|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
30-280 |
4.58e-93 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 301.97 E-value: 4.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 30 QQRGLFPAVLNLASNAIITANATCGENGPEMFCKLVEHVhgqpVRHSQCRTCDQNSPDKNlhYPIAHAING----KRTWW 105
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARNPRRS--HPAENLTDGnnpnNPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 106 QSPSIKNGVQYhyVTITLDLQQVFQIAYVIIKAAnSPRPGNWILERSLDGISYKPWQYHAitnSECLTRYNIIPRPGIPL 185
Cdd:smart00136 77 QSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 186 YtKDDEVICTSHYSKIHPLENGEIHTSLINGRPSAEDP--SPTLLEFTSARFIRLRLQKIRTLNADLMmlaysdpqDLDP 263
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 2019522063 264 IVTRRYFYSIKDISVGG 280
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
34-280 |
1.76e-83 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 274.07 E-value: 1.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 34 LFPAVLNLASNAIITANATCGENGPEMFCKLVEhvhgqPVRHSQCRTCDqnSPDKNLHYPIAHAI----NGKRTWWQSPS 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSG-----LEGGKKCFICD--SRDPHNSHPPSNLTdsnnGTNETWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 110 IKngVQYHYVTITLDLQQVFQIAYVIIKAAnSPRPGNWILERSLD-GISYKPWQYHAitnSECLTRYNIIPRPgiPLYTK 188
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSGP--SRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 189 DDEVICTSHYSKIHPLENGEIHTSLINGRPSAE--DPSPTLLEFTSARFIRLRLQKIRTLNadlmmlaysDPQDLDPIVT 266
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 2019522063 267 RRYFYSIKDISVGG 280
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1584-1843 |
1.09e-63 |
|
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: 218.44 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1584 VMSVN-LSGPLPPPYRMLFSIENETQELKHLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERT 1662
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQLKNFVKDILQTSKDIYDKAVKLNETlgiQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGLL 1742
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1743 NRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGHKQAVEKGKKETENT 1822
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 2019522063 1823 LNESDDIMTEVNNLAQNINEA 1843
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1369 |
6.43e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 159.74 E-value: 6.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1230 YWKLPEQFEGRKLTAYGGKLKYTIYFEAREETGPSAYEPQVVIRGGpasNHRIIVR--NVPDPQNGQLTRHDIEMTEFEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSspDQPPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1308 KHIDGGSVSREDFMDVLFDIQYILIKASYGRVLRQTRISEVFLEVAEEGTSftmSPKASRIE 1369
Cdd:pfam00052 78 RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1355 |
6.01e-42 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 150.87 E-value: 6.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1225 HSEPFYWKLPEQFEGRKLTAYGGKLKYTIYFEAREEtGPSAYEPQVVIRGGpasNHRIIVRNVPDPQNGQLTRHDIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 1305 FEWKHIDGGSVSREDFMDVLFDIQYILIKASYGRVLRQTRISEVFLEVAEE 1355
Cdd:smart00281 77 ENWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2028-2160 |
9.79e-42 |
|
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: 150.71 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2028 AKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVKVDN--VTDAGERVKLLEKEADRLLDKLKPIKE 2105
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANkaLDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 2106 LQDN---LGKNISQIKELINQARKQANSIKVSVSSGGDCIRTYKPDIKKGRYNTIILN 2160
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
2.31e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.95 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 579 YWSAPASYLHSKVAAVGGHLTYTISYDTSvkDEAEEFTDHSSIIIEGNGIWISTSQYEAD-LHPFEERTVNVVLHPEYFK 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPL--PGGGSLNSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 658 mHSTGYQVSREDFMTVMANVKRLLIRATYSNQPDAIyRLSSVNLEVAEEsSSSGRTAYDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVP-GGSGPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2794-2912 |
7.14e-37 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 136.68 E-value: 7.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2794 RTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMVPQRVNDGEWHKINIFRTKQTGYLFVDGIANST-NS 2872
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2019522063 2873 PKKADI-LDVVGMLYVGGLPVNYTTKRIGPVLHSIDGCIRN 2912
Cdd:pfam00054 82 PLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRD 122
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2941-3093 |
3.21e-35 |
|
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: 132.54 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2941 GTYFDGSGFAKTVGAFKVGTDLLIELEFRTTKTNGVLIGISGK-KMDGLGIEMVDGKLLFHADNGAGRftAVYEPEVPgs 3019
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGS--LVLSSKTP-- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 3020 LCDGQWHKVTANKIKHRLEMIVDNKKVEASSPNAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2766-2915 |
1.14e-34 |
|
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: 131.00 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2766 FGLSKNSHMAFAFDDTKvKNTLSIELELRTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMVPQRVNDG 2845
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 2846 EWHKINIFRTKQTGYLFVDGIA-NSTNSPKKADILDVVGMLYVGGLPVNYTTKRIgPVLHSIDGCIRNFRM 2915
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2354-2495 |
1.08e-33 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 127.43 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2354 FKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKNYNDGKWKSFTLSRIQKQANFSIVDmdtnEEE 2433
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG----EAR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2434 IVATTSTGSNFGLNLksDEKIYFGGLPGLsslspSVKARPEVNLKKYAGCLKDIEVSRTPYN 2495
Cdd:pfam00054 77 PTGESPLGATTDLDV--DGPLYVGGLPSL-----GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
579-706 |
3.29e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 125.84 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 579 YWSAPASYLHSKVAAVGGHLTYTISYDTSVKDEaeeftdHSS---IIIEGNGIWISTsQYEADLHPFEERTVNVVLHPEY 655
Cdd:smart00281 6 YWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT------HVSapdVILEGNGLRISH-PAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 656 FKMHStGYQVSREDFMTVMANVKRLLIRATYSNQPDAIYrLSSVNLEVAEE 706
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2915 |
1.88e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 123.99 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2788 SIELELRTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMV-PQRVNDGEWHKINIFRTKQTGYLFVDGI 2866
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2867 ANSTN-SPKKADILDVVGMLYVGGLPVNYTTKRIgPVLHSIDGCIRNFRM 2915
Cdd:smart00282 81 NRVSGeSPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2326-2489 |
1.31e-31 |
|
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: 122.14 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2326 TVQFDGDGYALVNRPvRWNPNISTIMFKFKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKNYND 2405
Cdd:cd00110 1 GVSFSGSSYVRLPTL-PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2406 GKWKSFTLSRIQKQANFSIvdmdtNEEEIVATTSTGSNFGLNLksDEKIYFGGLPglsslsPSVKARPEVNLKKYAGCLK 2485
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLP------EDLKSPGLPVSPGFVGCIR 146
|
....
gi 2019522063 2486 DIEV 2489
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2964-3093 |
1.40e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 121.68 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2964 IELEFRTTKTNGVLIGISGK-KMDGLGIEMVDGKLLFHADNGAGRFTAVYEPevpGSLCDGQWHKVTANKIKHRLEMIVD 3042
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 3043 NK-KVEASSPnAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:smart00282 79 GGnRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
smart00282 |
Laminin G domain; |
2349-2491 |
2.35e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.43 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2349 TIMFKFKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKN-YNDGKWKSFTLSRIQKQANFSIvdm 2427
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 2428 dtNEEEIVATTSTGSNFGLNLksDEKIYFGGLPglsslsPSVKARPEVNLKKYAGCLKDIEVSR 2491
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLP------EDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2968-3093 |
8.04e-27 |
|
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: 107.51 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2968 FRTTKTNGVLIGISGKKMDGLGIEMVDGKLLFHADNGAGRFTAVYEPEvpgSLCDGQWHKVTANKIKHRLEMIVDNKKVE 3047
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK---NLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2019522063 3048 ASSPNAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2161-2300 |
1.02e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 107.40 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2161 VKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLdINDDSWYRVEASRSGINGTISVqafDGpKA 2240
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV---DG-EA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2241 SIVpsiysSTSQPGYTI-LDVDGhELFVGGLTGKI-KKADAVKVTTFTGCMGETFFDGKPIG 2300
Cdd:pfam00054 76 RPT-----GESPLGATTdLDVDG-PLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2156-2297 |
1.45e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.04 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2156 TIILNVKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLDINDDSWYRVEASRSGINGTISVqaf 2235
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2236 DGPKASivpsiySSTSQPGYTILDVDGhELFVGGLTGKIKKADAVKVTTFTGCMGETFFDGK 2297
Cdd:smart00282 78 DGGNRV------SGESPGGLTILNLDG-PLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2137-2295 |
5.00e-26 |
|
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: 106.35 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2137 SGGDCIRtYKPDIKKGRYNTIILNVKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLdINDDSW 2216
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 2217 YRVEASRSGINGTISVqafDGPKasivpsIYSSTSQPGYTILDVDGhELFVGGLTGKIKKADAVKVTTFTGCMGETFFD 2295
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDG-PLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2516-2677 |
7.01e-26 |
|
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: 105.96 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2516 SVSFSKPGYIEVP-PVSMDVGTEITLSFSTKNESGMILFGNGgslisprrkrrQSGQAFYAVLLRKGKLEVAVSGSKEPh 2594
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2595 qIIIRPeKKKFHDGKEHSIRIERSRNILTAQVDEDR--NQTLKLPASYSISVKKLFVGGIPSDVQFPHYKSIPPFEGCIW 2672
Cdd:cd00110 69 -LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIR 146
|
....*
gi 2019522063 2673 DLLIN 2677
Cdd:cd00110 147 DLKVN 151
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1637-2151 |
4.97e-23 |
|
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: 107.80 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1637 EIDELLNRAAKVSADGEQTGKDAERTNERAKQLKN----FVKDIL---QTSKDIYDKAVKLNETLGI------------- 1696
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENelnlLEKEKLniqKNIDKIKNKLLKLELLLSNlkkkiqknksles 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1697 -------QNKTLEKSLQELQKDVDKMMAELRRRM------------FKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTN 1757
Cdd:TIGR04523 219 qiselkkQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1758 DLN--------LEVKDKLRHFQDKLEDVLDMLREARGKI-----------RESNHLSAINKHNMTALEGHKQAVEKGKKE 1818
Cdd:TIGR04523 299 DLNnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1819 TENTLNESDDIMTEVNNLAQNINEAENElmdiNKELPQLTERLNVKINNLTDEIQtrDLPEQVLQAElhaaqltessrml 1898
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL----NQQKDEQIKKLQQEKELLEKEIE--RLKETIIKNN------------- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1899 dgilAEAKNLSLNATAAFNAYSNIKKLIDNaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLD 1978
Cdd:TIGR04523 440 ----SEIKDLTNQDSVKELIIKNLDNTRES-------------------------LETQLKVLSRSINKIKQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1979 LKEKENELAAMKDKLQNADEKNVNLVR---ALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTAN-DVLARIKD-LNLNL 2053
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKkisSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkENLEKEIDeKNKEI 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2054 LGLKQNYSALK-------EDVAK------------TNAVVKVDNVTDageRVKLLEKEADRLLDKLKPIKELQDNLGKNI 2114
Cdd:TIGR04523 571 EELKQTQKSLKkkqeekqELIDQkekekkdlikeiEEKEKKISSLEK---ELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2115 SQIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPDIKK 2151
Cdd:TIGR04523 648 KQIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| LamG |
smart00282 |
Laminin G domain; |
2537-2677 |
2.92e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.02 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2537 EITLSFSTKNESGMILFgNGGSLisprrkrrqsGQAFYAVLLRKGKLEVAVSGSKEPhqIIIRPEKKKFHDGKEHSIRIE 2616
Cdd:smart00282 1 SISFSFRTTSPNGLLLY-AGSKG----------GGDYLALELRDGRLVLRYDLGSGP--ARLTSDPTPLNDGQWHRVAVE 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 2617 RSRNILTAQVDEDRNQTLKLPASYSI--SVKKLFVGGIPSDVQFPHYKSIPPFEGCIWDLLIN 2677
Cdd:smart00282 68 RNGRSVTLSVDGGNRVSGESPGGLTIlnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2542-2682 |
6.23e-20 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 88.14 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2542 FSTKNESGMILFGNggslisprrkrRQSGQAFYAVLLRKGKLEVAVSGSKepHQIIIRPeKKKFHDGKEHSIRIERSRNI 2621
Cdd:pfam00054 1 FRTTEPSGLLLYNG-----------TQTERDFLALELRDGRLEVSYDLGS--GAAVVRS-GDKLNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 2622 LTAQVDEDRNQTLKLPASYSISVK---KLFVGGIPSDVQFPHYKSI-PPFEGCIWDLLINAVPTD 2682
Cdd:pfam00054 67 GTLSVDGEARPTGESPLGATTDLDvdgPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVNGKPLD 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
4.70e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 4.70e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 963 CNCNSFGSKSFDCD-DKGQCHCQPGVAGDKCDRCAHGFFDFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
8.41e-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: 65.07 E-value: 8.41e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1102 CDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLHIGNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
3.13e-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: 63.53 E-value: 3.13e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 913 SCNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYG-PVSAQGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGlPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
1.03e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 1.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2019522063 914 CNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYGpVSAQGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1008 |
1.03e-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: 1.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 962 ACNCNSFGSKSFDCDDK-GQCHCQPGVAGDKCDRCAHGFFDF--QEGGCT 1008
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1603-2132 |
1.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1603 IENETQELKHLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKD 1682
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1683 IydkavklnETLGIQNKTLEKSLQELQKDVdKMMAELRRRMFKNQEKAAA------------DELKAAEGLLNRVKKLFQ 1750
Cdd:PRK03918 254 K--------RKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEyiklsefyeeylDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1751 DPHNKTNDLNlEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAInkhnMTALEGHKQ-----AVEKGKKETENTLNE 1825
Cdd:PRK03918 325 GIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAK----KEELERLKKrltglTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1826 SDDIMTEVNNLAQNINEAENELMDINK---EL-------P----QLTE--RLNV------KINNLTDEIQTRDLPEQVLQ 1883
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKaieELkkakgkcPvcgrELTEehRKELleeytaELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1884 AELhaaqltessRMLDGILAEAKNLSLNATAAfnaySNIKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDKAKSfiq 1963
