMLQGLRKdeleA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991177 2635 RRNSVQL-NKLA-----------PVI----VSKFE----ELKKLSSARSAK---VDSVSDKVSQIKEMIAVARDAANRI 2690
Cdd:PRK04778 417 REKLERYrNKLHeikryleksnlPGLpedyLEMFFevsdEIEALAEELEEKpinMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2307-2692 |
3.19e-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: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAK----------MLQLTKVENLVA 2376
Cdd:pfam10174 132 LFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEaemqlghlevLLDQKEKENIHL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2377 --------AITDDLERVEAAKGEFQKLNVAIGNITENLKDKREE--MTHAVTTLN-ETRNDVAEALEAAKKRVRRDEKSV 2445
Cdd:pfam10174 212 reelhrrnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEvqMLKTNGLLHtEDREEEIKQMEVYKSHSKFMKNKI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2446 DM--QLVNAKAHELHLQATTLrQTFDNNKDNTDQAVEAanafsnLTDTLkNAKAQ----IDNAYEALSAEPAFAESVQNA 2519
Cdd:pfam10174 292 DQlkQELSKKESELLALQTKL-ETLTNQNSDCKQHIEV------LKESL-TAKEQraaiLQTEVDALRLRLEEKESFLNK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2520 RDKPFPDETKEKiDALSKTVSqDLKET------------EKLKKQLEQLTELSEKLRKRKEAVKaGIPKYSKNT---LDS 2584
Cdd:pfam10174 364 KTKQLQDLTEEK-STLAGEIR-DLKDMldvkerkinvlqKKIENLQEQLRDKDKQLAGLKERVK-SLQTDSSNTdtaLTT 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2585 IDEKVQE----VEKLKAEIDaniEETRAKISEIAG--KAEEITEKANSAMEGIRLARRNSV-----QLNKLAPVIVSKFE 2653
Cdd:pfam10174 441 LEEALSEkeriIERLKEQRE---REDRERLEELESlkKENKDLKEKVSALQPELTEKESSLidlkeHASSLASSGLKKDS 517
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71991177 2654 ELKKLSSARSAKVDSVSDKVSQIK---EMIAVAR---DAANRIKL 2692
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKLENQLKkahNAEEAVRtnpEINDRIRL 562
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2179-2678 |
3.20e-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: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2179 DINEITKMLNDEENSFGNvfgDAQDILTNSTQIQNKLVRtKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLA 2258
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQN---EKADLDRKLRKLDQEMEQ-LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2259 -------EIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEEIQKKI------QEETEKLDKQK 2325
Cdd:TIGR00606 567 gyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLK 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2326 ETFEAQKKRAEELAAYLNSAQQLLKESKSKA-------DKSNNIAKMLQ--LTKVENLVAAITDDLERVEAAKGEFQK-- 2394
Cdd:TIGR00606 646 EEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQefISDLQSKLRLAPDKLKSTESELKKKEKrr 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2395 ---LNVA------IGNITENLKDKREEMTHAVTTLNETRNDVAE----------ALEAAK-------------KRVRRDE 2442
Cdd:TIGR00606 726 demLGLApgrqsiIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetllgtimpEEESAKvcltdvtimerfqMELKDVE 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2443 KSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAV--------------EAANAFSNLTDTLKNAKAQIDnayEALSA 2508
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVskielnrkliqdqqEQIQHLKSKTNELKSEKLQIG---TNLQR 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2509 EPAFAE--------------SVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEqLTELSEKLRKRKEAVKagi 2574
Cdd:TIGR00606 883 RQQFEEqlvelstevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-VNDIKEKVKNIHGYMK--- 958
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2575 pkyskntldSIDEKVQE-VEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLAR-RNSVQLNKLAPVIVSkf 2652
Cdd:TIGR00606 959 ---------DIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNLTLRKRE-- 1027
|
570 580
....*....|....*....|....*..
gi 71991177 2653 EELKKLSSARSAKVDSVS-DKVSQIKE 2678
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEMGqMQVLQMKQ 1054
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1937-1980 |
3.22e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 3.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71991177 1937 CQCNGNNNLTDSrsCHPNSGDCyLCEQNTDGRHCESCAAWFYGD 1980
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
297-345 |
3.32e-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: 3.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71991177 297 RCVCNGHA---VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQA 345
Cdd:cd00055 1 PCDCNGHGslsGQCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2446-2625 |
3.75e-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: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2446 DMQLVNAKAHELHLQATTLRQTFdnnKDNTDQAVEAANAfsNLTDTLKNAKAQIDNAYEALSAEpaFAESVQNARDKpfp 2525
Cdd:pfam01442 5 SLDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRE--RLQKDLEEVRAKLEPYLEELQAK--LGQNVEELRQR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2526 deTKEKIDALSKTVSQDLKEtekLKKQLEQLT-ELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQE--------VEKLK 2596
Cdd:pfam01442 75 --LEPYTEELRKRLNADAEE---LQEKLAPYGeELRERLEQNVDALRARLAPYAEELRQKLAERLEElkeslapyAEEVQ 149
|
170 180
....*....|....*....|....*....
gi 71991177 2597 AEIDANIEETRAKiseIAGKAEEITEKAN 2625
Cdd:pfam01442 150 AQLSQRLQELREK---LEPQAEDLREKLD 175
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
809-847 |
4.10e-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: 4.10e-06
10 20 30
....*....|....*....|....*....|....*....
gi 71991177 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 |
4.20e-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: 46.19 E-value: 4.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 71991177 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 ... |
2362-2612 |
4.61e-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: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2362 IAKMLQL----TKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEmthavttlnetRNDVAEALEAAKKR 2437
Cdd:COG1579 6 LRALLDLqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-----------IKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2438 VRRDEKsvdmQLVNAKahelhlqattlrqtfdNNKDntdqaveaanafsnltdtlknakaqidnaYEALSAEPAFAesvq 2517
Cdd:COG1579 75 IKKYEE----QLGNVR----------------NNKE-----------------------------YEALQKEIESL---- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2518 nardkpfpdetKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipkyskntldSIDEKVQEVEKLKA 2597
Cdd:COG1579 102 -----------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------ELDEELAELEAELE 159
|
250
....*....|....*
gi 71991177 2598 EIDANIEETRAKISE 2612
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2249-2691 |
4.75e-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: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2249 RARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAaSADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF 2328
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2329 EAQKKRAEELAAYLNSAQQLLKESKSKADKSN--------NIAKMLQ-LTKVENLVAAITDDLERVEAAKGEFQklnvai 2399
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKreinelkrELDRLQEeLQRLSEELADLNAAIAGIEAKINELE------ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2400 gnitENLKDKREEMTHAVTTLNETRNDVA------EALEAAKKRVRRDEKSVDMQLVNAKAhelhlQATTLRQTFDNNKD 2473
Cdd:TIGR02169 441 ----EEKEDKALEIKKQEWKLEQLAADLSkyeqelYDLKEEYDRVEKELSKLQRELAEAEA-----QARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2474 NTD------------------------QAVEAA--NAFSNL---TDT--------LKNAKA------------------- 2497
Cdd:TIGR02169 512 VEEvlkasiqgvhgtvaqlgsvgeryaTAIEVAagNRLNNVvveDDAvakeaielLKRRKAgratflplnkmrderrdls 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2498 ------QIDNAYEALSAEPAFA-------------ESVQNARD-------------------------------KPFPDE 2527
Cdd:TIGR02169 592 ilsedgVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAARRlmgkyrmvtlegelfeksgamtggsraprggILFSRS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2528 TKEK----------------------------IDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIpkysk 2579
Cdd:TIGR02169 672 EPAElqrlrerleglkrelsslqselrrienrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL----- 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2580 ntlDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEIteKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLS 2659
Cdd:TIGR02169 747 ---SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
570 580 590
....*....|....*....|....*....|..