Cdd:PRK03918 480 KEL---------RELEKVLKKESELIKLKELA----EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1964 ksfrVHTDAKtqslDLKEKENELAAMKDKLQNADEKNVNL-----------VRALNDTLGKLSAIPNDTIV--------- 2023
Cdd:PRK03918 544 ----LKKELE----KLEELKKKLAELEKKLDELEEELAELlkeleelgfesVEELEERLKELEPFYNEYLElkdaekele 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2024 ----KIQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYS------ALKEDVAKTNAVVKVDnvtdagERVKLLEK-- 2091
Cdd:PRK03918 616 reekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeeLREEYLELSRELAGLR------AELEELEKrr 689
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2092 -EADRLLDKLKP--------IKELQdNLGKNISQIKELINQARKQANSIK 2132
Cdd:PRK03918 690 eEIKKTLEKLKEeleerekaKKELE-KLEKALERVEELREKVKKYKALLK 738
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
1.82e-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: 61.22 E-value: 1.82e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 963 CNCNSFGSKSFDCDDK-GQCHCQPGVAGDKCDRCAHGFFDFQEGGCTPC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1411-1457 |
2.92e-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: 60.44 E-value: 2.92e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1411 CQCNGH---SDMCDPQTSVCQaCKHNTTGDHCEWCAPGFYGTVRGFPDDC 1457
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
3.82e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1009 PCDCPHVG---NNCEAETGQCVCPPNTVGEQCDKCAPNHWGYSIIT-GCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
5.92e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 5.92e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2019522063 1010 CDCP---HVGNNCEAETGQCVCPPNTVGEQCDKCAPNHWGYS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
7.60e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 7.60e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 914 CNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYG--PVSAQGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1049 |
1.91e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2019522063 1010 CDCPHVG---NNCEAETGQCVCPPNTVGEQCDKCAPNHWGYSI 1049
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1410-1458 |
2.05e-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: 2.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1410 PCQCNGHSDM---CDPQTSVCQaCKHNTTGDHCEWCAPGFYGtVRGFPDDCR 1458
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
2.31e-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: 2.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 860 PCQCNDNLDLSAPgcCDSETGECRiCKPGVTGEYCNTCSEGYFGNALGPSSCQ 912
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-797 |
7.76e-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: 7.76e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 752 PCRCFGH---SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTDGTD 797
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1663-2104 |
1.33e-09 |
|
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: 63.82 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEG-- 1740
Cdd:COG5185 116 ADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISel 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1741 LLNRVKKLFQDPHNKTnDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINkhnmtalEGHKQAVEKgkketE 1820
Cdd:COG5185 196 KKAEPSGTVNSIKESE-TGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-------DKLEKLVEQ-----N 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1821 NTLneSDDIMTEVNNLAQNINEAENELMdinKELPQLTERLNVKINNLTDEIQTRDLPEQVLQAELHaAQLTESSRMLD- 1899
Cdd:COG5185 263 TDL--RLEKLGENAESSKRLNENANNLI---KQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE-QELEESKRETEt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1900 GILAEAKNLSLNATAAFNAYSNIKKLIDNaddaakeakakaneAVELVTGPQGPLK-DKAKSFIQKSFR-VHTDAKTQsl 1977
Cdd:COG5185 337 GIQNLTAEIEQGQESLTENLEAIKEEIEN--------------IVGEVELSKSSEElDSFKDTIESTKEsLDEIPQNQ-- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1978 dlKEKENE-LAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNdTIVKIQTAKDKVKQAND-------------TANDVL 2043
Cdd:COG5185 401 --RGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSK-LLNELISELNKVMREADeesqsrleeaydeINRSVR 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2044 ARIKDLNLNLLGLKQNYSALKEDVAKTNA-----VVKVDNVTDAGER-VKLLEKEADRLLDKLKPIK 2104
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAklerqLEGVRSKLDQVAEsLKDFMRARGYAHILALENL 544
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
409-466 |
2.81e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 409 CNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYPNCVKCNC 466
Cdd:pfam00053 1 CDCNPHGSLSDTC---------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1101-1159 |
5.13e-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: 54.28 E-value: 5.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 1101 SCDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLHIgNPLGC 1159
Cdd:cd00055 1 PCDCNGHGSLSGQCD---------PGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
6.23e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 6.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1102 CDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLhigNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCD---------PDTGQCECKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1766-2126 |
7.97e-09 |
|
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: 61.61 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1766 KLRHFQDKLEDVLDMLREARGKIresNHL--------------SAINKHNMTALEGHKQAVEKGKKETENTLNESDDimt 1831
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQL---KSLerqaekaerykelkAELRELELALLVLRLEELREELEELQEELKEAEE--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1832 EVNNLAQNINEAENELMDINKELPQLTERLNV---KINNLTDEIQTRDLPEQVLQAELhaAQLTESSRMLDGILAEAKnl 1908
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQILRERL--ANLERQLEELEAQLEELE-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1909 slnataafnaysniKKLIDnaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAA 1988
Cdd:TIGR02168 330 --------------SKLDE--------------------------LAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1989 MKDKLQNADEKNVNLVRALNDTLGKLSAIPNdtivKIQTAKDKVKQANDT------------ANDVLARIKDLNLNLLGL 2056
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEARLERLEDRrerlqqeieellKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2057 KQNYSALKEDVAKTNAVVKV--DNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNISQIKELINQARK 2126
Cdd:TIGR02168 446 EEELEELQEELERLEEALEElrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1663-2127 |
8.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQ-LKNFVKDIL-----QTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMmAELRRRMFKNQEK--AAADE 1734
Cdd:COG4717 32 NEAGKStLLAFIRAMLlerleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEEleELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1735 LKAAEGLLNRVKKL--FQDPHNKTNDLNLEvkdkLRHFQDKLEDVLDMLREARGKIRESNHLSAinkhnmTALEGHKQAV 1812
Cdd:COG4717 111 LEELREELEKLEKLlqLLPLYQELEALEAE----LAELPERLEELEERLEELRELEEELEELEA------ELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1813 EKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELpqltERLNVKINNLTDEIQTRDLPEQVLQAELHAAQLT 1892
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1893 essrmldGILAeaknLSLNATAAFNAYSNIKKLIdnaddaakeakakaNEAVELVTGPQGPLKDKAKSFIQKSFRVHTDA 1972
Cdd:COG4717 257 -------ALLA----LLGLGGSLLSLILTIAGVL--------------FLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1973 KTQSLDlkekENELAAMKDKLQNADEKNVNLVRALNDTLGKLsaipNDTIVKIQTAKD--KVKQANDTANDVLARIKDLN 2050
Cdd:COG4717 312 ALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEEL----QELLREAEELEEelQLEELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2051 L----NLLGLKQNYSALKEDV--------AKTNAVVKVDNVTDAGErvklLEKEADRLLDKLKPIKELQDNLGKNISQIK 2118
Cdd:COG4717 384 EeelrAALEQAEEYQELKEELeeleeqleELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELE 459
|
....*....
gi 2019522063 2119 ELINQARKQ 2127
Cdd:COG4717 460 AELEQLEED 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-908 |
1.02e-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: 53.51 E-value: 1.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2019522063 861 CQCNDNLDLSAPgcCDSETGECRiCKPGVTGEYCNTCSEGYFGNALGP 908
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
1.17e-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: 1.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 1056 CDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGYRNYPHCISCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1686-2217 |
1.36e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1686 KAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKA-AEGLLNRVKKLFqdphnktnDLNLEVk 1764
Cdd:PRK01156 91 KGSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEMDSlISGDPAQRKKIL--------DEILEI- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1765 DKLRHFQDKLEDVLDMLR-------EARGKIRESNHLSAINKHNMTALEGHKQAVEKGKKE-------TENTLNESDDIM 1830
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRaeisnidYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERlsieynnAMDDYNNLKSAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1831 TEVNNLAQNINEAENELMDI----------NKELPQLTERLNVKINNLTdeIQTRdlpEQVLQAELHAAQLTESSRMLDG 1900
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAesdlsmelekNNYYKELEERHMKIINDPV--YKNR---NYINDYFKYKNDIENKKQILSN 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1901 ILAEaknlslnataaFNAY-SNIKKLIDnaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRvHTDAKTQSLDL 1979
Cdd:PRK01156 317 IDAE-----------INKYhAIIKKLSV--------------------------LQKDYNDYIKKKSR-YDDLNNQILEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1980 KEKE-------NELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPnDTIVKIQtakdkvKQANDTANDVLARIKDLNLN 2052
Cdd:PRK01156 359 EGYEmdynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP-DAIKKEL------NEINVKLQDISSKVSSLNQR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2053 LLGLKQNYSALKEDVA------------------KTNAVVKVDNVTDAG--ERVKLLEKEADRLLDKLKPIKELQDNLGK 2112
Cdd:PRK01156 432 IRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKSRleEKIREIEIEVKDIDEKIVDLKKRKEYLES 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2113 niSQIKELINQ------ARKQANSIKVSVSSGGDciRTYKPDIKKGRYNTI---ILNVKTSTPDNLLFYLGSnkfTDFLA 2183
Cdd:PRK01156 512 --EEINKSINEynkiesARADLEDIKIKINELKD--KHDKYEEIKNRYKSLkleDLDSKRTSWLNALAVISL---IDIET 584
|
570 580 590
....*....|....*....|....*....|....*
gi 2019522063 2184 IEMRKGKVNF-LWDVGSGVGRVEypnLDINDDSWY 2217
Cdd:PRK01156 585 NRSRSNEIKKqLNDLESRLQEIE---IGFPDDKSY 616
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1055-1097 |
1.58e-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: 1.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2019522063 1055 ACDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGYRNYP 1097
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-794 |
3.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2019522063 753 CRCFGH---SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTD 794
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1602-1862 |
3.96e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1602 SIENETQELKhllspqrapERLLQLaqNNQ--------DTLVIEIDELLNRAAKVSADgeqtgKDAErtNERAKQLKNFV 1673
Cdd:COG1340 19 ELREEIEELK---------EKRDEL--NEElkelaekrDELNAQVKELREEAQELREK-----RDEL--NEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1674 KDILQTSKDIYDKAVKLNETLGIQNKtLEKSLQELQKDVDKmmaeLRRR-----MFKNQEKAAADELKAAEGLLNRVKKL 1748
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNK-AGGSIDKLRKEIER----LEWRqqtevLSPEEEKELVEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1749 fqdphnktndlnLEVKDKLRHFQDKLEDVLDMLREARGKIREsnhLSA-INKHnmtalegHKQAVEKgKKETENTLNESD 1827
Cdd:COG1340 156 ------------LEKNEKLKELRAELKELRKEAEEIHKKIKE---LAEeAQEL-------HEEMIEL-YKEADELRKEAD 212
|
250 260 270
....*....|....*....|....*....|....*
gi 2019522063 1828 DIMTEVNNLAQNINEAENELMDINKELPQLTERLN 1862
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1411-1448 |
4.00e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2019522063 1411 CQCNG---HSDMCDPQTSVCQaCKHNTTGDHCEWCAPGFYG 1448
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1518-1555 |
4.17e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.17e-08
10 20 30
....*....|....*....|....*....|....*...
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRH 1555
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1660-1927 |
7.95e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1660 ERTNERAKQLKNFVKDILQTSKDIY--------DKAVKLNETLgIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKaa 1731
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLvlrleelrEELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVSELEEE-- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1732 adelkaaeglLNRVKKLFQDPHNKTNDLNLEV---KDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHN----MTA 1804
Cdd:TIGR02168 283 ----------IEELQKELYALANEISRLEQQKqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1805 LEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLT---ERLNVKINNLTDEIQTrdlpeqv 1881
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEE------- 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2019522063 1882 LQAELHAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLID 1927
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
408-459 |
8.44e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.82 E-value: 8.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 408 PCNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYP 459
Cdd:cd00055 1 PCDCNGHGSLSGQC---------DPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1518-1558 |
1.26e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRHVRE 1558
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
2.06e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.06e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2019522063 861 CQCNdnLDLSAPGCCDSETGECRiCKPGVTGEYCNTCSEGYFGN 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1518-1557 |
2.24e-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: 2.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRHVR 1557
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1099 |
2.38e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 1056 CDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGY--RNYPHC 1099
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
2.68e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 2.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 753 CRC--FGH-SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTDG 795
Cdd:smart00180 1 CDCdpGGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
464-510 |
1.03e-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: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 464 CNCSVPGSINeDPCVD---PCICKENVAGNNCDVCKHSYFNLKRDNPRGC 510
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
409-459 |
1.36e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 409 CNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYP 459
Cdd:smart00180 1 CDCDPGGSASGTC---------DPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
818-859 |
1.57e-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: 47.35 E-value: 1.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2019522063 818 CHLDPTRGLVCDA------CPPGYTGLRCERCANGYFGQPSLPGGsCQ 859
Cdd:cd00055 4 CNGHGSLSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
803-858 |
1.59e-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: 1.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019522063 803 CACPMSIASnnfSPTCHLdptRGLVCDaCPPGYTGLRCERCANGYFGQPSLPGGSC 858
Cdd:pfam00053 1 CDCNPHGSL---SDTCDP---ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1970-2137 |
2.42e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1970 TDAKTQSLDLKEKENELAAMKDKL-QNADEKNvNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKD 2048
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELaEKRDELN-AQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2049 L---NLNLLGLKQNYSALKEDVAK-----TNAVVKVDNVTDAGERVKLLEKEADRL---LDKLKPIKELQ---DNLGKNI 2114
Cdd:COG1340 97 LrkeLAELNKAGGSIDKLRKEIERlewrqQTEVLSPEEEKELVEKIKELEKELEKAkkaLEKNEKLKELRaelKELRKEA 176
|
170 180
....*....|....*....|...