gi 71991177 2660 SARSAKVDSVSDKVSQIKEMIavaRDAANRIK 2691
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQR---IDLKEQIK 850
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2397-2678 |
5.08e-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: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2397 VAIGNITENLKDKREEMTHAVTTL-NETRNDVAEaLEAAKKRVRRDEKsvDMQLVNAKAHELHLQATTLRQTFDNNKDNT 2475
Cdd:TIGR04523 22 VGYKNIANKQDTEEKQLEKKLKTIkNELKNKEKE-LKNLDKNLNKDEE--KINNSNNKIKILEQQIKDLNDKLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2476 DQAveaaNA-FSNLTDTLKNAKAQIDNayealsaepafaESVQNARDKPFPDETKEKIDalsktvsQDLKETEKLKKQLE 2554
Cdd:TIGR04523 99 NKL----NSdLSKINSEIKNDKEQKNK------------LEVELNKLEKQKKENKKNID-------KFLTEIKKKEKELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2555 QLTELSEKLRKRKEAVKagipKYSKNTLDSIDEKVQEVEKLKAEIDA------NIEETRAKISEIAGKAEEITEKANSAM 2628
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELE----NELNLLEKEKLNIQKNIDKIKNKLLKlelllsNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71991177 2629 EGIRLarrNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKE 2678
Cdd:TIGR04523 232 DNIEK---KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2146-2505 |
5.93e-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: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2146 LELEIDVLGTAIANISSATI-VGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDI---LTNSTQIQNKLVRTKTH 2221
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTsERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNItvrLQDLTEKLSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2222 SQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALA-----IGSSSKAVNVDPRLLKEAEETLMTLEAAsadqy 2296
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqerVREHALSIRVLPKELLASRQLALQKMQS----- 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2297 pEKAQTVPGK--LEEIQKKIQEETEKLDKQKETFE----AQKKRAEELAAYLNSAQQLLKESKSKADksnniakmlqlTK 2370
Cdd:TIGR00618 688 -EKEQLTYWKemLAQCQTLLRELETHIEEYDREFNeienASSSLGSDLAAREDALNQSLKELMHQAR-----------TV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2371 VENLVAAITDDLERVEAAKGEFQKLNVAIGNItENLKDKREEMTHAVTTL----NETRNDVAEALEAAKKRVRRDEKSVD 2446
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEI-QFFNRLREEDTHLLKTLeaeiGQEIPSDEDILNLQCETLVQEEEQFL 834
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71991177 2447 MQLvnAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLkNAKAQIDNAYEA 2505
Cdd:TIGR00618 835 SRL--EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL-NGINQIKIQFDG 890
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2307-2610 |
6.09e-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: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKldKQKETFEAQKKRAEELAAYlNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVE 2386
Cdd:pfam13868 103 MDEIVERIQEEDQA--EAEEKLEKQRQLREEIDEF-NEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2387 AAKgefQKLNVAIGNITENLKDKREEMthavttlNETRNDVAEalEAAKKRVRRDEKsvdmqlvnakahelhlqattlrq 2466
Cdd:pfam13868 180 EEK---EREIARLRAQQEKAQDEKAER-------DELRAKLYQ--EEQERKERQKER----------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2467 tfdnnkdntdQAVEAAnafsnltdtlKNAKAQIDNAYEALSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKET 2546
Cdd:pfam13868 225 ----------EEAEKK----------ARQRQELQQAREEQIELKERRLAEEAEREE---EEFERMLRKQAEDEEIEQEEA 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2547 EKLKKQLEQLTELSEKLRKRKEAVKAgipkyskntlDSIDEKVQEVEKLK---AEIDANIEETRAKI 2610
Cdd:pfam13868 282 EKRRMKRLEHRRELEKQIEEREEQRA----------AEREEELEEGERLReeeAERRERIEEERQKK 338
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2487-2686 |
8.39e-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: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2487 NLTDTLKNAKAQIDNAYEALSaePAfaesvqnardkpfpdeTKEKIDALSKtvsqdlkETEKLKKQLEQ-LTELSEKLRK 2565
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLG--PV----------------AQELVDRLEK-------ETEALRERLQKdLEEVRAKLEP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2566 RKEAVKAGIpkysKNTLDSIDEKVQE-VEKLKAEIDANIEETRAKISEiagKAEEITEKANSAMEGIRlarrnsvqlNKL 2644
Cdd:pfam01442 56 YLEELQAKL----GQNVEELRQRLEPyTEELRKRLNADAEELQEKLAP---YGEELRERLEQNVDALR---------ARL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71991177 2645 APV-------IVSKFEELKKLSSARSAKV-DSVSDKVSQIKEMIAVARDA 2686
Cdd:pfam01442 120 APYaeelrqkLAERLEELKESLAPYAEEVqAQLSQRLQELREKLEPQAED 169
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2200-2573 |
9.31e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2200 DAQDILTNSTQIQNKLVRTKTHSQNSVSSAknITLNGTEFLQEVMKRAQRARQSVRSLAE--IALAIGSSSkavnvdpRL 2277
Cdd:NF041483 903 DANRIRSDAAAQADRLIGEATSEAERLTAE--ARAEAERLRDEARAEAERVRADAAAQAEqlIAEATGEAE-------RL 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLmtleaASADQYPEKAQTVPGKL--------EEIQKKIQEETEK-LDKQKEtfEAQKKRAE--ELAAYLNS-- 2344
Cdd:NF041483 974 RAEAAETV-----GSAQQHAERIRTEAERVkaeaaaeaERLRTEAREEADRtLDEARK--DANKRRSEaaEQADTLITea 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2345 ---AQQLLKESKSKADKSNNIAKMLQLTKV-------ENLVA-AITDDLERVEAAKGEFQKLNV-------AIGNITENL 2406
Cdd:NF041483 1047 aaeADQLTAKAQEEALRTTTEAEAQADTMVgaarkeaERIVAeATVEGNSLVEKARTDADELLVgarrdatAIRERAEEL 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2407 kdkREEMTHAVTTLNE-TRNDVAEALEAAKKRVRRDEKSVDMQLVNA--KAHEL----HLQATTLRQTfdnnkdntdqAV 2479
Cdd:NF041483 1127 ---RDRITGEIEELHErARRESAEQMKSAGERCDALVKAAEEQLAEAeaKAKELvsdaNSEASKVRIA----------AV 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2480 EAANAFsnltdtLKNA---KAQIDNAYEALSAEpAFAESVQNArdkpfpDETKEKIDALSKTvSQDLK-ETEKLKKQLEQ 2555
Cdd:NF041483 1194 KKAEGL------LKEAeqkKAELVREAEKIKAE-AEAEAKRTV------EEGKRELDVLVRR-REDINaEISRVQDVLEA 1259
|
410
....*....|....*....
gi 71991177 2556 LTEL-SEKLRKRKEAVKAG 2573
Cdd:NF041483 1260 LESFeAPSGGGKGNGVKAG 1278
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2307-2679 |
1.07e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKLD---KQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNniakmlqLTKVENLVAAITDDLE 2383
Cdd:PTZ00440 1583 LENLNDKEADYVKYLDnilKEKQLMEAEYKKLNEIYSDVDNIEKELKKHKKNYEIGL-------LEKVIEINKNIKLYMD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEaakgefQKLNVAIGN--------------ITENLKDKREEMTHAVTTLNETRNDVAEALE---------AAKKRVRR 2440
Cdd:PTZ00440 1656 STK------ESLNSLVNNfsslfnnfylnkynINENLEKYKKKLNEIYNEFMESYNIIQEKMKevsnddvdyNEAKTLRE 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2441 DEKSVDMQLVNA-----------KAHELHLQATTLRQTFDN-NKDNTDQAVEAANAFSNLTDTLKNAKAQID--NAYEAL 2506
Cdd:PTZ00440 1730 EAQKEEVNLNNKeeeakkylndiKKQESFRFILYMKEKLDElSKMCKQQYNIVDEGYNYIKKKIEYIKTLNDenNLSDSL 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2507 SAEPAFAESVQNARDKPFPDETK---EKIDALSK----TVSQDLKETE-KLKKQLEQLTELSEKLrkrKEAVKAGIPKYS 2578
Cdd:PTZ00440 1810 NQAEDKNKEVANLTHYTNKNEAKnllGHVVKSANfigiKIMTGLQPTElTPDASLETAPELTFES---ENNSDLELDHLS 1886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2579 KNTLDS-IDEKVQEVEKLKAEIDANIEEtrakISEIAGKAEEITEKANsameGIRLarrNSVQLNKLAPVIVSkfeeLKK 2657
Cdd:PTZ00440 1887 SNKNELdVYKNIQDAYKSSLQILKYSDD----IDKKQRDCNKLVEDGN----EIYL---KSTAINELKNMINS----VKN 1951
|
410 420
....*....|....*....|..
gi 71991177 2658 LSSARSAKVDSVSDKVSQIKEM 2679
Cdd:PTZ00440 1952 KESAISNKIDNVSNKLSELNKI 1973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2146-2605 |
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 71991177 2146 LELEIDVLGTAIANISsativgARLARNKKEFNDINEITKMLNDEENsfgnvfgDAQDILTNSTQIQNKLVRTKTHSQNS 2225
Cdd:COG1196 321 LEEELAELEEELEELE------EELEELEEELEEAEEELEEAEAELA-------EAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2226 VSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASAdqypEKAQTVPG 2305
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----EEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSnniakmlQLTKVENLVAAITDDLERV 2385
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA-------GLRGLAGAVAVLIGVEAAY 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2386 EAAKGEFqkLNVAIGNIT-----------ENLKDKREEmthAVTTLNETRNDVAEALEAAKKRVRRDEK--SVDMQLVNA 2452
Cdd:COG1196 537 EAALEAA--LAAALQNIVveddevaaaaiEYLKAAKAG---RATFLPLDKIRARAALAAALARGAIGAAvdLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2453 KAHELHLQATTLRQTFDNNKDNTDQAV-----------------------EAANAFSNLTDTLKNAKAQIDNAYEALSAE 2509
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRavtlagrlrevtlegeggsaggsLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2510 PAFAESVQNARDkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKV 2589
Cdd:COG1196 692 ELELEEALLAEE-----EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
490 500
....*....|....*....|...
gi 71991177 2590 QEVEKLKAEIDA----N---IEE 2605
Cdd:COG1196 767 RELERLEREIEAlgpvNllaIEE 789
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2527-2622 |
1.27e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2527 ETKEKIDALSKTVSQDLKE-TEKLKKQLEQLTELSEKLRKRKEAVKAgipkySKNTLD----SIDEKVQEVEKLKAEIDA 2601
Cdd:PRK12704 61 EAKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKLELLEK-----REEELEkkekELEQKQQELEKKEEELEE 135
|
90 100
....*....|....*....|..
gi 71991177 2602 NIEETRAKISEIAG-KAEEITE 2622
Cdd:PRK12704 136 LIEEQLQELERISGlTAEEAKE 157
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2312-2690 |
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 71991177 2312 KKIQEETEKLDKQKETFEAQKKRAEelaaYLNSAQQL------LKESKS--KADKSNNIAKMLQLTKVENLvaaitDDLE 2383
Cdd:COG5185 77 KKSESSVKARKFLKEKKLDTKILQE----YVNSLIKLpnyewsADILISllYLYKSEIVALKDELIKVEKL-----DEIA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RVEAAKGEFQKLNVAIGNI--TENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKahELHLQA 2461
Cdd:COG5185 148 DIEASYGEVETGIIKDIFGklTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES--TLLEKA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2462 TTLRQTFDNNKDNTDQAVEAANaFSNLTDTLKNAKAQIDNayeaLSAEPAfaesvqnardkpfpDETKEKidalsktvSQ 2541
Cdd:COG5185 226 KEIINIEEALKGFQDPESELED-LAQTSDKLEKLVEQNTD----LRLEKL--------------GENAES--------SK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2542 DLKE-TEKLKKQLEQLTElseKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANI----------------- 2603
Cdd:COG5185 279 RLNEnANNLIKQFENTKE---KIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIqnltaeieqgqeslten 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2604 -EETRAKISEIAGKA--EEITEKANSAMEGIRLARRN----SVQLNKLAPVIVSKFEELKKLSSARSAKVD-SVSDKVSQ 2675
Cdd:COG5185 356 lEAIKEEIENIVGEVelSKSSEELDSFKDTIESTKESldeiPQNQRGYAQEILATLEDTLKAADRQIEELQrQIEQATSS 435
|
410
....*....|....*
gi 71991177 2676 IKEMIAVARDAANRI 2690
Cdd:COG5185 436 NEEVSKLLNELISEL 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2338-2702 |
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 71991177 2338 LAAYLNSAQQLLKESKSKadKSNNIAKMLQLTKvenlvaaitdDLERVEAAKGEFQKLnvaigniTENLKDKREEMthav 2417
Cdd:COG4717 48 LERLEKEADELFKPQGRK--PELNLKELKELEE----------ELKEAEEKEEEYAEL-------QEELEELEEEL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2418 ttlnetrndvaEALEAAKKRVRRDEKSVDMQLvnaKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKA 2497
Cdd:COG4717 105 -----------EELEAELEELREELEKLEKLL---QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2498 QIDNAYEALSAEpafaesvqnARDKPFPDEtkekidalsKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKY 2577
Cdd:COG4717 171 ELAELQEELEEL---------LEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2578 SKNTLDsiDEKVQEVEKLK---------AEIDANIEETRAKISEIAGKA----------EEITEKANSAMEGIRLARRNS 2638
Cdd:COG4717 233 ENELEA--AALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLflvlgllallFLLLAREKASLGKEAEELQAL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2639 VQLNKLAPVIVSKFEELKKLSSARSAK-VDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSL 2702
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEeLLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2241-2469 |
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 71991177 2241 QEVMKRAQRARQSV----RSLAEIALAIGSsskavnvdprlLKEAEETLMTLEAASADqypekaqtvpgkLEEIQKKIQE 2316
Cdd:PRK02224 561 AEAEEEAEEAREEVaelnSKLAELKERIES-----------LERIRTLLAAIADAEDE------------IERLREKREA 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2317 ETEKLDKQKETFEAQKKRAEELAAYLNSAqqllKESKSKADKSNniakmlqltkVENLVAAITDDLERVEAAKGEFQKLN 2396
Cdd:PRK02224 618 LAELNDERRERLAEKRERKRELEAEFDEA----RIEEAREDKER----------AEEYLEQVEEKLDELREERDDLQAEI 683
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2397 VAIGNITENLKDKREEMTHAVTTLN--ETRNDVAEALEAAKKRVRrdeksVDMQLVNAKAHElhlqaTTLRQTFD 2469
Cdd:PRK02224 684 GAVENELEELEELRERREALENRVEalEALYDEAEELESMYGDLR-----AELRQRNVETLE-----RMLNETFD 748
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2287-2791 |
1.98e-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: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2287 TLEAASADQYPEKAQTvpgKLEEIQKKIQEETEK----LDKQKETFEAQKKRAEElaaylnSAQQLLKESKSKADKSN-N 2361
Cdd:COG3064 4 ALEEKAAEAAAQERLE---QAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEE------EAREAKAEAEQRAAELAaE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2362 IAKmlQLTKVENLVAAITDDLERvEAAKGEfQKLNvaignitENLKDKREEMTHAVTTLNETRndvAEALEAAKKRVRRD 2441
Cdd:COG3064 75 AAK--KLAEAEKAAAEAEKKAAA-EKAKAA-KEAE-------AAAAAEKAAAAAEKEKAEEAK---RKAEEEAKRKAEEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2442 EKSVDMQLVNAKAHELHLQATTLRQTF-DNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNAR 2520
Cdd:COG3064 141 RKAAEAEAAAKAEAEAARAAAAAAAAAaAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2521 DKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEID 2600
Cdd:COG3064 221 VAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2601 ANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMI 2680
Cdd:COG3064 301 AALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2681 AVARDAANRIKLGAHFEKGssldlnipQRVTRSAAHADISFYFRTEQEHGIPLFFGNEETAVGSRAVPTADYVAAEIEYG 2760
Cdd:COG3064 381 ADVEEAAGAGILAAAGGGG--------LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIG 452
|
490 500 510
....*....|....*....|....*....|.
gi 71991177 2761 RpKITVDLGDAPAVVKLDTPVNDGLWRRLNI 2791
Cdd:COG3064 453 K-ALTGDADALLGILKAVALDGGAVLADLLL 482
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3368-3498 |
2.18e-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: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3368 FTFKIRPTSdNGIIFIATNkRTDHIAVMLE-HGR---VVFTYDTGSG--QVIIKSDKSIIDGRWHTIKVSRRGKSAHLIV 3441
Cdd:smart00210 58 TTFRQTPKS-RGVLFAIYD-AQNVRQFGLEvDGRantLLLRYQGVDGkqHTVSFRNLPLADGQWHKLALSVSGSSATLYV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 3442 DDNSYESegaanqnedlIETQPPFYvggVPADLAGFA-RNLVVGVRSQFSGCIKDFKL 3498
Cdd:smart00210 136 DCNEIDS----------RPLDRPGQ---PPIDTDGIEvRGAQAADRKPFQGDLQQLKI 180
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2364-2662 |
2.20e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.62 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2364 KMLQLTKVENLVAAITDDLER------VEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTT-LNET----RNDVAEALE 2432
Cdd:PLN03229 397 RMLKFRKIGGFQEGVPVDPERkvnmkkREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELaLNEMieklKKEIDLEYT 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2433 AAKKRVRRDEKSVDMQLVNAKAH-ELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLT---DTLKNA------------- 2495
Cdd:PLN03229 477 EAVIAMGLQERLENLREEFSKANsQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKyklDMLNEFsrakalsekkska 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2496 ---KAQIDNAYEALSAEPAFAESVQNARDK----------PFPDETKEKIDALSKTVSQDLKETEK---------LKKQL 2553
Cdd:PLN03229 557 eklKAEINKKFKEVMDRPEIKEKMEALKAEvassgassgdELDDDLKEKVEKMKKEIELELAGVLKsmglevigvTKKNK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2554 EQLTELS-EKLRKRKEAVKAGIPKYSKNTLDSIDEKvQEVEKLKAEI-DANIEETRAKISEIAGKAEEITEKANSAMegi 2631
Cdd:PLN03229 637 DTAEQTPpPNLQEKIESLNEEINKKIERVIRSSDLK-SKIELLKLEVaKASKTPDVTEKEKIEALEQQIKQKIAEAL--- 712
|
330 340 350
....*....|....*....|....*....|..
gi 71991177 2632 rlarrNSVQLNklapvivSKFEEL-KKLSSAR 2662
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. |
1937-1983 |
2.54e-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: 43.88 E-value: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71991177 1937 CQCNGNNnlTDSRSCHPNSGDCyLCEQNTDGRHCESCAAWFYGDAVT 1983
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 ... |
2275-2499 |
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 71991177 2275 PRLLKEAeetlmtLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLD-------KQKETFEAQKK---RAEELAAYLNS 2344
Cdd:pfam13166 266 PAERKAA------LEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPavsdlasLLSAFELDVEDiesEAEVLNSQLDG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2345 AQQLLKEskskadKSNNIAKMLQLTKVENLVAAITDDLerveaakgefQKLNVAIGNitenlkdkreemtHavttlNETR 2424
Cdd:pfam13166 340 LRRALEA------KRKDPFKSIELDSVDAKIESINDLV----------ASINELIAK-------------H-----NEIT 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2425 NDVAEALEAAKKRVRRDEKSvdmqlvnakahelhlQATTLRQTFDNNKDNTDQAVEAA-NAFSNLTDTLKNAKAQI 2499
Cdd:pfam13166 386 DNFEEEKNKAKKKLRLHLVE---------------EFKSEIDEYKDKYAGLEKAINSLeKEIKNLEAEIKKLREEI 446
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2516-2623 |
2.72e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2516 VQNARDkpFPDETKEKID-------ALSKTVSQDLKETEKLKKQLEQL-TELSEKLRKRKEavkagipkYSKNTLDSIDE 2587
Cdd:PRK00409 504 IEEAKK--LIGEDKEKLNeliasleELERELEQKAEEAEALLKEAEKLkEELEEKKEKLQE--------EEDKLLEEAEK 573
|
90 100 110
....*....|....*....|....*....|....*....