gi 2019522063 2115 SQIKELINQARKQANSIKVSVSS 2137
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIE 199
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1767-1927 |
4.48e-06 |
|
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: 50.87 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1767 LRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGH-----KQAV------EKGKKETENTLNESDDIMTEVNN 1835
Cdd:pfam06008 14 PYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQEteelqKKATqtlakaQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1836 LAQNINEAENELMDINKELPQLT----ERLNVKINNLTDEIQTRDL--PEQVLQAELHAAQ--LTESSRMLDGILAEAKN 1907
Cdd:pfam06008 94 LIDNIKEINEKVATLGENDFALPssdlSRMLAEAQRMLGEIRSRDFgtQLQNAEAELKAAQdlLSRIQTWFQSPQEENKA 173
|
170 180
....*....|....*....|
gi 2019522063 1908 LSLNATAAFNAYSNikKLID 1927
Cdd:pfam06008 174 LANALRDSLAEYEA--KLSD 191
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
282-329 |
5.24e-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: 45.81 E-value: 5.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 282 CICYGHA---RSCpwDPKTNKssCECEHNTCGHSCDRCCPGFHQKPWRAGT 329
Cdd:cd00055 2 CDCNGHGslsGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
5.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 5.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 803 CACPmsiASNNFSPTCHLDptrGLVCDaCPPGYTGLRCERCANGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1604-1885 |
1.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1604 ENETQELKHLLSPQRapERLLQLAQNN--------------------QDTLVIEIDELLNRAAKVSADGEQTGKDAERTN 1663
Cdd:PRK02224 271 EREREELAEEVRDLR--ERLEELEEERddllaeaglddadaeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1664 ERAKQLKnfvkdilQTSKDIYDKAVKLNETLGIQNKTLEKSlQELQKDVDKMMAELRRRmFKNqekaAADELKAAEGLLn 1743
Cdd:PRK02224 349 EDADDLE-------ERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRER-FGD----APVDLGNAEDFL- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1744 rvkklfqdphnktnDLNLEVKDKLRhfqDKLEDVLDMLREARGKIRESNHLSAINKHNMTA--LEG--HKQAVEKGKKET 1819
Cdd:PRK02224 415 --------------EELREERDELR---EREAELEATLRTARERVEEAEALLEAGKCPECGqpVEGspHVETIEEDRERV 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1820 ENTLNESDDIMTEVNNLAQNINEAEnELMDINKELpqltERLNVKINNLTDEIQTRD--LPEQVLQAE 1885
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAE-DLVEAEDRI----ERLEERREDLEELIAERRetIEEKRERAE 540
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1621-1852 |
2.17e-05 |
|
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: 49.29 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1621 ERLLQLAQNNQDTLVIEIDELLNRAAKVSadgEQTGKDAERTNERAKQLknfvkdilQTSKDIYDKavKLNETLGIQNKt 1700
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVV---DKLTDFENQTEKDQTAL--------ETLEKALKD--LLTDEGGAIAR- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1701 leKSLQELQKDVDKMMAELRRRMfKNQEKAAADELKAAEGLLNRVKKLFQDphnktndlnlevkdkLRHFQDKLEDVLDM 1780
Cdd:cd22656 179 --KEIKDLQKELEKLNEEYAAKL-KAKIDELKALIADDEAKLAAALRLIAD---------------LTAADTDLDNLLAL 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1781 LREArgkiresnhLSAINKhnmtaLEGHKQAVEkgkketentlNESDDIMTEVNNLAQNINEAENELMDINK 1852
Cdd:cd22656 241 IGPA---------IPALEK-----LQGAWQAIA----------TDLDSLKDLLEDDISKIPAAILAKLELEK 288
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1459-1516 |
5.75e-05 |
|
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: 42.73 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1459 PCACPLHIASNnfsPTCIMQgtnDYRCTaCPQGYEGQYCERCASGYTGNPSIPGGsCQ 1516
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
464-510 |
1.27e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 464 CNCSVPGSINeDPCvDP----CICKENVAGNNCDVCKHSYFNlkrDNPRGC 510
Cdd:smart00180 1 CDCDPGGSAS-GTC-DPdtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-510 |
4.67e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 4.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 464 CNCSVPGSINEDpCvDP----CICKENVAGNNCDVCKHSYFNLkRDNPRGC 510
Cdd:cd00055 2 CDCNGHGSLSGQ-C-DPgtgqCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1673-1786 |
4.67e-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: 42.96 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1673 VKDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAElRRRMFKNQEKAAADELKAAEGLLNRVKKLFQDp 1752
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKD-AATLSEAAREKKEKELQKKVQEFQRKQQKLQQ- 83
|
90 100 110
....*....|....*....|....*....|....
gi 2019522063 1753 hnktnDLNLEVKDKLRHFQDKLEDVLDMLREARG 1786
Cdd:smart00935 84 -----DLQKRQQEELQKILDKINKAIKEVAKKKG 112
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
1761-2131 |
8.57e-04 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 44.56 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1761 LEVKDKLRHFQDKLEDVLDMLREARGKIRESNH-----LSAINKhnmtaLEGHKQAVekgKKETENTLNE----SDDIMT 1831
Cdd:cd22654 58 IDLNQDMINFSQRFNNYYDKLYDLAGKINEDEQakedfLNGINK-----LQSQLQTI---QNSMEQTSSNlnrfKTLLDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1832 EVNNLAQNINEAENELMDINKELPQLTErlnvKINNLTDEIQtrdlpEQVLQAelhaaqLTESSRMLDGILaeaknlsln 1911
Cdd:cd22654 130 DSKNFSTDAKKAIDSLSGSNGEIAQLRT----QIKTINDEIQ-----EELTKI------LNRPIEVGDGSI--------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1912 ataafnaysNIKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDkaksfiqksfrvhTDAKTQSLDLKEKENELaamkd 1991
Cdd:cd22654 186 ---------NIGKQVFTITITTATTKTVDVTSIGGLINGIGNASD-------------DEVKEAANKIQQKQKEL----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1992 klqnadeknVNLVRALNDTLGKLSAIpndTIVkiqtaKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTN 2071
Cdd:cd22654 239 ---------VDLIKKLSDAEIQATQL---TLV-----EDQVNGFTELIKRQIATLENLVEDWEMLNQNMNQLQTNVNSGK 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2072 avvkVDNVTdagervkllekeadrLLDKLKPIKELQDNLGKnisqikelinQARKQANSI 2131
Cdd:cd22654 302 ----IDSKL---------------LQKQLKQIKKISDELNK----------QTKQFEDFL 332
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1357-1460 |
3.62e-03 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 40.75 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1357 TSFTMSPKASRIEKC----ECPVGYSGLS---------CEsCSPGFYRMAPAspgrrpgptlGTCVPCQcnghsdMCDPQ 1423
Cdd:cd13416 40 DGVTFSDVVSHTEPCqpctRCPGLMSMRApctathdtvCE-CAYGYYLDEDS----------GTCEPCT------VCPPG 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 2019522063 1424 TSVCQACKHNT-TGdhCEWCAPGFYGTVRGFPDDCRPC 1460
Cdd:cd13416 103 QGVVQSCGPNQdTV--CEACPEGTYSDEDSSTDPCLPC 138
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-325 |
5.36e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.36e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
30-280 |
4.58e-93 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 301.97 E-value: 4.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 30 QQRGLFPAVLNLASNAIITANATCGENGPEMFCKLVEHVhgqpVRHSQCRTCDQNSPDKNlhYPIAHAING----KRTWW 105
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARNPRRS--HPAENLTDGnnpnNPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 106 QSPSIKNGVQYhyVTITLDLQQVFQIAYVIIKAAnSPRPGNWILERSLDGISYKPWQYHAitnSECLTRYNIIPRPGIPL 185
Cdd:smart00136 77 QSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 186 YtKDDEVICTSHYSKIHPLENGEIHTSLINGRPSAEDP--SPTLLEFTSARFIRLRLQKIRTLNADLMmlaysdpqDLDP 263
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 2019522063 264 IVTRRYFYSIKDISVGG 280
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
34-280 |
1.76e-83 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 274.07 E-value: 1.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 34 LFPAVLNLASNAIITANATCGENGPEMFCKLVEhvhgqPVRHSQCRTCDqnSPDKNLHYPIAHAI----NGKRTWWQSPS 109
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSG-----LEGGKKCFICD--SRDPHNSHPPSNLTdsnnGTNETWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 110 IKngVQYHYVTITLDLQQVFQIAYVIIKAAnSPRPGNWILERSLD-GISYKPWQYHAitnSECLTRYNIIPRPgiPLYTK 188
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSGP--SRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 189 DDEVICTSHYSKIHPLENGEIHTSLINGRPSAE--DPSPTLLEFTSARFIRLRLQKIRTLNadlmmlaysDPQDLDPIVT 266
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 2019522063 267 RRYFYSIKDISVGG 280
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1584-1843 |
1.09e-63 |
|
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: 218.44 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1584 VMSVN-LSGPLPPPYRMLFSIENETQELKHLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERT 1662
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQLKNFVKDILQTSKDIYDKAVKLNETlgiQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGLL 1742
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1743 NRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGHKQAVEKGKKETENT 1822
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 2019522063 1823 LNESDDIMTEVNNLAQNINEA 1843
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1369 |
6.43e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 159.74 E-value: 6.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1230 YWKLPEQFEGRKLTAYGGKLKYTIYFEAREETGPSAYEPQVVIRGGpasNHRIIVR--NVPDPQNGQLTRHDIEMTEFEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSspDQPPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1308 KHIDGGSVSREDFMDVLFDIQYILIKASYGRVLRQTRISEVFLEVAEEGTSftmSPKASRIE 1369
Cdd:pfam00052 78 RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1355 |
6.01e-42 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 150.87 E-value: 6.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1225 HSEPFYWKLPEQFEGRKLTAYGGKLKYTIYFEAREEtGPSAYEPQVVIRGGpasNHRIIVRNVPDPQNGQLTRHDIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 1305 FEWKHIDGGSVSREDFMDVLFDIQYILIKASYGRVLRQTRISEVFLEVAEE 1355
Cdd:smart00281 77 ENWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2028-2160 |
9.79e-42 |
|
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: 150.71 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2028 AKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVKVDN--VTDAGERVKLLEKEADRLLDKLKPIKE 2105
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANkaLDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 2106 LQDN---LGKNISQIKELINQARKQANSIKVSVSSGGDCIRTYKPDIKKGRYNTIILN 2160
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
2.31e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.95 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 579 YWSAPASYLHSKVAAVGGHLTYTISYDTSvkDEAEEFTDHSSIIIEGNGIWISTSQYEAD-LHPFEERTVNVVLHPEYFK 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPL--PGGGSLNSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 658 mHSTGYQVSREDFMTVMANVKRLLIRATYSNQPDAIyRLSSVNLEVAEEsSSSGRTAYDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVP-GGSGPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2794-2912 |
7.14e-37 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 136.68 E-value: 7.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2794 RTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMVPQRVNDGEWHKINIFRTKQTGYLFVDGIANST-NS 2872
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2019522063 2873 PKKADI-LDVVGMLYVGGLPVNYTTKRIGPVLHSIDGCIRN 2912
Cdd:pfam00054 82 PLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRD 122
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2941-3093 |
3.21e-35 |
|
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: 132.54 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2941 GTYFDGSGFAKTVGAFKVGTDLLIELEFRTTKTNGVLIGISGK-KMDGLGIEMVDGKLLFHADNGAGRftAVYEPEVPgs 3019
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGS--LVLSSKTP-- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 3020 LCDGQWHKVTANKIKHRLEMIVDNKKVEASSPNAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2766-2915 |
1.14e-34 |
|
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: 131.00 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2766 FGLSKNSHMAFAFDDTKvKNTLSIELELRTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMVPQRVNDG 2845
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 2846 EWHKINIFRTKQTGYLFVDGIA-NSTNSPKKADILDVVGMLYVGGLPVNYTTKRIgPVLHSIDGCIRNFRM 2915
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2354-2495 |
1.08e-33 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 127.43 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2354 FKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKNYNDGKWKSFTLSRIQKQANFSIVDmdtnEEE 2433
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG----EAR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2434 IVATTSTGSNFGLNLksDEKIYFGGLPGLsslspSVKARPEVNLKKYAGCLKDIEVSRTPYN 2495
Cdd:pfam00054 77 PTGESPLGATTDLDV--DGPLYVGGLPSL-----GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
579-706 |
3.29e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 125.84 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 579 YWSAPASYLHSKVAAVGGHLTYTISYDTSVKDEaeeftdHSS---IIIEGNGIWISTsQYEADLHPFEERTVNVVLHPEY 655
Cdd:smart00281 6 YWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT------HVSapdVILEGNGLRISH-PAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 656 FKMHStGYQVSREDFMTVMANVKRLLIRATYSNQPDAIYrLSSVNLEVAEE 706
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2915 |
1.88e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 123.99 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2788 SIELELRTKADSGLIFYMARINHADFATIQIKEGMAHFRYDLGSGDTTTMV-PQRVNDGEWHKINIFRTKQTGYLFVDGI 2866
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2867 ANSTN-SPKKADILDVVGMLYVGGLPVNYTTKRIgPVLHSIDGCIRNFRM 2915
Cdd:smart00282 81 NRVSGeSPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2326-2489 |
1.31e-31 |
|
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: 122.14 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2326 TVQFDGDGYALVNRPvRWNPNISTIMFKFKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKNYND 2405
Cdd:cd00110 1 GVSFSGSSYVRLPTL-PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2406 GKWKSFTLSRIQKQANFSIvdmdtNEEEIVATTSTGSNFGLNLksDEKIYFGGLPglsslsPSVKARPEVNLKKYAGCLK 2485
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLP------EDLKSPGLPVSPGFVGCIR 146
|
....