gi 71991177 2588 KVQE-VEKLKAEIDANIEETRAKISE--IAGKAEEITEK 2623
Cdd:PRK00409 574 EAQQaIKEAKKEADEIIKELRQLQKGgyASVKAHELIEA 612
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2499-2624 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2499 IDNAYEALSAepaFAESVQNARDKPFPDET-----------KEKIDALSKTVSQDLKE-TEKLKKQLEQ----LTELSEK 2562
Cdd:cd13769 7 IQKAQEAINN---LAQQVQKQLGLQNPEEVvntlkeqsdnfANNLQEVSSSLKEEAKKkQGEVEEAWNEfktkLSETVPE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2563 LRKRKEAVKAgipkySKNTLDSIDEKVQ----EVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2624
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 ... |
2306-2640 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKL-DKQKEtFEAQKKRAEEL---AAYLNSAQQLLKESKSKADKSnniakmlqltkVENLVAAIT-D 2380
Cdd:pfam10174 395 KINVLQKKIENLQEQLrDKDKQ-LAGLKERVKSLqtdSSNTDTALTTLEEALSEKERI-----------IERLKEQRErE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2381 DLERVEaakgEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAE-ALEAAKKRVRRD------EKSVD----MQL 2449
Cdd:pfam10174 463 DRERLE----ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKsleiavEQKKEecskLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2450 VNAKAHELHLQATTlRQTFDNNKDNTDQAV-----EAANAFSNL---------TDTLKNAKAQIDNAYEALSAEPAFAES 2515
Cdd:pfam10174 539 QLKKAHNAEEAVRT-NPEINDRIRLLEQEVarykeESGKAQAEVerllgilreVENEKNDKDKKIAELESLTLRQMKEQN 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2516 VQNARDKPFPDETKEKIDALSKTVS--QDLKETEKLKKQLEQLTELSEKLRKRKEAVKAgipKYSkNTLDSIDEKVQEVE 2593
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQLLEEARrrEDNLADNSQQLQLEELMGALEKTRQELDATKA---RLS-STQQSLAEKDGHLT 693
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 71991177 2594 KLKAEIDANIEEtrakISEIAGKA--EEITEK-ANSAMEGIRLARRNSVQ 2640
Cdd:pfam10174 694 NLRAERRKQLEE----ILEMKQEAllAAISEKdANIALLELSSSKKKKTQ 739
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2312-2572 |
3.89e-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: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2312 KKIQEETEKLDKQKEtfeaqkkRAEElaaylnsAQQLLKESKSKADKSnniakmlqltkvENLVAAIT-------DDLER 2384
Cdd:pfam00261 1 KKMQQIKEELDEAEE-------RLKE-------AMKKLEEAEKRAEKA------------EAEVAALNrriqlleEELER 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2385 VEaakgefQKLNVAIGNITENLKdKREEMTHAVTTLnETR----NDVAEALEAAKKRVRRDEKSVDMQLVNAkahELHLQ 2460
Cdd:pfam00261 55 TE------ERLAEALEKLEEAEK-AADESERGRKVL-ENRalkdEEKMEILEAQLKEAKEIAEEADRKYEEV---ARKLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2461 ATT--LRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEalsaepafaesvqnaRDkpfpDETKEKIdalsKT 2538
Cdd:pfam00261 124 VVEgdLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASE---------------RE----DKYEEQI----RF 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71991177 2539 VSQDLKETE-----------KLKKQLEQLTELSEKLRKRKEAVKA 2572
Cdd:pfam00261 181 LTEKLKEAEtraefaersvqKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2300-2407 |
5.44e-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: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2300 AQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSK-ADKSNNIAKMLQlTKVENLVAAI 2378
Cdd:TIGR04320 249 IPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElANAQAQALQTAQ-NNLATAQAAL 327
|
90 100
....*....|....*....|....*....
gi 71991177 2379 TDDLERVEAAKGEFQKLNVAIGNITENLK 2407
Cdd:TIGR04320 328 ANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
2474-2624 |
5.97e-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: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2474 NTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAepaFAESVQnardkpfpDETKEKIDALSKTVSQdlketekLKKQL 2553
Cdd:pfam07464 4 ELQQSVQKQLGLPSQQEVVETIKENTENLVDQLKQ---VQKSLQ--------EELKKASGEAEEALKE-------LNTKI 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991177 2554 EQLTElseKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKA 2624
Cdd:pfam07464 66 VETAD---KLSEANPEVVQKANELQEKFQSGVQSLVTESQKLAKSISENSQGATEKLQKATKQAYDDAVQA 133
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2309-2609 |
6.02e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.18 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2309 EIqKKIQEETEKLDKQKETFEAQKKRAEElaaylnsaQQLLKESKSKADKSNNIAKMlqltkvENLVAAItddLERVEAA 2388
Cdd:PRK05035 437 EI-RAIEQEKKKAEEAKARFEARQARLER--------EKAAREARHKKAAEARAAKD------KDAVAAA---LARVKAK 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2389 KGEFQKLNVAIGNItenLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTF 2468
Cdd:PRK05035 499 KAAATQPIVIKAGA---RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2469 DNNKDntdqAVEAANAfsnltdtlkNAKAQidnayealSAEPAfAESVQNARDKPFPDETKEKIDALSKTVsqdlketeK 2548
Cdd:PRK05035 576 DPKKA----AVAAAIA---------RAKAK--------KAAQQ-AASAEPEEQVAEVDPKKAAVAAAIARA--------K 625
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2549 LKK-QLEQLTELSEKLRKRKEAVKAGIP--KYSKNTLDSIDEKVQE-VEKLKAEIDANIEETRAK 2609
Cdd:PRK05035 626 AKKaEQQANAEPEEPVDPRKAAVAAAIAraKARKAAQQQANAEPEEaEDPKKAAVAAAIARAKAK 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2478-2689 |
8.72e-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: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2478 AVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDkpfpdETKEKIDALSKTVSQDLKETEKLKKQLEQLT 2557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2558 ELSEKLRKRKEAVKA-------GIPKYSKNTL-------DSIDEKVQEVEKLKA---EIDANIEETRAKISEIAGKAEEI 2620
Cdd:COG4942 90 KEIAELRAELEAQKEelaellrALYRLGRQPPlalllspEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2621 TEKANSAMEgirLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQ-------IKEMIAVARDAANR 2689
Cdd:COG4942 170 EAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEaeelealIARLEAEAAAAAER 242
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2308-2568 |
9.71e-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: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2308 EEIQKKIQEETEKLDKQKETFEAQ-KKRAEELAAYLNSAQQLLKESKSKADK--SNNIAKMLQLTKVENLVAAITDDLER 2384
Cdd:pfam15964 370 ERLEKELASQQEKRAQEKEALRKEmKKEREELGATMLALSQNVAQLEAQVEKvtREKNSLVSQLEEAQKQLASQEMDVTK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2385 VeAAKGEFQkLNVAIGNITENLKDKRE--------------EMTHAVTTLNETRNDVAEALEAAKKRvrRDEKSVDMQLV 2450
Cdd:pfam15964 450 V-CGEMRYQ-LNQTKMKKDEAEKEHREyrtktgrqleikdqEIEKLGLELSESKQRLEQAQQDAARA--REECLKLTELL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2451 NAKAHELHL---QATTLRQTFDNNKdnTDQAVEAANAFSNLTDTLKNAKAQIDNA----YEALSAepafaesvQNArdkp 2523
Cdd:pfam15964 526 GESEHQLHLtrlEKESIQQSFSNEA--KAQALQAQQREQELTQKMQQMEAQHDKTvneqYSLLTS--------QNT---- 591
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71991177 2524 FPDETKEKIDALSKT---VSQDLK-ETEKLKKQLEQLTELSEKLRKRKE 2568
Cdd:pfam15964 592 FIAKLKEECCTLAKKleeITQKSRsEVEQLSQEKEYLQDRLEKLQKRNE 640
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2525-2712 |
9.85e-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: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2525 PDETKEKIDALSKTVsQDLKET----EKLKKQLEQLTELSEKLRKRKEA---------VKAGIPKY-------------- 2577
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLERAhealEDAREQIELLEPIRELAERYAAArerlaeleyLRAALRLWfaqrrlelleaele 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2578 -SKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKA-EEITEKANSAMEGIRLARRNSVQLNKLA-------PVI 2648
Cdd:COG4913 299 eLRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLaalglplPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2649 VSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANR--------IklgAHFEKGSSldlNIPQRVTR 2712
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelreleaeI---ASLERRKS---NIPARLLA 444
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2196-2691 |
1.05e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2196 NVFGDAQDILTNSTQI---QNKLVRTKTHSQNSVSSAKNITLNGTEFLQ-EVMKRAQRARQSVrslaeIALAIGSSSKav 2271
Cdd:PTZ00440 1893 DVYKNIQDAYKSSLQIlkySDDIDKKQRDCNKLVEDGNEIYLKSTAINElKNMINSVKNKESA-----ISNKIDNVSN-- 1965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2272 nvdprLLKEAEEtlMTLEAASADQYPEKaqtvpGKLEEIQKK----IQEETE-----KLDKQKETFEAQKKRAEELAAYL 2342
Cdd:PTZ00440 1966 -----KLSELNK--ITCNDESYDEILEK-----EEYEELKDLrnsfNQEKAEtlnnlKLNKIKEDFNSYKNLLDELEKSV 2033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2343 N--SAQQLLKESKSKADKS-NNIAKMLQLTK--VENLVAAITDDLER---VEAAKGEF--QKLNVAIGNITENLKDKREE 2412
Cdd:PTZ00440 2034 KtlKASENIKKIVENKKTSiDAINTNIEDIEkeIESINPSLDELLKKghkIEISRYTSiiDNVQTKISNDSKNINDIEKK 2113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2413 MTHAVTTLNETRNDVAEALEAAKKRVrrDEKSVDMQLVN--AKAHELHLQAT-----------TLRQTFDNNKDNT--DQ 2477
Cdd:PTZ00440 2114 AQIYLAYIKNNYNSIKKDISTLNEYF--DEKQVSNYILTniDKANKLSSELSeavtnseeiieNIKKEIIEINENTemNT 2191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2478 AVEAANAFSNLTDTLKNAKAQIDNAYEALsaepaFAESVQNARdkpfpdETKEKIDALSKTVSQDLkETEKlKKQLEQLT 2557
Cdd:PTZ00440 2192 LENTADKLKELYENLKKKKNIINNIYKKI-----NFIKLQEIE------NSSEKYNDISKLFNNVV-ETQK-KKLLDNKN 2258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2558 ELSEKLRKRKEAVKAGIPKYSKNTLDSIDE----------KVQEVEKL----KAEID------ANIEETRAKISEIAGKA 2617
Cdd:PTZ00440 2259 KINNIKDKINDKEKELINVDSSFTLESIKTfneiyddiksNIGDLYKLedtnNDELKkvklyiENITHLLNRINTLINDL 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2618 EEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLssARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:PTZ00440 2339 DNYQDENYGKDKNIELNNENNSYIIKTKEKINNLKEEFSKL--LKNIKRNNTLCNNNNIKDFISNIGKSVETIK 2410
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
331-648 |
1.23e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 47.66 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 331 CERCCPGF---VQKQWQAATAHNNF-TCEACNCFGRS--NECEYDAEVDLNKQSIDSQ---GNYEGGGVCKN---CRENT 398
Cdd:pfam03302 1 CDECKPGYelsADKTKCTSSAPCKTeNCKACSNDKREvcEECNSNNYLTPTSQCIDDCakiGNYYYTTNANNkkiCKECT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 399 EGvNCNKCsfgyfrpegvtwNEPQPCKVCDCDPDKHTGACAEETGKCECLPRFVGEDCDQCASGyydapkcKPCECNVNG 478
Cdd:pfam03302 81 VA-NCKTC------------EDQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTG-------KALRYGNDG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 479 TIGDvclpEDGQCPCKAGFGGtfCETCA---DGytnvTAGCVECVCDATGSEHGNCSASTGQ----CECKPAYAGLsCDK 551
Cdd:pfam03302 141 TKGT----CGEGCTTGTGAGA--CKTCGltiDG----TSYCSECATETEYPQNGVCTSTAARatatCKASSVANGM-CSS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 552 CQVGYFgddckfcncdpmGTEGGvCDQTT---GQCLCKEGFAGDKCDRCDIAFY--------GYPNCKACAC-------- 612
Cdd:pfam03302 210 CANGYF------------RMNGG-CYETTkfpGKSVCEEANSGGTCQKEAPGYKlnngdlvtCSPGCKTCTSntvcttcm 276
|
330 340 350
....*....|....*....|....*....|....*..
gi 71991177 613 DGAGITSPECDATSGQCP-CNGNFTgrTCDKCAAGFY 648
Cdd:pfam03302 277 DGYVKTSDSCTKCDSSCEtCTGATT--TCKTCATGYY 311
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2290-2563 |
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 71991177 2290 AASADQYPEKAQtVPGKLEEIQK-KIQEETEKLDKQK--------ETFEAQKKRAEELAAYLNSAQQLLKES-------- 2352
Cdd:PRK11281 29 AASNGDLPTEAD-VQAQLDALNKqKLLEAEDKLVQQDleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAqaelealk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2353 KSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLkdkREEMTHAVTTLNETRNDVAeALE 2432
Cdd:PRK11281 108 DDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERA---QAALYANSQRLQQIRNLLK-GGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2433 AAKKRVRRDEKsvdmQLVNAKAHELHLQATTLRQTFDNNkdntdqaveaanafSNLTDTLKN----AKAQIDNayeaLSA 2508
Cdd:PRK11281 184 VGGKALRPSQR----VLLQAEQALLNAQNDLQRKSLEGN--------------TQLQDLLQKqrdyLTARIQR----LEH 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2509 EPAFAESVQNARDKPFPDETKEKidALSKTVSQDLKETEKLKKQLEQLTELSEKL 2563
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; ... |
2278-2475 |
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 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVP---------GKLE----EIQKKIQEETEKLDKQ-KETFEAQKKRAEELAAYLN 2343
Cdd:cd07673 41 IEEAYSRSMTKLAKSASNYSQLGTFAPvwdvfktstEKLAnchlELVRKLQELIKEVQKYgEEQVKSHKKTKEEVAGTLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2344 SAQ--QLLKESKSKAdKSNNIAKMLQLTKvenlvaaitddLERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLN 2421
Cdd:cd07673 121 AVQniQSITQALQKS-KENYNAKCLEQER-----------LKKEGATQREIEKAAVKSKKATESYKLYVEKYALAKADFE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2422 ETRNDVAEALEAAKKRVRRDEKSVDMQLVNAkAHELHLQATTLRQTFDNNKDNT 2475
Cdd:cd07673 189 QKMTETAQKFQDIEETHLIRIKEIIGSYSNS-VKEIHIQIGQVHEEFINNMANT 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2505-2691 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2505 ALSAEPAFAEsvqnardkPFPDETKEKIDALSKTVSQDLKETEKLKKQLEqltELSEKLRKrkeavkagipkysknTLDS 2584
Cdd:COG3883 6 LAAPTPAFAD--------PQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNE---------------LQAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2585 IDEKVQEVEKLKAEID---ANIEETRAKISEIAgkaeeitekansamegiRLARRNSVQLNKLAPVIVSK-FEE------ 2654
Cdd:COG3883 60 LEALQAEIDKLQAEIAeaeAEIEERREELGERA-----------------RALYRSGGSVSYLDVLLGSEsFSDfldrls 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 71991177 2655 -LKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:COG3883 123 aLSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
701-749 |
1.77e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71991177 701 CNCNPSGVTRDfqGCDKVSpGElCSCRKHVTGRICDQCKPTFWDLQYHH 749
Cdd:smart00180 1 CDCDPGGSASG--TCDPDT-GQ-CECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2307-2509 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKLD------KQKETFEAQKKRAEELAAYLNSAQQLLKEskskadksnniakmLQLTKVENLVAAITD 2380
Cdd:COG4913 237 LERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2381 DLERVEAAKGEFQKLnvaigniTENLKDKREEMTHAvttLNETRNDVAEALEA--AKKRVRRDEKSVDMQLVNAKAHELH 2458
Cdd:COG4913 303 ELARLEAELERLEAR-------LDALREELDELEAQ---IRGNGGDRLEQLEReiERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2459 LQATTLRQTFDNNKDNTDQAVEAAN----AFSNLTDTLKNAKAQIDNAYEALSAE 2509
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEeeleALEEALAEAEAALRDLRRELRELEAE 427
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2532-2632 |
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 71991177 2532 IDALSKTVSQDLKETEKLKKQLEQL-TELSEKLRK-RKEAvkAGIpkyskntldsIDEKVQEVEKLKAEIdanIEETRAK 2609
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAAlAEYEEKLAEaRAEA--AEI----------IAEARKEAEAIAEEA---KAEAEAE 93
|
90 100
....*....|....*....|....
gi 71991177 2610 ISEIAGKAE-EITEKANSAMEGIR 2632
Cdd:COG0711 94 AERIIAQAEaEIEQERAKALAELR 117
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2175-2691 |
2.97e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2175 KEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLV--------------------------RTKTHSQNSVSS 2228
Cdd:PTZ00440 1927 EDGNEIYLKSTAINELKNMINSVKNKESAISNKIDNVSNKLSelnkitcndesydeilekeeyeelkdLRNSFNQEKAET 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2229 AKNITLNGT-EFLQEVMKRAQRARQSVRSL---AEIALAIGSSSKAVNVdprLLKEAEETLMTLEA--ASADQYPEKAQT 2302
Cdd:PTZ00440 2007 LNNLKLNKIkEDFNSYKNLLDELEKSVKTLkasENIKKIVENKKTSIDA---INTNIEDIEKEIESinPSLDELLKKGHK 2083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2303 VPGKL-----EEIQKKIQEETEKLDKQK----ETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTkvEN 2373
Cdd:PTZ00440 2084 IEISRytsiiDNVQTKISNDSKNINDIEkkaqIYLAYIKNNYNSIKKDISTLNEYFDEKQVSNYILTNIDKANKLS--SE 2161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2374 LVAAITDDLERVEAAKGEFQKLN-----VAIGNITENLKDKREEMTHAVTTLN------------------ETRNDVAEA 2430
Cdd:PTZ00440 2162 LSEAVTNSEEIIENIKKEIIEINentemNTLENTADKLKELYENLKKKKNIINniykkinfiklqeienssEKYNDISKL 2241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2431 ----LEAAKKRVRRDEKSVD--MQLVNAKAHEL--HLQATTLR--QTFDNNKDNTDQAVEAANAFSNLT-DTLKNAKAQI 2499
Cdd:PTZ00440 2242 fnnvVETQKKKLLDNKNKINniKDKINDKEKELinVDSSFTLEsiKTFNEIYDDIKSNIGDLYKLEDTNnDELKKVKLYI 2321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2500 DNAYEALSAEPAFAESVQNARDKpfpDETKEKIDALSKTVSQDLKETEKLKKQLEQltELSEKLRKRKEAVKAgipKYSK 2579
Cdd:PTZ00440 2322 ENITHLLNRINTLINDLDNYQDE---NYGKDKNIELNNENNSYIIKTKEKINNLKE--EFSKLLKNIKRNNTL---CNNN 2393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2580 NTLDSIDEKVQEVEKLKAEIDANIEEtRAKISEIAGKAEEItekaNSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLS 2659
Cdd:PTZ00440 2394 NIKDFISNIGKSVETIKQRFSSNLPE-KEKLHQIEENLNEI----KNIMNETKRISNVDAFTNKILQDIDNEKNKENNNM 2468
|
570 580 590
....*....|....*....|....*....|....