gi 2019522063 2486 DIEV 2489
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2964-3093 |
1.40e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 121.68 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2964 IELEFRTTKTNGVLIGISGK-KMDGLGIEMVDGKLLFHADNGAGRFTAVYEPevpGSLCDGQWHKVTANKIKHRLEMIVD 3042
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 3043 NK-KVEASSPnAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:smart00282 79 GGnRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
smart00282 |
Laminin G domain; |
2349-2491 |
2.35e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.43 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2349 TIMFKFKTFSSSALLMYLATSDLKDFMSVELSDGRIKVSYDLGSGTAYAVSNKN-YNDGKWKSFTLSRIQKQANFSIvdm 2427
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 2428 dtNEEEIVATTSTGSNFGLNLksDEKIYFGGLPglsslsPSVKARPEVNLKKYAGCLKDIEVSR 2491
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLP------EDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2968-3093 |
8.04e-27 |
|
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: 107.51 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2968 FRTTKTNGVLIGISGKKMDGLGIEMVDGKLLFHADNGAGRFTAVYEPEvpgSLCDGQWHKVTANKIKHRLEMIVDNKKVE 3047
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK---NLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2019522063 3048 ASSPNAASTSTDTNDPVFVGGYPEDVKQFGLTTQVSFKGCIRDLKL 3093
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2161-2300 |
1.02e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 107.40 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2161 VKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLdINDDSWYRVEASRSGINGTISVqafDGpKA 2240
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV---DG-EA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2241 SIVpsiysSTSQPGYTI-LDVDGhELFVGGLTGKI-KKADAVKVTTFTGCMGETFFDGKPIG 2300
Cdd:pfam00054 76 RPT-----GESPLGATTdLDVDG-PLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2156-2297 |
1.45e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.04 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2156 TIILNVKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLDINDDSWYRVEASRSGINGTISVqaf 2235
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2236 DGPKASivpsiySSTSQPGYTILDVDGhELFVGGLTGKIKKADAVKVTTFTGCMGETFFDGK 2297
Cdd:smart00282 78 DGGNRV------SGESPGGLTILNLDG-PLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2137-2295 |
5.00e-26 |
|
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: 106.35 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2137 SGGDCIRtYKPDIKKGRYNTIILNVKTSTPDNLLFYLGSNKFTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLdINDDSW 2216
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 2217 YRVEASRSGINGTISVqafDGPKasivpsIYSSTSQPGYTILDVDGhELFVGGLTGKIKKADAVKVTTFTGCMGETFFD 2295
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDG-PLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2516-2677 |
7.01e-26 |
|
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: 105.96 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2516 SVSFSKPGYIEVP-PVSMDVGTEITLSFSTKNESGMILFGNGgslisprrkrrQSGQAFYAVLLRKGKLEVAVSGSKEPh 2594
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2595 qIIIRPeKKKFHDGKEHSIRIERSRNILTAQVDEDR--NQTLKLPASYSISVKKLFVGGIPSDVQFPHYKSIPPFEGCIW 2672
Cdd:cd00110 69 -LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIR 146
|
....*
gi 2019522063 2673 DLLIN 2677
Cdd:cd00110 147 DLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2968-3093 |
1.25e-25 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 104.32 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2968 FRTTKTNGVLI-GISGKKMDGLGIEMVDGKLLFHADNGAGRFTAVYEPEvpgsLCDGQWHKVTANKIKHRLEMIVDNKKV 3046
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK----LNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2019522063 3047 E-ASSPNAASTSTDTNDPVFVGGYPED-VKQFGLTTQVSFKGCIRDLKL 3093
Cdd:pfam00054 77 PtGESPLGATTDLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIV 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2793-2915 |
1.38e-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: 101.34 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2793 LRTKADSGLIFYMARINHaDFATIQIKEGMAHFRYDLGSGDTTTMV-PQRVNDGEWHKINIFRTKQTGYLFVDGI-ANST 2870
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQtVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2019522063 2871 NSPKKADILDVVGMLYVGGLPVNYTTKRIgPVLHSIDGCIRNFRM 2915
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1637-2151 |
4.97e-23 |
|
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: 107.80 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1637 EIDELLNRAAKVSADGEQTGKDAERTNERAKQLKN----FVKDIL---QTSKDIYDKAVKLNETLGI------------- 1696
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENelnlLEKEKLniqKNIDKIKNKLLKLELLLSNlkkkiqknksles 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1697 -------QNKTLEKSLQELQKDVDKMMAELRRRM------------FKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTN 1757
Cdd:TIGR04523 219 qiselkkQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1758 DLN--------LEVKDKLRHFQDKLEDVLDMLREARGKI-----------RESNHLSAINKHNMTALEGHKQAVEKGKKE 1818
Cdd:TIGR04523 299 DLNnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1819 TENTLNESDDIMTEVNNLAQNINEAENElmdiNKELPQLTERLNVKINNLTDEIQtrDLPEQVLQAElhaaqltessrml 1898
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL----NQQKDEQIKKLQQEKELLEKEIE--RLKETIIKNN------------- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1899 dgilAEAKNLSLNATAAFNAYSNIKKLIDNaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLD 1978
Cdd:TIGR04523 440 ----SEIKDLTNQDSVKELIIKNLDNTRES-------------------------LETQLKVLSRSINKIKQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1979 LKEKENELAAMKDKLQNADEKNVNLVR---ALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTAN-DVLARIKD-LNLNL 2053
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKkisSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkENLEKEIDeKNKEI 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2054 LGLKQNYSALK-------EDVAK------------TNAVVKVDNVTDageRVKLLEKEADRLLDKLKPIKELQDNLGKNI 2114
Cdd:TIGR04523 571 EELKQTQKSLKkkqeekqELIDQkekekkdlikeiEEKEKKISSLEK---ELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2115 SQIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPDIKK 2151
Cdd:TIGR04523 648 KQIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2354-2489 |
2.22e-22 |
|
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: 95.18 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2354 FKTFSSSALLMYlATSDLKDFMSVELSDGRIKVSYDLGSG-TAYAVSNKNYNDGKWKSFTLSRIQKQANFSiVDmdtnee 2432
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLS-VD------ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2433 EIVATTSTGSNFGLNLKSDEKIYFGGLPGLSSLSPSVKARPevnlkkYAGCLKDIEV 2489
Cdd:pfam02210 73 GQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAG------FVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2537-2677 |
2.92e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.02 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2537 EITLSFSTKNESGMILFgNGGSLisprrkrrqsGQAFYAVLLRKGKLEVAVSGSKEPhqIIIRPEKKKFHDGKEHSIRIE 2616
Cdd:smart00282 1 SISFSFRTTSPNGLLLY-AGSKG----------GGDYLALELRDGRLVLRYDLGSGP--ARLTSDPTPLNDGQWHRVAVE 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 2617 RSRNILTAQVDEDRNQTLKLPASYSI--SVKKLFVGGIPSDVQFPHYKSIPPFEGCIWDLLIN 2677
Cdd:smart00282 68 RNGRSVTLSVDGGNRVSGESPGGLTIlnLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2542-2682 |
6.23e-20 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 88.14 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2542 FSTKNESGMILFGNggslisprrkrRQSGQAFYAVLLRKGKLEVAVSGSKepHQIIIRPeKKKFHDGKEHSIRIERSRNI 2621
Cdd:pfam00054 1 FRTTEPSGLLLYNG-----------TQTERDFLALELRDGRLEVSYDLGS--GAAVVRS-GDKLNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 2622 LTAQVDEDRNQTLKLPASYSISVK---KLFVGGIPSDVQFPHYKSI-PPFEGCIWDLLINAVPTD 2682
Cdd:pfam00054 67 GTLSVDGEARPTGESPLGATTDLDvdgPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVNGKPLD 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1629-2160 |
4.06e-18 |
|
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: 91.62 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1629 NNQDTlviEIDELLNRAAKVSAD---GEQTGKDAERT-NERAKQLKNF---VKDILQTSKDIYDKAVKLNETLGIQNKTL 1701
Cdd:TIGR04523 29 NKQDT---EEKQLEKKLKTIKNElknKEKELKNLDKNlNKDEEKINNSnnkIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1702 EKSLQELQKDVDKM------MAELRRRMFKNQEKAA--ADELKAAEGLLNrvkKLFqdphNKTNDLN---LEVKDKLRHF 1770
Cdd:TIGR04523 106 SKINSEIKNDKEQKnkleveLNKLEKQKKENKKNIDkfLTEIKKKEKELE---KLN----NKYNDLKkqkEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1771 QDKLEDVLDMLREARGKIRESNHL-----SAINKHN-----MTALEGHKQAVEKGKKETENTLNEsddIMTEVNNLAQNI 1840
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLlsnlkKKIQKNKslesqISELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1841 NEAENELMDINKELPQLT---ERLNVKINNLTDEIQT-----RDL---PEQVLQAELHAaQLTESSRMLDGI---LAEAK 1906
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQkelEQNNKKIKELEKQLNQlkseiSDLnnqKEQDWNKELKS-ELKNQEKKLEEIqnqISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1907 NL--SLNataafNAYSNIKKLIDNADDAAKEAkakaneavelvtgpQGPLKDKaKSFIQKSFRVHTDAKTQSLDLKEKEN 1984
Cdd:TIGR04523 335 KIisQLN-----EQISQLKKELTNSESENSEK--------------QRELEEK-QNEIEKLKKENQSYKQEIKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1985 ELaamKDKLQNADEKNVNLvralnDTLGKLSAIPNDTIVK-IQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSAL 2063
Cdd:TIGR04523 395 DL---ESKIQNQEKLNQQK-----DEQIKKLQQEKELLEKeIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2064 KEDVAKTNAVVKV--DNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNISQIKELINQARKQANSIKVSVSSGGDC 2141
Cdd:TIGR04523 467 ETQLKVLSRSINKikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
570
....*....|....*....
gi 2019522063 2142 IRTYKPDIKKGRYNTIILN 2160
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDE 565
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2542-2677 |
1.88e-17 |
|
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: 80.93 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2542 FSTKNESGMILFGNGGslisprrkrrqsGQAFYAVLLRKGKLEVAVSGSKEPhqIIIRPEKKKFHDGKEHSIRIERSRNI 2621
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG------------GSDFLALELVNGRLVLRYDLGSGP--ESLLSSGKNLNDGQWHSVRVERNGNT 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 2622 LTAQVDEDRNQTLKLPASYSI--SVKKLFVGGIPSDVQFPHYKSIPPFEGCIWDLLIN 2677
Cdd:pfam02210 67 LTLSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2161-2297 |
5.02e-17 |
|
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: 79.77 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2161 VKTSTPDNLLFYLGSNKfTDFLAIEMRKGKVNFLWDVGSGVGRVEYPNLDINDDSWYRVEASRSGINGTISVqafDGPKA 2240
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DGQTV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2241 SivpsiySSTSQPGYTILDVDGhELFVGGLTGKIKKADAVKVTTFTGCMGETFFDGK 2297
Cdd:pfam02210 77 V------SSLPPGESLLLNLNG-PLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
4.70e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 4.70e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 963 CNCNSFGSKSFDCD-DKGQCHCQPGVAGDKCDRCAHGFFDFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
8.41e-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: 65.07 E-value: 8.41e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1102 CDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLHIGNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
3.13e-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: 63.53 E-value: 3.13e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 913 SCNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYG-PVSAQGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGlPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
1.03e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 1.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2019522063 914 CNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYGpVSAQGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1008 |
1.03e-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: 1.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 962 ACNCNSFGSKSFDCDDK-GQCHCQPGVAGDKCDRCAHGFFDF--QEGGCT 1008
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1603-2132 |
1.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1603 IENETQELKHLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKD 1682
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1683 IydkavklnETLGIQNKTLEKSLQELQKDVdKMMAELRRRMFKNQEKAAA------------DELKAAEGLLNRVKKLFQ 1750
Cdd:PRK03918 254 K--------RKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEyiklsefyeeylDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1751 DPHNKTNDLNlEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAInkhnMTALEGHKQ-----AVEKGKKETENTLNE 1825
Cdd:PRK03918 325 GIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAK----KEELERLKKrltglTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1826 SDDIMTEVNNLAQNINEAENELMDINK---EL-------P----QLTE--RLNV------KINNLTDEIQTRDLPEQVLQ 1883
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKaieELkkakgkcPvcgrELTEehRKELleeytaELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1884 AELhaaqltessRMLDGILAEAKNLSLNATAAfnaySNIKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDKAKSfiq 1963
Cdd:PRK03918 480 KEL---------RELEKVLKKESELIKLKELA----EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1964 ksfrVHTDAKtqslDLKEKENELAAMKDKLQNADEKNVNL-----------VRALNDTLGKLSAIPNDTIV--------- 2023
Cdd:PRK03918 544 ----LKKELE----KLEELKKKLAELEKKLDELEEELAELlkeleelgfesVEELEERLKELEPFYNEYLElkdaekele 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2024 ----KIQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYS------ALKEDVAKTNAVVKVDnvtdagERVKLLEK-- 2091
Cdd:PRK03918 616 reekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeeLREEYLELSRELAGLR------AELEELEKrr 689
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2092 -EADRLLDKLKP--------IKELQdNLGKNISQIKELINQARKQANSIK 2132
Cdd:PRK03918 690 eEIKKTLEKLKEeleerekaKKELE-KLEKALERVEELREKVKKYKALLK 738
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
1.82e-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: 61.22 E-value: 1.82e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 963 CNCNSFGSKSFDCDDK-GQCHCQPGVAGDKCDRCAHGFFDFQEGGCTPC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1411-1457 |
2.92e-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: 60.44 E-value: 2.92e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1411 CQCNGH---SDMCDPQTSVCQaCKHNTTGDHCEWCAPGFYGTVRGFPDDC 1457
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
3.82e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1009 PCDCPHVG---NNCEAETGQCVCPPNTVGEQCDKCAPNHWGYSIIT-GCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
5.92e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 5.92e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2019522063 1010 CDCP---HVGNNCEAETGQCVCPPNTVGEQCDKCAPNHWGYS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1599-2131 |
6.83e-11 |
|
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: 68.21 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1599 MLFSIENETQELKHLlspQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAK----QLKNFVK 1674
Cdd:pfam05483 213 MHFKLKEDHEKIQHL---EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdeNLKELIE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1675 DILQTSKDIYDKAVKLNETLGIQnKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEgllnrvkklfqdphN 1754
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQ-KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE--------------F 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1755 KTNDLNLEvkDKLRHFQDKLEDVLDMLREARGKI-RESNHLsainkHNMTALeghkqaveKGKKETEntLNESDDIMTEv 1833
Cdd:pfam05483 355 EATTCSLE--ELLRTEQQRLEKNEDQLKIITMELqKKSSEL-----EEMTKF--------KNNKEVE--LEELKKILAE- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1834 nnlaqnineaENELMDINKELPQLTERLNVKINNLTDEIQTR-----DLPEQV----------------LQAELHAAQL- 1891
Cdd:pfam05483 417 ----------DEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeihDLEIQLtaiktseehylkevedLKTELEKEKLk 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1892 -TESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLIDNaddaAKEAKAKANEAVELVTGPQGPLKDKAKSfIQKSFRVHT 1970
Cdd:pfam05483 487 nIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN----CKKQEERMLKQIENLEEKEMNLRDELES-VREEFIQKG 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1971 DAKTQSLDlKEKENELAAMKDKLQNadEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVL----ARI 2046
Cdd:pfam05483 562 DEVKCKLD-KSEENARSIEYEVLKK--EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnayeIKV 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2047 KDLNLNLLGLKQNYSALKEDVAKTNAVVKV--DNVTDAGERVKLLEKEADRLLdklkpiKELQDNLGKNISQIKELINQA 2124
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKIseEKLLEEVEKAKAIADEAVKLQ------KEIDKRCQHKIAEMVALMEKH 712
|
....*..
gi 2019522063 2125 RKQANSI 2131
Cdd:pfam05483 713 KHQYDKI 719
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
7.60e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 7.60e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 914 CNCNINGSISTVCNLQTGQCECRSNVKGRQCDECMPQTYG--PVSAQGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1049 |
1.91e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2019522063 1010 CDCPHVG---NNCEAETGQCVCPPNTVGEQCDKCAPNHWGYSI 1049
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1410-1458 |
2.05e-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: 2.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1410 PCQCNGHSDM---CDPQTSVCQaCKHNTTGDHCEWCAPGFYGtVRGFPDDCR 1458
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
2.31e-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: 2.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 860 PCQCNDNLDLSAPgcCDSETGECRiCKPGVTGEYCNTCSEGYFGNALGPSSCQ 912
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-797 |
7.76e-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: 7.76e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 752 PCRCFGH---SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTDGTD 797
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1663-2104 |
1.33e-09 |
|
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: 63.82 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEG-- 1740
Cdd:COG5185 116 ADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISel 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1741 LLNRVKKLFQDPHNKTnDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINkhnmtalEGHKQAVEKgkketE 1820
Cdd:COG5185 196 KKAEPSGTVNSIKESE-TGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-------DKLEKLVEQ-----N 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1821 NTLneSDDIMTEVNNLAQNINEAENELMdinKELPQLTERLNVKINNLTDEIQTRDLPEQVLQAELHaAQLTESSRMLD- 1899
Cdd:COG5185 263 TDL--RLEKLGENAESSKRLNENANNLI---KQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE-QELEESKRETEt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1900 GILAEAKNLSLNATAAFNAYSNIKKLIDNaddaakeakakaneAVELVTGPQGPLK-DKAKSFIQKSFR-VHTDAKTQsl 1977
Cdd:COG5185 337 GIQNLTAEIEQGQESLTENLEAIKEEIEN--------------IVGEVELSKSSEElDSFKDTIESTKEsLDEIPQNQ-- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1978 dlKEKENE-LAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNdTIVKIQTAKDKVKQAND-------------TANDVL 2043
Cdd:COG5185 401 --RGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSK-LLNELISELNKVMREADeesqsrleeaydeINRSVR 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2044 ARIKDLNLNLLGLKQNYSALKEDVAKTNA-----VVKVDNVTDAGER-VKLLEKEADRLLDKLKPIK 2104
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAklerqLEGVRSKLDQVAEsLKDFMRARGYAHILALENL 544
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1621-1898 |
1.43e-09 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 62.28 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1621 ERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNfVKDILQTskdiydkavKLNETLGIQNKt 1700
Cdd:pfam09728 3 ARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQK-EKDQLQS---------ELSKAILAKSK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1701 LEKSLQELQKDVDKMMAELRRRMfkNQEKAAADELKAA-EGLLNRVKKLFQD---PHNKTNDLNLEVKDKLRHFQDKLEd 1776
Cdd:pfam09728 72 LEKLCRELQKQNKKLKEESKKLA--KEEEEKRKELSEKfQSTLKDIQDKMEEkseKNNKLREENEELREKLKSLIEQYE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1777 vldmLREArgkiresnHLSAINKH-------NMTALEGHKQAVEKGKKETE----------------------------- 1820
Cdd:pfam09728 149 ----LREL--------HFEKLLKTkelevqlAEAKLQQATEEEEKKAQEKEvakarelkaqvqtlsetekelreqlnlyv 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1821 -------NTLNESDDIMT----EVNNLAQNINEAENElmdiNKELPQLTERLNVKINNLTDEIQTRDLPEQVLQAELHaa 1889
Cdd:pfam09728 217 ekfeefqDTLNKSNEVFTtfkkEMEKMSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLE-- 290
|
....*....