gi 71991177 2660 SARSAK--VDSVSDKVSQIKEMIAVARDAANRIK 2691
Cdd:PTZ00440 2469 NAEKIDdlIENVTSHNEKIKSELLIINDALRRVK 2502
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2271-2378 |
3.45e-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: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2271 VNVDpRLLKEAEETlmtlEAASAdQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKKRAEELAAYLNSAQQL 2348
Cdd:smart00935 4 VDVQ-KILQESPAG----KAAQK-QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseAAREKKEKELQKKVQEFQRK 77
|
90 100 110
....*....|....*....|....*....|..
gi 71991177 2349 LKESKSKADKSNN--IAKMLQltKVENLVAAI 2378
Cdd:smart00935 78 QQKLQQDLQKRQQeeLQKILD--KINKAIKEV 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2265-2521 |
3.53e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2265 GSSSKAVNVDP--------RLLKEAEEtlmtleAASADQYPEK-AQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRA 2335
Cdd:PRK09510 47 GSVIDAVMVDPgavveqynRQQQQQKS------AKRAEEQRKKkEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2336 EElAAYLNSAQQllKESKSKADKSNNIAKMlqltkvenlvaaitddlerveAAKGEFQKLNVAIGNITENlKDKREEMTH 2415
Cdd:PRK09510 121 EE-AAKQAALKQ--KQAEEAAAKAAAAAKA---------------------KAEAEAKRAAAAAKKAAAE-AKKKAEAEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2416 AVTTLNETRndvAEALEAAKKRVRRDEKSVDMQLVNAKAHELhlqattlrqtfDNNKDNTDQAVEAANAfsnltdtLKNA 2495
Cdd:PRK09510 176 AKKAAAEAK---KKAEAEAAAKAAAEAKKKAEAEAKKKAAAE-----------AKKKAAAEAKAAAAKA-------AAEA 234
|
250 260
....*....|....*....|....*.
gi 71991177 2496 KAQIDNAYEALSAEPAFAESVQNARD 2521
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2150-2671 |
3.54e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2150 IDVLGTAIANISSA-----TIVGARLARNKKEFNDINEITKMLN--DEENSFGNVfgdaqdILTN---STQIQNKLVRTK 2219
Cdd:PTZ00440 2093 IDNVQTKISNDSKNindieKKAQIYLAYIKNNYNSIKKDISTLNeyFDEKQVSNY------ILTNidkANKLSSELSEAV 2166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2220 THSQNSVSSAKNITLNGTE-----FLQEVMKRAQRARQSVR----SLAEIALAIGSSSkavnvdprlLKEAEetlmtlea 2290
Cdd:PTZ00440 2167 TNSEEIIENIKKEIIEINEntemnTLENTADKLKELYENLKkkknIINNIYKKINFIK---------LQEIE-------- 2229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2291 ASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKEtfeaqkKRAEELAAYLNSAQQLLKESKSKADK--SNNIAKMLQL 2368
Cdd:PTZ00440 2230 NSSEKYNDISKLFNNVVETQKKKLLDNKNKINNIKD------KINDKEKELINVDSSFTLESIKTFNEiyDDIKSNIGDL 2303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2369 TKVEnlvaaitddlervEAAKGEFQKLNVAIGNIT------ENLK---DKREEMTHAVTTLNETRNDVAEALEAAKKRVR 2439
Cdd:PTZ00440 2304 YKLE-------------DTNNDELKKVKLYIENIThllnriNTLIndlDNYQDENYGKDKNIELNNENNSYIIKTKEKIN 2370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2440 RDEKSVDMQLVNAKAHELHLQATTLRQTFdnnkDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAepAFAESVQNA 2519
Cdd:PTZ00440 2371 NLKEEFSKLLKNIKRNNTLCNNNNIKDFI----SNIGKSVETIKQRFSSNLPEKEKLHQIEENLNEIKN--IMNETKRIS 2444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2520 RDKPFPDETKEKIDAlSKTVSQDLKETEKLKKQLEQLTELSEKLRKR----KEAVKAGIPKYSK-------------NTL 2582
Cdd:PTZ00440 2445 NVDAFTNKILQDIDN-EKNKENNNMNAEKIDDLIENVTSHNEKIKSElliiNDALRRVKEKKDEmnklfnsltennnNNN 2523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2583 DSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEK----------ANSAMEGIRLAR------RNSVQLNKLAP 2646
Cdd:PTZ00440 2524 NSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENEklkllekakiEESRKERERIESetqednTDEEQINRQQQ 2603
|
570 580
....*....|....*....|....*
gi 71991177 2647 VIVSKFEELKKLSSARSAKVDSVSD 2671
Cdd:PTZ00440 2604 ERLQKEEEQKAYSQERLNREVSGTD 2628
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2273-2483 |
3.81e-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: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2273 VDPRLLKEAEETLMTLEAA-----SADQYPEKAQTVPGKLEEIQKKIqeetEKLDKQKETFEAQKKRAEELAAyLNsaQQ 2347
Cdd:pfam12795 14 AKKKLLQDLQQALSLLDKIdaskqRAAAYQKALDDAPAELRELRQEL----AALQAKAEAAPKEILASLSLEE-LE--QR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2348 LLKESKSKADKSNniakmlQLTKVENLVAAITDDLERVEAAKGEfqkLNVAIGNITENLKDKReemtHAVTTLNETRNDV 2427
Cdd:pfam12795 87 LLQTSAQLQELQN------QLAQLNSQLIELQTRPERAQQQLSE---ARQRLQQIRNRLNGPA----PPGEPLSEAQRWA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71991177 2428 AEALEAAKK--------------------RVRRDeksvdmqLVNAKAHELHLQATTLRQTFDN-NKDNTDQAVEAAN 2483
Cdd:pfam12795 154 LQAELAALKaqidmleqellsnnnrqdllKARRD-------LLTLRIQRLEQQLQALQELLNEkRLQEAEQAVAQTE 223
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2306-2547 |
4.64e-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: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLK---------ESKSKADKSNNiakmlQLTKVENlva 2376
Cdd:pfam15818 223 KFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQqqtqantemEAELKALKENN-----QTLERDN--- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2377 aitdDLERVEAAKGEFQKLNV------AIG---NITENLKDKREEMTHAVTTLNETRNDVAEALE--AAKKRVRRDEKSV 2445
Cdd:pfam15818 295 ----ELQREKVKENEEKFLNLqnehekALGtwkKHVEELNGEINEIKNELSSLKETHIKLQEHYNklCNQKKFEEDKKFQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2446 DMQLVNAKAHELHLQATtlrQTFDNNKDNTDQAVEAANA--FSNLTDTLKNAKAqidnayEALSAEPAFAESVQnardkP 2523
Cdd:pfam15818 371 NVPEVNNENSEMSTEKS---ENLIIQKYNSEQEIREENTksFCSDTEYRETEKK------KGPPVEEIIIEDLQ-----V 436
|
250 260
....*....|....*....|....
gi 71991177 2524 FPDETKEKIDAlskTVSQDLKETE 2547
Cdd:pfam15818 437 LEKSFKNEIDT---SVPQDKNQSE 457
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2238-2609 |
4.90e-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: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2238 EFLQEVMKRAQRARQSV---RSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASAdQYPEKAQTVPGKL--EEIQK 2312
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIeeqETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA-QQAAKLQGSDLDRtvQQVNQ 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2313 KIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKS-KADKSNNIAKMLQL--------TKVENLVAAITDDLE 2383
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeKLQIGTNLQRRQQFeeqlvelsTEVQSLIREIKDAKE 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2384 RV---EAAKGEFQKLNVAIGNI--TEN------LKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNA 2452
Cdd:TIGR00606 910 QDsplETFLEKDQQEKEELISSkeTSNkkaqdkVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2453 KAHELHLQAT--TLRQTFDNNK-------DN-TDQAVEaaNAFSNLTDTLKNAKAQID--------NAYEALSAEPAF-- 2512
Cdd:TIGR00606 990 EKHQEKINEDmrLMRQDIDTQKiqerwlqDNlTLRKRE--NELKEVEEELKQHLKEMGqmqvlqmkQEHQKLEENIDLik 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2513 -AESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEK-LRKRKEAVKAGIPKYSKNTLDSIDEKV- 2589
Cdd:TIGR00606 1068 rNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKdLDIYYKTLDQAIMKFHSMKMEEINKIIr 1147
|
410 420
....*....|....*....|....*....
gi 71991177 2590 ---------QEVEKLKAEIDANiEETRAK 2609
Cdd:TIGR00606 1148 dlwrstyrgQDIEYIEIRSDAD-ENVSAS 1175
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
2452-2676 |
5.32e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2452 AKAHELHLQATTLRQTFDNNKDNTDQAVE---AANAFSNLTDTLKNaKAQIDNAYEALSaEPAFAESVqnardkpfpdET 2528
Cdd:COG5325 8 AQSKGNSVRFTDEYKNQHRKEDDALTPTFilsAASVDQELTAVRRS-ISRLGKVYAKHT-EPSFSDKS----------EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2529 KEKIDALSKTVSQDLKETEKLKKqlEQLTELSEKLRKRKEAVKAGIPK---YSKNTLdSIDEKVQEVEKLKAEIDANI-- 2603
Cdd:COG5325 76 EDEIDELSKKVNQDLQRCEKILK--TKYKNLQSSFLQSKLLRDLNTECmegQRIQQK-SAQFRKYQVLQAKFLRNKNNdq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2604 ----EETRAKISEIAGKAEEITEKANSAMEG---IRLARRNSVQLNKLAPVIV---SKFEELKKLSSARSAKVDSVSDKV 2673
Cdd:COG5325 153 hpleEEEDEESLSSLGSQQTLQQQGLSNEELeyqQILITERDEEIKNLARGIYelnEIFRDLGSLVGEQGELVDRIDFNI 232
|
...