gi 2019522063 1890 QLTESSRML 1898
Cdd:pfam09728 291 KLENLCRAL 299
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
409-466 |
2.81e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 409 CNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYPNCVKCNC 466
Cdd:pfam00053 1 CDCNPHGSLSDTC---------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1101-1159 |
5.13e-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: 54.28 E-value: 5.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 1101 SCDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLHIgNPLGC 1159
Cdd:cd00055 1 PCDCNGHGSLSGQCD---------PGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
6.23e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 6.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1102 CDCTLAGSKPESCDhetekcscaEETGQCSCKTNVEGVHCDRCKPSTFGLhigNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCD---------PDTGQCECKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1766-2126 |
7.97e-09 |
|
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: 61.61 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1766 KLRHFQDKLEDVLDMLREARGKIresNHL--------------SAINKHNMTALEGHKQAVEKGKKETENTLNESDDimt 1831
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQL---KSLerqaekaerykelkAELRELELALLVLRLEELREELEELQEELKEAEE--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1832 EVNNLAQNINEAENELMDINKELPQLTERLNV---KINNLTDEIQTRDLPEQVLQAELhaAQLTESSRMLDGILAEAKnl 1908
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQILRERL--ANLERQLEELEAQLEELE-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1909 slnataafnaysniKKLIDnaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAA 1988
Cdd:TIGR02168 330 --------------SKLDE--------------------------LAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1989 MKDKLQNADEKNVNLVRALNDTLGKLSAIPNdtivKIQTAKDKVKQANDT------------ANDVLARIKDLNLNLLGL 2056
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEARLERLEDRrerlqqeieellKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2057 KQNYSALKEDVAKTNAVVKV--DNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNISQIKELINQARK 2126
Cdd:TIGR02168 446 EEELEELQEELERLEEALEElrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1663-2127 |
8.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQ-LKNFVKDIL-----QTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMmAELRRRMFKNQEK--AAADE 1734
Cdd:COG4717 32 NEAGKStLLAFIRAMLlerleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEEleELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1735 LKAAEGLLNRVKKL--FQDPHNKTNDLNLEvkdkLRHFQDKLEDVLDMLREARGKIRESNHLSAinkhnmTALEGHKQAV 1812
Cdd:COG4717 111 LEELREELEKLEKLlqLLPLYQELEALEAE----LAELPERLEELEERLEELRELEEELEELEA------ELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1813 EKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELpqltERLNVKINNLTDEIQTRDLPEQVLQAELHAAQLT 1892
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1893 essrmldGILAeaknLSLNATAAFNAYSNIKKLIdnaddaakeakakaNEAVELVTGPQGPLKDKAKSFIQKSFRVHTDA 1972
Cdd:COG4717 257 -------ALLA----LLGLGGSLLSLILTIAGVL--------------FLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1973 KTQSLDlkekENELAAMKDKLQNADEKNVNLVRALNDTLGKLsaipNDTIVKIQTAKD--KVKQANDTANDVLARIKDLN 2050
Cdd:COG4717 312 ALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEEL----QELLREAEELEEelQLEELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2051 L----NLLGLKQNYSALKEDV--------AKTNAVVKVDNVTDAGErvklLEKEADRLLDKLKPIKELQDNLGKNISQIK 2118
Cdd:COG4717 384 EeelrAALEQAEEYQELKEELeeleeqleELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELE 459
|
....*....
gi 2019522063 2119 ELINQARKQ 2127
Cdd:COG4717 460 AELEQLEED 468
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1652-2037 |
9.41e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1652 GEQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRmfKNQEKAA 1731
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA--RSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1732 ADELKAAEGLLNRVKKlfqdphnktndlnlevkdKLRHFQDKLEDVLDMLREARGKIREsnhlsaINKhNMTALEGHKQA 1811
Cdd:COG4372 79 EEELEELNEQLQAAQA------------------ELAQAQEELESLQEEAEELQEELEE------LQK-ERQDLEQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1812 VEKGKKETENTLNESDdimTEVNNLAQNINEAENELMDINKELPQLT-ERLNVKINNLTDEIQTRDLPEQVLQAEL---H 1887
Cdd:COG4372 134 LEAQIAELQSEIAERE---EELKELEEQLESLQEELAALEQELQALSeAEAEQALDELLKEANRNAEKEEELAEAEkliE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1888 AAQLTESSRMLDGILAEAKNLSLNATAAFNAYSNIK---------KLIDNADDAAKEAKAKANEAVELVTGPQGPLKDKA 1958
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEdkeelleevILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 1959 KSFIQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQAND 2037
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-908 |
1.02e-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: 53.51 E-value: 1.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2019522063 861 CQCNDNLDLSAPgcCDSETGECRiCKPGVTGEYCNTCSEGYFGNALGP 908
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
1.17e-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: 1.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 1056 CDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGYRNYPHCISCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1686-2217 |
1.36e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1686 KAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKA-AEGLLNRVKKLFqdphnktnDLNLEVk 1764
Cdd:PRK01156 91 KGSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEMDSlISGDPAQRKKIL--------DEILEI- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1765 DKLRHFQDKLEDVLDMLR-------EARGKIRESNHLSAINKHNMTALEGHKQAVEKGKKE-------TENTLNESDDIM 1830
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRaeisnidYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERlsieynnAMDDYNNLKSAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1831 TEVNNLAQNINEAENELMDI----------NKELPQLTERLNVKINNLTdeIQTRdlpEQVLQAELHAAQLTESSRMLDG 1900
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAesdlsmelekNNYYKELEERHMKIINDPV--YKNR---NYINDYFKYKNDIENKKQILSN 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1901 ILAEaknlslnataaFNAY-SNIKKLIDnaddaakeakakaneavelvtgpqgpLKDKAKSFIQKSFRvHTDAKTQSLDL 1979
Cdd:PRK01156 317 IDAE-----------INKYhAIIKKLSV--------------------------LQKDYNDYIKKKSR-YDDLNNQILEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1980 KEKE-------NELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPnDTIVKIQtakdkvKQANDTANDVLARIKDLNLN 2052
Cdd:PRK01156 359 EGYEmdynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP-DAIKKEL------NEINVKLQDISSKVSSLNQR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2053 LLGLKQNYSALKEDVA------------------KTNAVVKVDNVTDAG--ERVKLLEKEADRLLDKLKPIKELQDNLGK 2112
Cdd:PRK01156 432 IRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKSRleEKIREIEIEVKDIDEKIVDLKKRKEYLES 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2113 niSQIKELINQ------ARKQANSIKVSVSSGGDciRTYKPDIKKGRYNTI---ILNVKTSTPDNLLFYLGSnkfTDFLA 2183
Cdd:PRK01156 512 --EEINKSINEynkiesARADLEDIKIKINELKD--KHDKYEEIKNRYKSLkleDLDSKRTSWLNALAVISL---IDIET 584
|
570 580 590
....*....|....*....|....*....|....*
gi 2019522063 2184 IEMRKGKVNF-LWDVGSGVGRVEypnLDINDDSWY 2217
Cdd:PRK01156 585 NRSRSNEIKKqLNDLESRLQEIE---IGFPDDKSY 616
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1055-1097 |
1.58e-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: 1.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2019522063 1055 ACDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGYRNYP 1097
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-794 |
3.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2019522063 753 CRCFGH---SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTD 794
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1602-1862 |
3.96e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1602 SIENETQELKhllspqrapERLLQLaqNNQ--------DTLVIEIDELLNRAAKVSADgeqtgKDAErtNERAKQLKNFV 1673
Cdd:COG1340 19 ELREEIEELK---------EKRDEL--NEElkelaekrDELNAQVKELREEAQELREK-----RDEL--NEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1674 KDILQTSKDIYDKAVKLNETLGIQNKtLEKSLQELQKDVDKmmaeLRRR-----MFKNQEKAAADELKAAEGLLNRVKKL 1748
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNK-AGGSIDKLRKEIER----LEWRqqtevLSPEEEKELVEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1749 fqdphnktndlnLEVKDKLRHFQDKLEDVLDMLREARGKIREsnhLSA-INKHnmtalegHKQAVEKgKKETENTLNESD 1827
Cdd:COG1340 156 ------------LEKNEKLKELRAELKELRKEAEEIHKKIKE---LAEeAQEL-------HEEMIEL-YKEADELRKEAD 212
|
250 260 270
....*....|....*....|....*....|....*
gi 2019522063 1828 DIMTEVNNLAQNINEAENELMDINKELPQLTERLN 1862
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1411-1448 |
4.00e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2019522063 1411 CQCNG---HSDMCDPQTSVCQaCKHNTTGDHCEWCAPGFYG 1448
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1518-1555 |
4.17e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.17e-08
10 20 30
....*....|....*....|....*....|....*...
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRH 1555
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1708-2133 |
4.51e-08 |
|
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: 59.31 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1708 LQKDVDKM--MAELRRRM----------FKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTNDLNLEVKDKLRHfqdklE 1775
Cdd:TIGR02169 140 LQGDVTDFisMSPVERRKiideiagvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY-----Q 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1776 DVLDMLREARGKIresnHLSAINkhnmtALEGHKQAVEKGKKETENtlnESDDIMTEVNNLAQNINEAENELMDINKELP 1855
Cdd:TIGR02169 215 ALLKEKREYEGYE----LLKEKE-----ALERQKEAIERQLASLEE---ELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1856 QLTE----RLNVKINNLTDEI------------QTRDLPEQVLQAELHAAQLTESSRMLDGILAEAKnlsLNATAAFNAY 1919
Cdd:TIGR02169 283 DLGEeeqlRVKEKIGELEAEIaslersiaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEER---KRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1920 SNIKKLIDnaddaakeakakaneavELVTgpqgPLKDKAKSFiQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQnadek 1999
Cdd:TIGR02169 360 AELKEELE-----------------DLRA----ELEEVDKEF-AETRDELKDYREKLEKLKREINELKRELDRLQ----- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2000 nvnlvralnDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNLNLLGLK-------QNYSALKEDVAKTNa 2072
Cdd:TIGR02169 413 ---------EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlskyeQELYDLKEEYDRVE- 482
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 2073 vvkvDNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNIS----QIKELINQARKQANSIKV 2133
Cdd:TIGR02169 483 ----KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgTVAQLGSVGERYATAIEV 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1660-1927 |
7.95e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1660 ERTNERAKQLKNFVKDILQTSKDIY--------DKAVKLNETLgIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKaa 1731
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLvlrleelrEELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVSELEEE-- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1732 adelkaaeglLNRVKKLFQDPHNKTNDLNLEV---KDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHN----MTA 1804
Cdd:TIGR02168 283 ----------IEELQKELYALANEISRLEQQKqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1805 LEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLT---ERLNVKINNLTDEIQTrdlpeqv 1881
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEE------- 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2019522063 1882 LQAELHAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLID 1927
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
408-459 |
8.44e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.82 E-value: 8.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 408 PCNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYP 459
Cdd:cd00055 1 PCDCNGHGSLSGQC---------DPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1636-1916 |
9.82e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1636 IEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLEK------SLQELQ 1709
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1710 KDVDKMMAELRRRMFKNQEKAAADELKAA------EGLLNRVKKL------FQDPHNKTNDLNLEVKDKLRHFQDKLEDV 1777
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEeleaqiEQLKEELKALrealdeLRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1778 LDMLREARGKIRESNHLSAINKHNMTALEghkQAVEKGKKETENTLNESDDIMTEVN-------NLAQNINEAENELMDI 1850
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELE---ELIEELESELEALLNERASLEEALAllrseleELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1851 NKELPQLTERLN----------VKINNLTDEIQTR------DLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLNATA 1914
Cdd:TIGR02168 914 RRELEELREKLAqlelrlegleVRIDNLQERLSEEysltleEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE 993
|
..
gi 2019522063 1915 AF 1916
Cdd:TIGR02168 994 EY 995
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1809-2127 |
1.10e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1809 KQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTER---LNVKINNLTDEIQTRDLPEQVLQAE 1885
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1886 LHAA----------------QLTESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLIDNADDAakeakakaneavelvtg 1949
Cdd:TIGR02168 777 LAEAeaeieeleaqieqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR----------------- 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1950 pqgpLKDKAKSFIQKSFRVhTDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLSAipndtivKIQTAK 2029
Cdd:TIGR02168 840 ----LEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE-------ELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2030 DKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKE----------DVAKTNAVVKVDNVTDAGERVKLLEKEADRL--- 2096
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeysltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpv 987
|
330 340 350
....*....|....*....|....*....|....*
gi 2019522063 2097 ----LDKLKPIKELQDNLGKnisQIKELiNQARKQ 2127
Cdd:TIGR02168 988 nlaaIEEYEELKERYDFLTA---QKEDL-TEAKET 1018
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1518-1558 |
1.26e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRHVRE 1558
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
2.06e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.06e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2019522063 861 CQCNdnLDLSAPGCCDSETGECRiCKPGVTGEYCNTCSEGYFGN 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1518-1557 |
2.24e-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: 2.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2019522063 1518 CECNPYGSLSMICHPSTGQCTCKPEATGLKCGGCTDRHVR 1557
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1099 |
2.38e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 1056 CDCGGPGSLSTQCNADTGCCFCRPNFSGDKCTSCRVGY--RNYPHC 1099
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
2.68e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 2.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2019522063 753 CRC--FGH-SDSCDDITGFCKnCKHNTYGRYCDYCLPGFYGNPTDG 795
Cdd:smart00180 1 CDCdpGGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1664-2120 |
4.26e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1664 ERA-KQLKNFVKDIlQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRrmfknqekaAADELKAAEGLL 1742
Cdd:PRK03918 161 ENAyKNLGEVIKEI-KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE---------LREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1743 NRVKKLFqdphNKTNDLNLEV----------KDKLRHFQDKLEDVLDMLREARGKIRESNHL-------SAINKHNMTAL 1805
Cdd:PRK03918 231 KELEELK----EEIEELEKELeslegskrklEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1806 EGhKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLT------ERLNVKINNLtDEIQTR--DL 1877
Cdd:PRK03918 307 DE-LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEEL-ERLKKRltGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1878 PEQVLQAELHAAQL--TESSRMLDGILAEAKNLSlnataafnaySNIKKLIDNaddaakeakakaneaVELVTGPQG--- 1952
Cdd:PRK03918 385 TPEKLEKELEELEKakEEIEEEISKITARIGELK----------KEIKELKKA---------------IEELKKAKGkcp 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1953 ----PLKDKAKSFIQKSFRvhtdaktqsLDLKEKENELAAMKDKLQNADEKNVNLVRALNdtlGKLSAIPNDTIVK-IQT 2027
Cdd:PRK03918 440 vcgrELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLK---KESELIKLKELAEqLKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2028 AKDKVKQANdtANDVLARIKD---LNLNLLGLKQNYSALKEDVAKTNAVVKvdnvtdageRVKLLEKEADRLLDKLKPIK 2104
Cdd:PRK03918 508 LEEKLKKYN--LEELEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKK---------KLAELEKKLDELEEELAELL 576
|
490
....*....|....*.
gi 2019522063 2105 ELQDNLGknISQIKEL 2120
Cdd:PRK03918 577 KELEELG--FESVEEL 590
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
464-510 |
1.03e-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: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2019522063 464 CNCSVPGSINeDPCVD---PCICKENVAGNNCDVCKHSYFNLKRDNPRGC 510
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1602-2149 |
1.13e-06 |
|
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: 55.06 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1602 SIENETQELKHLlspqRAPERLLQLAQNNQDTlvieIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSK 1681
Cdd:TIGR01612 905 SIEEEYQNINTL----KKVDEYIKICENTKES----IEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKI 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1682 DIYDKAVKlnetlgiqnktlEKSLQELQKDVDKMMA---ELRRRMFKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTND 1758
Cdd:TIGR01612 977 NELDKAFK------------DASLNDYEAKNNELIKyfnDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPN 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1759 LNLEVKDKLRHFQDKLEDVLDMLREARGK-IRESNHLSAINKHNMTALEGHKQAVEKGKKETENTLNESDDIMTEVNNLA 1837
Cdd:TIGR01612 1045 IEIAIHTSIYNIIDEIEKEIGKNIELLNKeILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLD 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1838 QNINEAENELMDINKELPQLTERLNVKINNLTDeiqtrdlpeqvlqaelhAAQLTESSRMLDGILAEAKNLSLNATAAFN 1917
Cdd:TIGR01612 1125 QKIDHHIKALEEIKKKSENYIDEIKAQINDLED-----------------VADKAISNDDPEEIEKKIENIVTKIDKKKN 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1918 AYSNIKKLIDN-ADDAAKEAKAKANEAVELVTGpqgplKDKAKSFIQKsfrvhTDAKTqsldlKEKENELAAMKDKLQNA 1996
Cdd:TIGR01612 1188 IYDEIKKLLNEiAEIEKDKTSLEEVKGINLSYG-----KNLGKLFLEK-----IDEEK-----KKSEHMIKAMEAYIEDL 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1997 DEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDvlARIKDLNLNLLGLKQNYSAlKEDVAKTNAVVKv 2076
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIEDFSE-ESDINDIKKELQ- 1328
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 2077 DNVTDAGERvkllEKEADRLLDKLKPIKEL--QDNLGKNISQIKELINQARKQANSIKVSVSSGGDCIRTYKPDI 2149
Cdd:TIGR01612 1329 KNLLDAQKH----NSDINLYLNEIANIYNIlkLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1657-2113 |
1.31e-06 |
|
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: 54.67 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1657 KDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNeTLGIQNKTLEKSLQELQKDVDKMMaELRRRMFKNQekAAADEL- 1735
Cdd:TIGR01612 565 KELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYIN-KLKLELKEKIKNISDKNEYIKKAI-DLKKIIENNN--AYIDELa 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1736 -----------KAAEGLLNRVK----KLFQDP----HN------KTNDL-NLEVKDKLRHFQDKLEDVLDMLREARGKIR 1789
Cdd:TIGR01612 641 kispyqvpehlKNKDKIYSTIKselsKIYEDDidalYNelssivKENAIdNTEDKAKLDDLKSKIDKEYDKIQNMETATV 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1790 ESnHLSAI--NKHNMTALeghkqAVEKGK---KETENTLNES-DDIMTEVNNLAQNINEAENELMDINKELPQLTE---R 1860
Cdd:TIGR01612 721 EL-HLSNIenKKNELLDI-----IVEIKKhihGEINKDLNKIlEDFKNKEKELSNKINDYAKEKDELNKYKSKISEiknH 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1861 LNVKINnlTDEIQTRDLPEQVLQAELHAAQLTESSRMLDGILAEAKNLS---LNATAAF-NAYSNIKKLIDNaddaakea 1936
Cdd:TIGR01612 795 YNDQIN--IDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddfLNKVDKFiNFENNCKEKIDS-------- 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1937 kaKANEAVELVTGPQGPLKDKAKSFIQKSFRvhtdaktqslDLKEKENELAAMKDKlqnaDEKNVNLVRALNDTLgklsA 2016
Cdd:TIGR01612 865 --EHEQFAELTNKIKAEISDDKLNDYEKKFN----------DSKSLINEINKSIEE----EYQNINTLKKVDEYI----K 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2017 IPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNLnllgLKQNYSAlKEDVAKTNAVVKVDNV-TDAGerVKLLEKEADR 2095
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNL----IEKSYKD-KFDNTLIDKINELDKAfKDAS--LNDYEAKNNE 997
|
490
....*....|....*...
gi 2019522063 2096 LldkLKPIKELQDNLGKN 2113
Cdd:TIGR01612 998 L---IKYFNDLKANLGKN 1012
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
409-459 |
1.36e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 409 CNCDPIGSLQDLCvkdkkeateDLLPGSCYCKPGYAGEKCNQCDLGYKGYP 459
Cdd:smart00180 1 CDCDPGGSASGTC---------DPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
818-859 |
1.57e-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: 47.35 E-value: 1.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2019522063 818 CHLDPTRGLVCDA------CPPGYTGLRCERCANGYFGQPSLPGGsCQ 859
Cdd:cd00055 4 CNGHGSLSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
803-858 |
1.59e-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: 1.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2019522063 803 CACPMSIASnnfSPTCHLdptRGLVCDaCPPGYTGLRCERCANGYFGQPSLPGGSC 858
Cdd:pfam00053 1 CDCNPHGSL---SDTCDP---ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1629-2130 |
1.94e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1629 NNQDTLVIEIDEL--LNRAAKVSADGEQTGKDA-----ERTNE------RAKQLKNFVKDILQTSKDIYDKAVKLNETLG 1695
Cdd:PTZ00440 460 NQLKTLISIMKSFydLIISEKDSMDSKEKKESSdsnyqEKVDEllqiinSIKEKNNIVNNNFKNIEDYYITIEGLKNEIE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1696 IQNKTLEKSLQELQKDVDKmmaELRRRMFKNQEKA-------AADELKAAEGLLNRVKKLFQDPHNKTNDlNLEVKDKLR 1768
Cdd:PTZ00440 540 GLIELIKYYLQSIETLIKD---EKLKRSMKNDIKNkikyieeNVDHIKDIISLNDEIDNIIQQIEELINE-ALFNKEKFI 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1769 H----FQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGH-KQAVEKGKKETENTLNE-----SDDIMTEVNNL-- 1836
Cdd:PTZ00440 616 NekndLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKsKEDLQTLLNTSKNEYEKlefmkSDNIDNIIKNLkk 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1837 -AQNINEAENELMD-----INKELPQLTERLNVKINNLTDEIQTRDLPEQVLqaELHAAQLTESSRML-------DGILA 1903
Cdd:PTZ00440 696 eLQNLLSLKENIIKkqlnnIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKL--EVYKHQIINRKNEFilhlyenDKDLP 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1904 EAKNLSLNATAAFNAYSNIKKLIDNADDAAKEAKAKAneavelvtgpqgplKDKAKSF---IQKsFRVHTDAKTQSL-DL 1979
Cdd:PTZ00440 774 DGKNTYEEFLQYKDTILNKENKISNDINILKENKKNN--------------QDLLNSYnilIQK-LEAHTEKNDEELkQL 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1980 KEKENElaamKDKLQNADEknvnLVRALNDTLGKLSAIPNDtIVKIQTAKDKVKQANDTANdvlaRIKDLNLNLLGLKQN 2059
Cdd:PTZ00440 839 LQKFPT----EDENLNLKE----LEKEFNENNQIVDNIIKD-IENMNKNINIIKTLNIAIN----RSNSNKQLVEHLLNN 905
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 2060 YSALKEDVAKTNAVVKVDNVTDAGERVKL---LEKEADRLLDKLKPIKelQDNLGKNISQIKELINQARKQANS 2130
Cdd:PTZ00440 906 KIDLKNKLEQHMKIINTDNIIQKNEKLNLlnnLNKEKEKIEKQLSDTK--INNLKMQIEKTLEYYDKSKENING 977
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1660-2171 |
2.26e-06 |
|
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: 53.90 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1660 ERTNERAKQLKNfVKDILQTSKDIYdKAVKLNETLGIQNKTLEKSLQElqKDVD---KMMAELRRRMFkNQEKAAADELK 1736
Cdd:TIGR01612 1369 EYTKEIEENNKN-IKDELDKSEKLI-KKIKDDINLEECKSKIESTLDD--KDIDeciKKIKELKNHIL-SEESNIDTYFK 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1737 AAEGLLNRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKireSNHLSAINKHNMTALEGHKQAVEKGK 1816
Cdd:TIGR01612 1444 NADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDK---SKGCKDEADKNAKAIEKNKELFEQYK 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1817 KETENTLNESDDIMTEvNNLAQNINEAE---NELMDINKELPQLTERLNVKINNLTDEiqtrdlpeqVLQAELHAAQLTE 1893
Cdd:TIGR01612 1521 KDVTELLNKYSALAIK-NKFAKTKKDSEiiiKEIKDAHKKFILEAEKSEQKIKEIKKE---------KFRIEDDAAKNDK 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1894 SSRMLDGILAEAKNLSlnatAAFNAYSNIKKLI----------------------DNADDAAKEAKAKANEAVELVTGPQ 1951
Cdd:TIGR01612 1591 SNKAAIDIQLSLENFE----NKFLKISDIKKKIndclketesiekkissfsidsqDTELKENGDNLNSLQEFLESLKDQK 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1952 GPLKDKAK------SFIQK-SFRVHTDAKTQSLDLKEKENELA-AMKDKLQNADEknvnlvrALNDTLGKLSAIPNDTIV 2023
Cdd:TIGR01612 1667 KNIEDKKKeldeldSEIEKiEIDVDQHKKNYEIGIIEKIKEIAiANKEEIESIKE-------LIEPTIENLISSFNTNDL 1739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2024 KIQTAKDKVKQANDTANDVLAR-IKDLNLNLLGLKqnySALKEDVakTNAVVKVDNVTDAGERVKLLEKEadrlldklKP 2102
Cdd:TIGR01612 1740 EGIDPNEKLEEYNTEIGDIYEEfIELYNIIAGCLE---TVSKEPI--TYDEIKNTRINAQNEFLKIIEIE--------KK 1806
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 2103 IKELQDNLgkNISQIKELINQARKQANSIKVSVSSGGDCIRTYKPDIKKGryntiILNVKTSTPDNLLF 2171
Cdd:TIGR01612 1807 SKSYLDDI--EAKEFDRIINHFKKKLDHVNDKFTKEYSKINEGFDDISKS-----IENVKNSTDENLLF 1868
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1970-2137 |
2.42e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1970 TDAKTQSLDLKEKENELAAMKDKL-QNADEKNvNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKD 2048
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELaEKRDELN-AQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2049 L---NLNLLGLKQNYSALKEDVAK-----TNAVVKVDNVTDAGERVKLLEKEADRL---LDKLKPIKELQ---DNLGKNI 2114
Cdd:COG1340 97 LrkeLAELNKAGGSIDKLRKEIERlewrqQTEVLSPEEEKELVEKIKELEKELEKAkkaLEKNEKLKELRaelKELRKEA 176
|
170 180
....*....|....*....|...
gi 2019522063 2115 SQIKELINQARKQANSIKVSVSS 2137
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIE 199
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1624-2132 |
3.11e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 53.30 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1624 LQLAQNNQDTLVIEIDELLNRAAkvsADGEQTGKDAERTNERAKQ-LKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLE 1702
Cdd:PTZ00440 586 IISLNDEIDNIIQQIEELINEAL---FNKEKFINEKNDLQEKVKYiLNKFYKGDLQELLDELSHFLDDHKYLYHEAKSKE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1703 KsLQELQKDVDKMMAELrrrmfknqEKAAADELkaaEGLLNRVKKLFQdphnktNDLNLE---VKDKLRHFQDKLEDVLD 1779
Cdd:PTZ00440 663 D-LQTLLNTSKNEYEKL--------EFMKSDNI---DNIIKNLKKELQ------NLLSLKeniIKKQLNNIEQDISNSLN 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1780 MLREARGKIResnhlSAIN--KHNMTALEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQL 1857
Cdd:PTZ00440 725 QYTIKYNDLK-----SSIEeyKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1858 TERLNVKINNLTDEIQTRDLPEQVLQA--ELHAAQLTESsrmLDGILAEAKNLSLNA-TAAFN----AYSNIKKLIDNAD 1930
Cdd:PTZ00440 800 INILKENKKNNQDLLNSYNILIQKLEAhtEKNDEELKQL---LQKFPTEDENLNLKElEKEFNennqIVDNIIKDIENMN 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1931 D---------AAKEAKAKANEAVELVTGPQGPLKDKAKSFIQKsfrVHTDaktQSLDLKEKENelaaMKDKLqNADEKNV 2001
Cdd:PTZ00440 877 KniniiktlnIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKI---INTD---NIIQKNEKLN----LLNNL-NKEKEKI 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2002 NlvRALNDT-LGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKD----LNLNLLGLKQNYSALKedvAKTNAVVK- 2075
Cdd:PTZ00440 946 E--KQLSDTkINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILN---KKIDDLIKk 1020
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2076 --------VDN-VTDAG----ERVKLLEKEADRLLDKLKP------IKELQDNLGKNisQIKEL----------INQARK 2126
Cdd:PTZ00440 1021 qhddiielIDKlIKEKGkeieEKVDQYISLLEKMKTKLSSfhfnidIKKYKNPKIKE--EIKLLeekveallkkIDENKN 1098
|
....*.