gi 71991177 2674 SQI 2676
Cdd:COG5325 233 ENT 235
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2255-2412 |
5.91e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2255 RSLA-EIALAIGssskavnVDPRLLKEA-----------EETLMTLEAASADQyPEKAQTVPGKLEEIQKKIQEETEKLD 2322
Cdd:PRK00409 487 KSNAfEIAKRLG-------LPENIIEEAkkligedkeklNELIASLEELEREL-EQKAEEAEALLKEAEKLKEELEEKKE 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2323 KQKETFEAQKKRAEElaaylnSAQQLLKESKSKADKSnnIAKMLQLTKVENlvAAITDdlERVEAAKgefQKLNVAIGNI 2402
Cdd:PRK00409 559 KLQEEEDKLLEEAEK------EAQQAIKEAKKEADEI--IKELRQLQKGGY--ASVKA--HELIEAR---KRLNKANEKK 623
|
170
....*....|
gi 71991177 2403 TENLKDKREE 2412
Cdd:PRK00409 624 EKKKKKQKEK 633
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
2518-2662 |
5.97e-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: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2518 NARDKPfpDETKEKIdalsKTVSQDLKETEKLKKQL--------EQLTELSEKLRKRKEAVKAGIPKYSKNtlDSIDEKV 2589
Cdd:pfam12718 11 NAQERA--EELEEKV----KELEQENLEKEQEIKSLthknqqleEEVEKLEEQLKEAKEKAEESEKLKTNN--ENLTRKI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2590 QEVEKLKAEIDANIEETRAKISEIAGKAEEiTEKANSAMEgirlARRNsvQLNKlapvivsKFEEL-KKLSSAR 2662
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 ... |
2530-2629 |
6.27e-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: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2530 EKI-DALSKTVSQdlkeTEKLKKQLEQLTELSEKLRKR-KEAVKAG------IPKYSKNTLDSIDEKVQEVEKLKAeida 2601
Cdd:pfam10368 4 EKIyDHLEEAVEL----EKPFEEQQEPLVELEKKEQELyEEIIELGmdefdeIKKLSDEALENVEEREELLEKEKE---- 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 71991177 2602 NIEETRAKISEIAGKAEEI--------TEKANSAME 2629
Cdd:pfam10368 76 SIEEAKEEFKKIKEIIEEIedeelkkeAEELIDAME 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2248-2634 |
6.82e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2248 QRARQSVRSLAEIALAIgssskAVNVDPR-LLKEAEETLMTLEAASADQYpEKAQTVPGKLEEIQKKIQE---------- 2316
Cdd:PRK04863 813 QRLHQAFSRFIGSHLAV-----AFEADPEaELRQLNRRRVELERALADHE-SQEQQQRSQLEQAKEGLSAlnrllprlnl 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2317 -ETEKLDKQKETFEAQKKRAEELAAYLNSAQQllkeskskadksnniakmlQLTKVENLVAAITDDLERVEAAKGEFQKL 2395
Cdd:PRK04863 887 lADETLADRVEEIREQLDEAEEAKRFVQQHGN-------------------ALAQLEPIVSVLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2396 NVAIGNITEN---LKDKREEMTH-----AVTTLNETrNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHelHLQATTLRQT 2467
Cdd:PRK04863 948 QQTQRDAKQQafaLTEVVQRRAHfsyedAAEMLAKN-SDLNEKLRQRLEQAEQERTRAREQLRQAQAQ--LAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2468 FDNNKDNTDQAV-EAANAFSNLT-----DTLKNAKAQIDNAYEALSAepafaesvqnardkpfpdeTKEKIDALSKTVSQ 2541
Cdd:PRK04863 1025 LKSSYDAKRQMLqELKQELQDLGvpadsGAEERARARRDELHARLSA-------------------NRSRRNQLEKQLTF 1085
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2542 DLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKvqeveKLKAEIDANIEetrakiseiAGKAEEIT 2621
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVER-----RLHRRELAYLS---------ADELRSMS 1151
|
410
....*....|...
gi 71991177 2622 EKANSAMegiRLA 2634
Cdd:PRK04863 1152 DKALGAL---RLA 1161
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
2537-2613 |
7.14e-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: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2537 KTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSknTLDSIDEkvqEVEKLKAEID---ANIEETRAKISEI 2613
Cdd:cd22248 3 QTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKDES--VLRDLEE---EIDSLKANIDyvqENITECQSNIMQM 77
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
2389-2641 |
7.20e-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: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2389 KGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAE-------ALEAAKK-----RVRRDEKSVDMQLVNAKAHE 2456
Cdd:smart00806 84 DDEIDTLQNELDEVKQALESQREAIQRLKERQQNSAANIARpaaspspVLASSSSaislaNNPDKLNKEQRAELKSLQRE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2457 LhlqaTTLRQTFDNNkdntdqaveaanaFSNLTDTLKNAKAQIDNAYEAlsaepafAESVQNARDKPFPDETKEKIDALS 2536
Cdd:smart00806 164 L----AVLRQTHNSF-------------FTEIKESIKDILEKIDKFKSS-------SLSASGSSNRAYVESSKKKLSEDS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2537 KTVS------QDLKETEK----------LKKQLEQLTELSEKLRKR----KEAVKAGIPKYSK---NTLDSIDEKVQEVe 2593
Cdd:smart00806 220 DSLLtkvddlQDIIEALRkdvaqrgvrpSKKQLETVQKELETARKElkkmEEYIDIEKPIWKKiweAELDKVCEEQQFL- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71991177 2594 KLKAEIDANIEETRAKISEIAGKAEEITEKansAMEGIRLARRNSVQL 2641
Cdd:smart00806 299 TLQEDLIADLKEDLEKAEETFDLVEQCCEE---QEKGPSKNRNKPVSL 343
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2272-2408 |
8.45e-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: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2272 NVDPRLLKEAEETLMTL---EAASADQYPEKAQTV--------------PGKLEEIQKKIQE---------ETEKLDK-Q 2324
Cdd:cd22656 106 ATDDEELEEAKKTIKALlddLLKEAKKYQDKAAKVvdkltdfenqtekdQTALETLEKALKDlltdeggaiARKEIKDlQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2325 KETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTK--VENLVAAITDDLERVEAAKGEFQKLNVAIGNI 2402
Cdd:cd22656 186 KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADtdLDNLLALIGPAIPALEKLQGAWQAIATDLDSL 265
|
....*.
gi 71991177 2403 TENLKD 2408
Cdd:cd22656 266 KDLLED 271
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2493-2698 |
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 71991177 2493 KNAKAQIDNAYEALSAEpafAESVQNARDKPFPDETKEKI----DALSKTVSQDLKETEKLKKQL----EQLTELSEKLR 2564
Cdd:cd22656 83 QNAGGTIDSYYAEILEL---IDDLADATDDEELEEAKKTIkallDDLLKEAKKYQDKAAKVVDKLtdfeNQTEKDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2565 KRKEAVKAGIPKYSK-NTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQL-N 2642
Cdd:cd22656 160 TLEKALKDLLTDEGGaIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLlA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2643 KLAPVIVSkFEELKKLSSARSAKVDSVSDKVSQIkemiavARDAANRIKLGAHFEK 2698
Cdd:cd22656 240 LIGPAIPA-LEKLQGAWQAIATDLDSLKDLLEDD------ISKIPAAILAKLELEK 288
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
2252-2500 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2252 QSVRSLAEIALAIGSSSKAVNvdprllKEAEETLMTLE--AASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFE 2329
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELA------ERMEELSASIEevAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2330 AQKKRAEELAAYLNSAQQLLKESKSKADKSNniakMLQLtkveNlvAAItddlervEAA------KG------EFQKL-- 2395
Cdd:smart00283 78 EAVSAVEELEESSDEIGEIVSVIDDIADQTN----LLAL----N--AAI-------EAArageagRGfavvadEVRKLae 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2396 NVA---------IGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDM-QLVNAKAHElhlQATTLR 2465
Cdd:smart00283 141 RSAesakeieslIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLvQEIAAATDE---QAAGSE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71991177 2466 Q---TFDN----NKDNTDQAVEAANAFSNLTDTLKNAKAQID 2500
Cdd:smart00283 218 EvnaAIDEiaqvTQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
2278-2436 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVP----GKLEEIQKKI---QEETEKLDKQKETFEAQKKRA----EELAAYLNSAQ 2346
Cdd:pfam15294 95 IAEFEEREFTSSNKKPNFELNKPKLEPlnegGGSALLHMEIerlKEENEKLKERLKTLESQATQAldekSKLEKALKDLQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2347 QLLKESKSKADKSNNIAKMlqltkvENLVAAITDDLErveaakgefQKLNvaigNITENLKDKREEMThavttlnETRND 2426
Cdd:pfam15294 175 KEQGAKKDVKSNLKEISDL------EEKMAALKSDLE---------KTLN----ASTALQKSLEEDLA-------STKHE 228
|
170
....*....|...