gi 2019522063 2127 QANSIK 2132
Cdd:PTZ00440 1099 KLIEIK 1104
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1668-2151 |
3.48e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1668 QLKNFVKDILQTSKDIYDKAVKLNETLGiQNKTLEKSLQELQKDVDKMMAELRRRMFK-------NQEKAAADELKAAEG 1740
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLK-EIERLSIEYNNAMDDYNNLKSALNELSSLedmknryESEIKTAESDLSMEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1741 LLNRVKKLFQDPHNK-TNDLNLEVKDKLR-HFQDK--LEDVLDMLREARGKIreSNHLSAINKhnMTALEGHKQAVEKGK 1816
Cdd:PRK01156 270 EKNNYYKELEERHMKiINDPVYKNRNYINdYFKYKndIENKKQILSNIDAEI--NKYHAIIKK--LSVLQKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1817 KETENTLNESDDIMTEVNNLAQNINEAENELMDINKElpqlterlNVKINNLTDEIqTRDLPEQVLQAELHAAQLTESSR 1896
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY--------SKNIERMSAFI-SEILKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1897 MLDGIlaEAKNLSLNAT---------------AAFNAYS---------------NIKKLIDNADDAAKEAKAKANEAVEL 1946
Cdd:PRK01156 417 KLQDI--SSKVSSLNQRiralrenldelsrnmEMLNGQSvcpvcgttlgeeksnHIINHYNEKKSRLEEKIREIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1947 VTGPQGPLKdKAKSFIQK--------SFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEK----NVNLVRALN-DTLGK 2013
Cdd:PRK01156 495 IDEKIVDLK-KRKEYLESeeinksinEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslKLEDLDSKRtSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2014 LSAIPNDTIVKIQTAKDKVKQandTANDVLARIKDLNLNLLGLKQ-NYSALKEDVAKTNAVV-KVDNVTDAGERVKLLEK 2091
Cdd:PRK01156 574 LAVISLIDIETNRSRSNEIKK---QLNDLESRLQEIEIGFPDDKSyIDKSIREIENEANNLNnKYNEIQENKILIEKLRG 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 2092 EADRLLDKLKPIKELQDNLGK---NISQIKELINQARKQANSIKVSVSSGGDCIRTYKPDIKK 2151
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1685-2132 |
3.94e-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: 53.05 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1685 DKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRmfKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTNDLNLE-- 1762
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKE--KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRsq 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1763 -VKDKLRHFQDKLEDVldmlreargkiresnhlsainKHNMTALEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNIN 1841
Cdd:TIGR00618 205 lLTLCTPCMPDTYHER---------------------KQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1842 EAENELMDINKELPQLtERLNVKINnltdeiqtrdLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSN 1921
Cdd:TIGR00618 264 QLRARIEELRAQEAVL-EETQERIN----------RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1922 IKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDKAKSFIQKSFRVHTDAKTQSLD-LKEKENELAAMKDKLQNADEKN 2000
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTtLTQKLQSLCKELDILQREQATI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2001 VNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNlnllGLKQNYSALKEDVA-KTNAVVKVDNV 2079
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ----ESAQSLKEREQQLQtKEQIHLQETRK 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2080 TDAGERVKLLEKEADRLLDK--LKPIKELQD--NLGKNISQIKELINQARKQANSIK 2132
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGscIHPNPARQDidNPGPLTRRMQRGEQTYAQLETSEE 545
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1767-1927 |
4.48e-06 |
|
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: 50.87 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1767 LRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGH-----KQAV------EKGKKETENTLNESDDIMTEVNN 1835
Cdd:pfam06008 14 PYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQEteelqKKATqtlakaQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1836 LAQNINEAENELMDINKELPQLT----ERLNVKINNLTDEIQTRDL--PEQVLQAELHAAQ--LTESSRMLDGILAEAKN 1907
Cdd:pfam06008 94 LIDNIKEINEKVATLGENDFALPssdlSRMLAEAQRMLGEIRSRDFgtQLQNAEAELKAAQdlLSRIQTWFQSPQEENKA 173
|
170 180
....*....|....*....|
gi 2019522063 1908 LSLNATAAFNAYSNikKLID 1927
Cdd:pfam06008 174 LANALRDSLAEYEA--KLSD 191
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
282-329 |
5.24e-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: 45.81 E-value: 5.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 282 CICYGHA---RSCpwDPKTNKssCECEHNTCGHSCDRCCPGFHQKPWRAGT 329
Cdd:cd00055 2 CDCNGHGslsGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
5.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 5.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2019522063 803 CACPmsiASNNFSPTCHLDptrGLVCDaCPPGYTGLRCERCANGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1978-2132 |
6.83e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1978 DLKEKENELAAMKDKLQNADEKnvnlVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNlNLLG-- 2055
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-EELGer 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2056 LKQNYSAlKEDVAKTNAVVKVDNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNISQIKELINQARKQANSIK 2132
Cdd:COG3883 92 ARALYRS-GGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1667-2142 |
7.13e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1667 KQLKNFVKDILQTSKDI--YDKAVKLNETLGIQNKTLEKSLQELQKDVDKMmAELRrrmfknqekaaaDELKAAEGLLNR 1744
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIkaLETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-CEIR------------DQITSKEAQLES 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1745 VKKLfqdphnktndlnleVKDKlrhfqdklEDVLDMLREARGKIRESnhLSAINKhnmtaLEGHKQAVEKGKKETENTLN 1824
Cdd:TIGR00606 236 SREI--------------VKSY--------ENELDPLKNRLKEIEHN--LSKIMK-----LDNEIKALKSRKKQMEKDNS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1825 ESDDIMTEV--------NNLAQN----INEAENELMDINKELPQLTER---LNVKINNLTDEIQTRDLpeqvlQAELHAA 1889
Cdd:TIGR00606 287 ELELKMEKVfqgtdeqlNDLYHNhqrtVREKERELVDCQRELEKLNKErrlLNQEKTELLVEQGRLQL-----QADRHQE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1890 QltesSRMLDG-ILAEAKNLSLNAtaaFNAYSNIKKLIDNADDAAKEAKAKANEAV-ELVTGPQGPLKDKAKSFIQKSFR 1967
Cdd:TIGR00606 362 H----IRARDSlIQSLATRLELDG---FERGPFSERQIKNFHTLVIERQEDEAKTAaQLCADLQSKERLKQEQADEIRDE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1968 VHTDAKT---QSLDLKEKENELAAMKDKLQNAD---EKNVNLVRALNDTLGKLSAIPNDTIVKIQTAK-----------D 2030
Cdd:TIGR00606 435 KKGLGRTielKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERELSKAEKNSLTETLKKEvkslqnekadlD 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2031 KVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVKVDNVTDAGE--RVKLLEKEADRLLDKLKPIKELQD 2108
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLA 594
|
490 500 510
....*....|....*....|....*....|....
gi 2019522063 2109 NLGKNISQIKELINQARKQANSIKVSVSSGGDCI 2142
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1624-2163 |
8.36e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.14 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1624 LQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKavKLNET----LGIQ-N 1698
Cdd:PTZ00440 885 LNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEK--QLSDTkinnLKMQiE 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1699 KTLE---KSLQELQKDVDKMMAELrrrmfkNQEKaaaDELKAAEGLLNRVKKLFQDPHNKTNDLNLE------------V 1763
Cdd:PTZ00440 963 KTLEyydKSKENINGNDGTHLEKL------DKEK---DEWEHFKSEIDKLNVNYNILNKKIDDLIKKqhddiielidklI 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1764 KDKLRHFQDKLEDVLDMLREARGKIRE-------SNHLSAINKHNMTALEGHKQAVEKGKKETENTLNE----SDDIMTE 1832
Cdd:PTZ00440 1034 KEKGKEIEEKVDQYISLLEKMKTKLSSfhfnidiKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEiknkSHEHVVN 1113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1833 VNNLAQNINEAEN----ELMDINKELPQLTERLNVKINNLT--DEIQTRDLPEQVLQAELHAAQLTESSRMLDGILAEAK 1906
Cdd:PTZ00440 1114 ADKEKNKQTEHYNkkkkSLEKIYKQMEKTLKELENMNLEDItlNEVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIE 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1907 ----------------NLSLNATAAFNAY--------SNIKKLIDNADDAAKEAKAKANEAvELVTgpqgpLKDKAKSFI 1962
Cdd:PTZ00440 1194 sykkdidqvkknmskeRNDHLTTFEYNAYydkatasyENIEELTTEAKGLKGEANRSTNVD-ELKE-----IKLQVFSYL 1267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1963 QKsfrvhtdAKTQSLDLKEKENELAAMKDKLQ------------NADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKD 2030
Cdd:PTZ00440 1268 QQ-------VIKENNKMENALHEIKNMYEFLIsidsekilkeilNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKE 1340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2031 KVKQANDTANDvlARIKDLNLNLLGLKQNYSALKEDVAKTnavvkVDNVTDAGERVKLLEKEADRLLDK---LKPIKELQ 2107
Cdd:PTZ00440 1341 HKNKIYGSLED--KQIDDEIKKIEQIKEEISNKRKEINKY-----LSNIKSNKEKCDLHVRNASRGKDKidfLNKHEAIE 1413
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 2108 DNLGK--NISQIKELINQARK---QANSIKVSVSSGGDCIRTYKPDIKKGRYNTIILNVKT 2163
Cdd:PTZ00440 1414 PSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSILGKKT 1474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1643-1875 |
8.58e-06 |
|
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: 50.92 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1643 NRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNK---TLEKSLQELQKDVDKMMAEL 1719
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1720 RRrmfknQEKAAADELKAAE--GLLNRVKKLF--QDPHNKTNDLNLevkdkLRHFQDKLEDVLDMLREARGKIRESNhls 1795
Cdd:COG4942 100 EA-----QKEELAELLRALYrlGRQPPLALLLspEDFLDAVRRLQY-----LKYLAPARREQAEELRADLAELAALR--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1796 ainkhnmTALEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVKINNLTDEIQTR 1875
Cdd:COG4942 167 -------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1703-1873 |
1.00e-05 |
|
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: 49.54 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1703 KSLQELQKdVDKMMAELRRRMfknqeKAAADELKAAEGLLNRVKKLFQDPHNKTNDLNLEVKDKlrhfQDKLEDVLDMLR 1782
Cdd:COG1579 7 RALLDLQE-LDSELDRLEHRL-----KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1783 EARGKIresnhLSAINKHNMTALEGHKQAVEKGKKETENTLNEsddIMTEVNNLAQNINEAENELMDINKELPQLTERLN 1862
Cdd:COG1579 77 KYEEQL-----GNVRNNKEYEALQKEIESLKRRISDLEDEILE---LMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170
....*....|.
gi 2019522063 1863 VKINNLTDEIQ 1873
Cdd:COG1579 149 EELAELEAELE 159
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1663-2177 |
1.20e-05 |
|
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: 51.59 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1663 NERAKQlKNFVKDILQTSKDIYD----------KAVKLNETLGIQ-----NKTLEKSLQ-------ELQKDVDKMMAELR 1720
Cdd:TIGR01612 486 DENSKQ-DNTVKLILMRMKDFKDiidfmelykpDEVPSKNIIGFDidqniKAKLYKEIEaglkesyELAKNWKKLIHEIK 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1721 RRMFKNQEKAAADElKAAEGLLNRVKKLfQDPHNKTNDLNLEVKDKLRHFQDKLEDV---LDMlrearGKIRESNH---- 1793
Cdd:TIGR01612 565 KELEEENEDSIHLE-KEIKDLFDKYLEI-DDEIIYINKLKLELKEKIKNISDKNEYIkkaIDL-----KKIIENNNayid 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1794 -LSAINKHNMTALEGHKQAVEKGKKETENTLNEsDDIMTEVNNLAQNINEAENElmdiNKELPQLTERLNVKINNLTDEI 1872
Cdd:TIGR01612 638 eLAKISPYQVPEHLKNKDKIYSTIKSELSKIYE-DDIDALYNELSSIVKENAID----NTEDKAKLDDLKSKIDKEYDKI 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1873 Q---TRDLPEQVLQAELHAAQLT------------ESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLIDNADDAAKEAK 1937
Cdd:TIGR01612 713 QnmeTATVELHLSNIENKKNELLdiiveikkhihgEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIK 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1938 AKANEAVELVTGPQGPLK---DKAKSFIqKSFRVHTDAKTQSLdlkekeNELAAMKDKLQNADEKNVNL----VRALNDT 2010
Cdd:TIGR01612 793 NHYNDQINIDNIKDEDAKqnyDKSKEYI-KTISIKEDEIFKII------NEMKFMKDDFLNKVDKFINFenncKEKIDSE 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2011 LGKLSAIPNDtiVKIQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKedvaKTNAVVKV-DNVTDAGERVKll 2089
Cdd:TIGR01612 866 HEQFAELTNK--IKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLK----KVDEYIKIcENTKESIEKFH-- 937
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2090 ekeadrllDKLKPIKELqdnLGKNISQIKElinqarkqANSIKVSVSSGGDCIRTYKPDIKKGRYNTIILNVKTSTPDNL 2169
Cdd:TIGR01612 938 --------NKQNILKEI---LNKNIDTIKE--------SNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNEL 998
|
570
....*....|....*
gi 2019522063 2170 LFY-------LGSNK 2177
Cdd:TIGR01612 999 IKYfndlkanLGKNK 1013
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1599-1915 |
1.32e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.79 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1599 MLFSIENETQELKHLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQ 1678
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1679 TSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGLLNrvkklfQDPHNKTND 1758
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLT------VRIDVDSKD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1759 LNLEVKDKLRHFQDKLEDVLDMLREARGKIRE-SNHLSAINKHNMTALEGHKQAVEkgkkETENTLNEsddiMTE-VNNL 1836
Cdd:COG0840 236 EIGQLADAFNRMIENLRELVGQVRESAEQVASaSEELAASAEELAAGAEEQAASLE----ETAAAMEE----LSAtVQEV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1837 AQNINEAENELMDINkelpQLTERLNVKINNLTDEIQtrDLPEQVLQAELHAAQLTESSR-------MLDGIlAEAKN-L 1908
Cdd:COG0840 308 AENAQQAAELAEEAS----ELAEEGGEVVEEAVEGIE--EIRESVEETAETIEELGESSQeigeivdVIDDI-AEQTNlL 380
|
....*....