gi 71991177 2427 ---VAEALEAAKK 2436
Cdd:pfam15294 229 llkVQEQLEMAEK 241
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
298-344 |
1.67e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71991177 298 CVCN--GHA-VTCDilepqrPKSLLCRCEHNTCGDMCERCCPGFVQKQWQ 344
Cdd:smart00180 1 CDCDpgGSAsGTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2579-2676 |
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 71991177 2579 KNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKA-EEITEKANSAMEGIR--LARRNSVQLNKLApvivSKFEEL 2655
Cdd:PRK08476 44 KNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKAiAKAKEEAEKKIEAKKaeLESKYEAFAKQLA----NQKQEL 119
|
90 100
....*....|....*....|..
gi 71991177 2656 K-KLSSARSAKVDSVSDKVSQI 2676
Cdd:PRK08476 120 KeQLLSQMPEFKEALNAKLSKI 141
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2526-2675 |
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 71991177 2526 DETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRK-------EAVKAGIPKYSKNtLDSI-DEKvqEVEKLKA 2597
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrleleiEEVEARIKKYEEQ-LGNVrNNK--EYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2598 EIDAN---IEETRAKISEIAGKAEEITEKANSAMEgiRLARRNSvQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVS 2674
Cdd:COG1579 97 EIESLkrrISDLEDEILELMERIEELEEELAELEA--ELAELEA-ELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 71991177 2675 Q 2675
Cdd:COG1579 174 P 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2527-2686 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2527 ETKEKIDALSKTVSqdLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNtLDSIDEKVQEVEKLKAEIDANIEET 2606
Cdd:TIGR02168 217 ELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2607 RAKISEIAGKAEEITEKANSAMEGIrlaRRNSVQLNKLApvivSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDA 2686
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, ... |
2347-2444 |
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 71991177 2347 QLLKESKSKAD----KSNNIAKMLQLTKvENLVAAITDdlerVEAAKGEFQKLNVAIGNITENLKDkreeMTHAVTTLNE 2422
Cdd:pfam10473 10 EKLKESERKADslkdKVENLERELEMSE-ENQELAILE----AENSKAEVETLKAEIEEMAQNLRD----LELDLVTLRS 80
|
90 100
....*....|....*....|..
gi 71991177 2423 TRNDVAEALEAAKKRVRRDEKS 2444
Cdd:pfam10473 81 EKENLTKELQKKQERVSELESL 102
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2306-2440 |
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 71991177 2306 KLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKsnNIAKmlQLTKVENlVAAITddlerV 2385
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE--LIEE--QLQELER-ISGLT-----A 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2386 EAAKGEfqklnvaignITENLKDK-REEMTHAVttlnetRNDVAEALEAAKKRVRR 2440
Cdd:PRK12704 153 EEAKEI----------LLEKVEEEaRHEAAVLI------KEIEEEAKEEADKKAKE 192
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2307-2457 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKLDKQKEtfEAQKKRAEelaaylnsAQQLLKESKSKAdksnniAKMLQLTK--VENLVAAITDDLER 2384
Cdd:COG0711 29 LDERQEKIADGLAEAERAKE--EAEAALAE--------YEEKLAEARAEA------AEIIAEARkeAEAIAEEAKAEAEA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991177 2385 vEAAKgefqklnvaignITENLKDKREEMTHAVttLNETRNDVAE-ALEAAKKRVRR--DEKSVDmQLVNAKAHEL 2457
Cdd:COG0711 93 -EAER------------IIAQAEAEIEQERAKA--LAELRAEVADlAVAIAEKILGKelDAAAQA-ALVDRFIAEL 152
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
2933-3027 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2933 GLLFFVGKDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGeteVLEGDVPGKDSE 3012
Cdd:pfam13385 35 RAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRLYVNG---VLVGSSTLTGGP 111
|
90
....*....|....*.
gi 71991177 3013 MSVTEF-LYIGGTPSG 3027
Cdd:pfam13385 112 PPGTGGpLYIGRSPGG 127
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
2543-2632 |
4.95e-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: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2543 LKETEKLKKQLEQLTELSEKLRKRKEAVkagipkyskntldsidekVQEVEKLKAEIDANIEETRA----KISEIAGKAE 2618
Cdd:cd21759 71 LRKIRALEKQLKEMEEIASQLKKDKDKW------------------TKQVKELKKEIDALIKKIKTndmiTRKEIDKLYN 132
|
90
....*....|....
gi 71991177 2619 EITEKANSAMEGIR 2632
Cdd:cd21759 133 ALVKKVDKQLAELQ 146
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2367-2522 |
5.11e-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: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2367 QLTKVENLVAAITDDL-----ERVEAAKGEFQKlnvAIGNITENLKDKREEMTHAVT-TLNETRNDVAEALEAAKKRVRR 2440
Cdd:pfam01442 12 YAEELQEQLGPVAQELvdrleKETEALRERLQK---DLEEVRAKLEPYLEELQAKLGqNVEELRQRLEPYTEELRKRLNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2441 DEKSVdMQLVNAKAHELHLQA----TTLRQTF----DNNKDNTDQAVEAANAfsNLTDTLKNAKAQIDNAYEALSAepAF 2512
Cdd:pfam01442 89 DAEEL-QEKLAPYGEELRERLeqnvDALRARLapyaEELRQKLAERLEELKE--SLAPYAEEVQAQLSQRLQELRE--KL 163
|
170
....*....|
gi 71991177 2513 AESVQNARDK 2522
Cdd:pfam01442 164 EPQAEDLREK 173
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2278-2435 |
5.40e-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: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2278 LKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETF--EAQKK---RAEELAAYLNSAQQLLKES 2352
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYleELQAKlgqNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2353 KSKAdksnniAKMLQlTKVENLVAAITDDLER-VEAAKGEF--------QKLNVAIGNITENLKDKREEM-THAVTTLNE 2422
Cdd:pfam01442 86 LNAD------AEELQ-EKLAPYGEELRERLEQnVDALRARLapyaeelrQKLAERLEELKESLAPYAEEVqAQLSQRLQE 158
|
170
....*....|...
gi 71991177 2423 TRNDVAEALEAAK 2435
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. ... |
2544-2605 |
5.51e-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: 5.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991177 2544 KETEKLKKQLEQLTELSEKLRKRKEAVKAgipKYSKNTLDSIDEKVQEVEKLKAEIDANIEE 2605
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 ... |
3499-3623 |
5.73e-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: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 3499 NGKSLDNGKEFGTEQCSQFS-EPGM----YFGKDGGYAIVQKDYEvglTFGLEVEMR--PRMKNGILF----SVGVLEYI 3567
Cdd:pfam06439 7 NGKDLDGWKGAGGGGVGGWKvEDGVlvdgSSGKGGGFLITKKKFG---DFELHLEFKitPGGNSGVFFrsqpEEGQDFVK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 71991177 3568 TVEF-VNGSIKTTVESGSGGEELWHHPDIENQYC-DGQWQSFKISKKRNLLTVAVNGK 3623
Cdd:pfam06439 84 GYEVqILDSGGDLGLNRGTGSLYGEIAPSANATFpPGEWNTYEIIVKGNRITVWLNGV 141
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
2529-2626 |
5.96e-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: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2529 KEKIDALSK---TVSQDLKETEKLKKQLEQLTELSEKlrkrKEA---------VKAGIPKYSKNTLD---------SIDE 2587
Cdd:cd23160 13 EQQAEALQQqieLLQASINELNRAKETLEELKKLKEG----TEIlvpigggsfVKAKIKDTDKVLVNigagvvvekTIDE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 71991177 2588 KVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANS 2626
Cdd:cd23160 89 AIEILEKRIKELEKALEKLQEQLQQIAQRLEELEAELQE 127
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
2525-2632 |
6.83e-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: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2525 PDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVkagipkysKNTL---DSIDEKVQEVEKLKAEIda 2601
Cdd:pfam05103 20 PDEVDEFLDQVAEDYEALIRENAELKEKIEELEEKLAHYKNLEETL--------QNTLilaQETAEEVKANAQKEAEL-- 89
|
90 100 110
....*....|....*....|....*....|.
gi 71991177 2602 NIEETRAKISEIAGKAEEITEKANSAMEGIR 2632
Cdd:pfam05103 90 IIKEAEAKAERIVDDANNEVKKINDEIEELK 120
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2541-2691 |
7.10e-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: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2541 QDL-KETEKLKKQLEQLTELSEKLRKRKEAVKAgipkysknTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEE 2619
Cdd:COG1579 13 QELdSELDRLEHRLKELPAELAELEDELAALEA--------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991177 2620 I-TEKANSAMEG-IRLARRNSVQLNKlapVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIK 2691
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 ... |
2307-2439 |
7.68e-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: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2307 LEEIQKKIQEETEKLDKQKEtfEAQKKRAEelaaylnsAQQLLKESKSKADKSNNIAKmlqlTKVENLVAAItddlerVE 2386
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKE--EAEELLAE--------YEEKLAEARAEAQEIIEEAR----KEAEKIKEEI------LA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 71991177 2387 AAKGEFQKLnvaignitenLKDKREEMTHAVT-TLNETRNDVAE-ALEAAKKRVR 2439
Cdd:cd06503 88 EAKEEAERI----------LEQAKAEIEQEKEkALAELRKEVADlAVEAAEKILG 132
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
2604-2688 |
7.94e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991177 2604 EETRAKISEiagKAEEITEKANSAMEGIRLarrnsvQLNKLAPVIVSKFEELKK-LSSARSAKVDSVSDKVSQIKEMIAV 2682
Cdd:COG4980 30 KETRKKLKD---KADDLKDKAEDLKDELKE------KASELSEEAKEKLDELIEeIKEKIEELKEEVEPKIEELKEEAEK 100
|
....*.
gi 71991177 2683 ARDAAN 2688
Cdd:COG4980 101 LQKEVE 106
|
|
| |