gi 2019522063 1909 SLNAT--AA 1915
Cdd:COG0840 381 ALNAAieAA 389
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1604-1885 |
1.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1604 ENETQELKHLLSPQRapERLLQLAQNN--------------------QDTLVIEIDELLNRAAKVSADGEQTGKDAERTN 1663
Cdd:PRK02224 271 EREREELAEEVRDLR--ERLEELEEERddllaeaglddadaeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1664 ERAKQLKnfvkdilQTSKDIYDKAVKLNETLGIQNKTLEKSlQELQKDVDKMMAELRRRmFKNqekaAADELKAAEGLLn 1743
Cdd:PRK02224 349 EDADDLE-------ERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRER-FGD----APVDLGNAEDFL- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1744 rvkklfqdphnktnDLNLEVKDKLRhfqDKLEDVLDMLREARGKIRESNHLSAINKHNMTA--LEG--HKQAVEKGKKET 1819
Cdd:PRK02224 415 --------------EELREERDELR---EREAELEATLRTARERVEEAEALLEAGKCPECGqpVEGspHVETIEEDRERV 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1820 ENTLNESDDIMTEVNNLAQNINEAEnELMDINKELpqltERLNVKINNLTDEIQTRD--LPEQVLQAE 1885
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAE-DLVEAEDRI----ERLEERREDLEELIAERRetIEEKRERAE 540
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1603-2163 |
1.65e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.99 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1603 IENETQELKHLLspqrapERLLQLAQNNQDtlviEIDELLNRAA--KVSADGEQtgkdaERTNERAKQLKNFVKDILQTS 1680
Cdd:PTZ00440 1075 IKEEIKLLEEKV------EALLKKIDENKN----KLIEIKNKSHehVVNADKEK-----NKQTEHYNKKKKSLEKIYKQM 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1681 KDIYDKAVKLNETLGIQNktlekslqelqkDVDKMMAELRRRMFKNQEKAAADELKAAEGLLNRVKKLFQDPHNKTNDLN 1760
Cdd:PTZ00440 1140 EKTLKELENMNLEDITLN------------EVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMS 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1761 LEVKDKLRHF-----QDKL----EDVLDMLREARGKIRESNH------LSAINKHNMTALEGHKQ---AVEKGKKETEN- 1821
Cdd:PTZ00440 1208 KERNDHLTTFeynayYDKAtasyENIEELTTEAKGLKGEANRstnvdeLKEIKLQVFSYLQQVIKennKMENALHEIKNm 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1822 ----TLNESDDIMTEVNNlaqNINEAENELMDINKELPqlterlnvKINNLTDEIQtrdlpEQVLQAELHAAQLTESSRM 1897
Cdd:PTZ00440 1288 yeflISIDSEKILKEILN---STKKAEEFSNDAKKELE--------KTDNLIKQVE-----AKIEQAKEHKNKIYGSLED 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1898 lDGILAEAKNLSL------NATAAFNAY-SNIKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDKAKSFIQKSFRVHT 1970
Cdd:PTZ00440 1352 -KQIDDEIKKIEQikeeisNKRKEINKYlSNIKSNKEKCDLHVRNASRGKDKIDFLNKHEAIEPSNSKEVNIIKITDNIN 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1971 DAKTQSLDLKEKENELAAMKDKLQNADEKNVNLvraLNDTLgkLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDL- 2049
Cdd:PTZ00440 1431 KCKQYSNEAMETENKADENNDSIIKYEKEITNI---LNNSS--ILGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSs 1505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2050 -NLNLLGLKQNYSALKEDVAktNAVVKVDNVTDA--GERVK-------LLEKEADRLLDK----LKPIKELQDNLG---- 2111
Cdd:PTZ00440 1506 eKLNQLNEQPNIKREGDVLN--NDKSTIAYETIQynLGRVKhnllnilNIKDEIETILNKaqdlMRDISKISKIVEnknl 1583
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019522063 2112 -----------KNISQI---KELINQARKQANSIKVSVSSGGDCIRTYKPDIKKGRYNTIILNVKT 2163
Cdd:PTZ00440 1584 enlndkeadyvKYLDNIlkeKQLMEAEYKKLNEIYSDVDNIEKELKKHKKNYEIGLLEKVIEINKN 1649
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1621-1852 |
2.17e-05 |
|
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: 49.29 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1621 ERLLQLAQNNQDTLVIEIDELLNRAAKVSadgEQTGKDAERTNERAKQLknfvkdilQTSKDIYDKavKLNETLGIQNKt 1700
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVV---DKLTDFENQTEKDQTAL--------ETLEKALKD--LLTDEGGAIAR- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1701 leKSLQELQKDVDKMMAELRRRMfKNQEKAAADELKAAEGLLNRVKKLFQDphnktndlnlevkdkLRHFQDKLEDVLDM 1780
Cdd:cd22656 179 --KEIKDLQKELEKLNEEYAAKL-KAKIDELKALIADDEAKLAAALRLIAD---------------LTAADTDLDNLLAL 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1781 LREArgkiresnhLSAINKhnmtaLEGHKQAVEkgkketentlNESDDIMTEVNNLAQNINEAENELMDINK 1852
Cdd:cd22656 241 IGPA---------IPALEK-----LQGAWQAIA----------TDLDSLKDLLEDDISKIPAAILAKLELEK 288
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1597-1864 |
2.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1597 YRMLFSIENETQELKHLLSPqRAPERL---LQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAER------------ 1661
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTG-LTPEKLekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcg 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1662 ---TNERAKQLKNF----VKDILQTSKDIYDKAVKLNETLgiqnKTLEKSLQEL-----QKDVDKMMAELRRRMFK-NQE 1728
Cdd:PRK03918 443 relTEEHRKELLEEytaeLKRIEKELKEIEEKERKLRKEL----RELEKVLKKEselikLKELAEQLKELEEKLKKyNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1729 KAAADElKAAEGLLNRVKKL------FQDPHNKTNDLN---LEVKDKLRHFQDKLEDVLDMLR--------EARGKIREs 1791
Cdd:PRK03918 519 ELEKKA-EEYEKLKEKLIKLkgeiksLKKELEKLEELKkklAELEKKLDELEEELAELLKELEelgfesveELEERLKE- 596
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019522063 1792 nhlsainkhnmtaLEG-HKQAVE--KGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVK 1864
Cdd:PRK03918 597 -------------LEPfYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1599-1887 |
2.51e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1599 MLFSIENE---------TQELKHLlspqrapERLLQLAQNNQDTLVIEIDELL-----NRAA-------------KVSAD 1651
Cdd:PRK04778 87 QLFEAEELndkfrfrkaKHEINEI-------ESLLDLIEEDIEQILEELQELLeseekNREEveqlkdlyrelrkSLLAN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1652 GEQTGkDAERTNEraKQLKNFVKDILQ-----------TSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELR 1720
Cdd:PRK04778 160 RFSFG-PALDELE--KQLENLEEEFSQfveltesgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1721 ---RRM----FKNQEKAAADELKAAEGLLNRVKKLFQdphnktnDLNL-EVKDKLRHFQDKLEDVLDMLR---EAR---- 1785
Cdd:PRK04778 237 agyRELveegYHLDHLDIEKEIQDLKEQIDENLALLE-------ELDLdEAEEKNEEIQERIDQLYDILErevKARkyve 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1786 ---GKIRES-NHLSAINKHNMTALEGHKQAVEKGKKETENT---LNESDDIMTEVNNLAQNINEAE-------NELMDIN 1851
Cdd:PRK04778 310 knsDTLPDFlEHAKEQNKELKEEIDRVKQSYTLNESELESVrqlEKQLESLEKQYDEITERIAEQEiayselqEELEEIL 389
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2019522063 1852 KELPQLT---ERLNVKINNL-TDEIQTRDLPEQvLQAELH 1887
Cdd:PRK04778 390 KQLEEIEkeqEKLSEMLQGLrKDELEAREKLER-YRNKLH 428
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1654-2101 |
2.68e-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: 50.21 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1654 QTGKDAERT---------NERAKQLKNFVKDI------LQTSKDIYDkaVKLNETLGIQNKTleKSLQELQKDVDKMMAE 1718
Cdd:pfam10174 344 QTEVDALRLrleekesflNKKTKQLQDLTEEKstlageIRDLKDMLD--VKERKINVLQKKI--ENLQEQLRDKDKQLAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1719 LRRRMFKNQ-------------EKAAADELKAAEGL---LNRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLR 1782
Cdd:pfam10174 420 LKERVKSLQtdssntdtalttlEEALSEKERIIERLkeqREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1783 EArgKIRESNHLSAINKHN--MTALEGhkqAVEKGKKE---TENTLNEsddimtevnnlAQNINEAEnelmdinkelpQL 1857
Cdd:pfam10174 500 DL--KEHASSLASSGLKKDskLKSLEI---AVEQKKEEcskLENQLKK-----------AHNAEEAV-----------RT 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1858 TERLNVKINNLTDEIQTRdlpeqvlQAELHAAQlTESSRMLdGILAEAKNlslnataafNAYSNIKKLIDNADDAAKEAK 1937
Cdd:pfam10174 553 NPEINDRIRLLEQEVARY-------KEESGKAQ-AEVERLL-GILREVEN---------EKNDKDKKIAELESLTLRQMK 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1938 AKANEAVELVTGPQGpLKDKAKSFIQKSFRVHTDAK--TQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLS 2015
Cdd:pfam10174 615 EQNKKVANIKHGQQE-MKKKGAQLLEEARRREDNLAdnSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLT 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2016 AIPNDTIVKIQTAKDKVKQAndtandVLARI--KDLNLNLLGLkqnySALKEdvaKTNAvvkvdnvtdagERVKLLEKEA 2093
Cdd:pfam10174 694 NLRAERRKQLEEILEMKQEA------LLAAIseKDANIALLEL----SSSKK---KKTQ-----------EEVMALKREK 749
|
....*...
gi 2019522063 2094 DRLLDKLK 2101
Cdd:pfam10174 750 DRLVHQLK 757
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1710-2101 |
2.79e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1710 KDVDKMMAELRRRmfKNQEKAAADELKAA-EGLLNRVKKLFQdphnKTNDLNLEVKdKLRhfqDKLEDVLDMLREARGKI 1788
Cdd:COG1340 4 DELSSSLEELEEK--IEELREEIEELKEKrDELNEELKELAE----KRDELNAQVK-ELR---EEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1789 REsnhlsainkhnmtalegHKQAvekgKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVKINNL 1868
Cdd:COG1340 74 KE-----------------LKEE----RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1869 TDEiqtRDLPEQV--LQAELHAAQ-LTESSRMLDGILAEAKNLSLNATAAFNaysNIKKLIDNaddaakeakakaneave 1945
Cdd:COG1340 133 EEE---KELVEKIkeLEKELEKAKkALEKNEKLKELRAELKELRKEAEEIHK---KIKELAEE----------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1946 lvtgpqgplkdkaksfIQKsfrvhtdAKTQSLDLKEKENELaamkdklqnadeknvnlvRALNDTLGKlsaipndtivKI 2025
Cdd:COG1340 190 ----------------AQE-------LHEEMIELYKEADEL------------------RKEADELHK----------EI 218
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019522063 2026 QTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKtnavvkvdnvtdagervKLLEKEADRLLDKLK 2101
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----------------EELEEKAEEIFEKLK 277
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1974-2132 |
3.13e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1974 TQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNLNL 2053
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2054 LGLKQNYSALKEDVAKTNAvvKVDNVTDAGERVKLLEKEADRLLDKL--KPI-KELQDNLGKNISQIKELIN---QARKQ 2127
Cdd:COG1340 81 DELNEKLNELREELDELRK--ELAELNKAGGSIDKLRKEIERLEWRQqtEVLsPEEEKELVEKIKELEKELEkakKALEK 158
|
....*
gi 2019522063 2128 ANSIK 2132
Cdd:COG1340 159 NEKLK 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1803-2040 |
3.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1803 TALEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTERlnvkINNLTDEIQTRdlpEQVL 1882
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEER---REEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1883 QAELHAAQLTESSRMLDGILAEAKNLSlnatAAFNAYSNIKKLIDNaddaakeakakANEAVELVTgpqgplKDKAKSFI 1962
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFS----DFLDRLSALSKIADA-----------DADLLEELK------ADKAELEA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1963 QKSfrvhtDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTAN 2040
Cdd:COG3883 148 KKA-----ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1804-2135 |
3.51e-05 |
|
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: 49.68 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1804 ALEGHKQAVEKGKKETENTLNESDDIMTEvnnLAQNINEAENELMDINKELPQLTERL----------NVKINNLTDEIQ 1873
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSD---ASRKIGEIEKEIEQLEQEEEKLKERLeeleedlsslEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1874 TRDLPEQVLQAELHA--AQLTESSRMLDGILAEAKNLSLNATAAfnAYSNIKKLIDNaddaakeakakaneaVELVTGPQ 1951
Cdd:TIGR02169 762 ELEARIEELEEDLHKleEALNDLEARLSHSRIPEIQAELSKLEE--EVSRIEARLRE---------------IEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1952 GPLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDK 2031
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2032 VKQANDTANDVLARIKDLNLNLLGLKQNYSAL-------KEDVAKTNAVVKVDNVTDA-GERVKLLE-------KEADRL 2096
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIedpkgedEEIPEEELSLEDVQAELQRvEEEIRALEpvnmlaiQEYEEV 984
|
330 340 350
....*....|....*....|....*....|....*....
gi 2019522063 2097 LDKLKPIKELQDNLGKNISQIKELINQARKQANSIKVSV 2135
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1604-1925 |
4.52e-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: 49.19 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1604 ENETQELKHL-LSPQRAPERLLQLAQNNQDTLVIEIDELLNR--AAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTS 1680
Cdd:COG5185 190 KGISELKKAEpSGTVNSIKESETGNLGSESTLLEKAKEIINIeeALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1681 -KDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGLLNR---VKKLFQDPHNKT 1756
Cdd:COG5185 270 lGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETetgIQNLTAEIEQGQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1757 NDL------------NLEVKDKLRHFQDKLEDVLDMLREargkIRESNHLSAINKHNMT-----ALEGHKQAVEKGKKET 1819
Cdd:COG5185 350 ESLtenleaikeeieNIVGEVELSKSSEELDSFKDTIES----TKESLDEIPQNQRGYAqeilaTLEDTLKAADRQIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1820 ENTLNESDDIMTEVNNLaqnINEAENEL----MDINKELPQLTERLNVKINNlTDEIQTRDLPEQVLQAELHAAQLTES- 1894
Cdd:COG5185 426 QRQIEQATSSNEEVSKL---LNELISELnkvmREADEESQSRLEEAYDEINR-SVRSKKEDLNEELTQIESRVSTLKATl 501
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2019522063 1895 -------SRMLDGI--LAEAKNLSLNATAAFNAYSNIKKL 1925
Cdd:COG5185 502 eklraklERQLEGVrsKLDQVAESLKDFMRARGYAHILAL 541
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1619-1893 |
4.53e-05 |
|
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: 49.40 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1619 APERLLQLAQNNQDTLVIEIDELLNRAAKVSADgeqtgkdaertnerakqlKNFVKDILQTSKDIYDKAVKLNETLGIQN 1698
Cdd:pfam01576 9 AKEEELQKVKERQQKAESELKELEKKHQQLCEE------------------KNALQEQLQAETELCAEAEEMRARLAARK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1699 KTLEKSLQELQKDVDK-------MMAElRRRMFKN---------QEKAAADELK----AAEGllnRVKKLFQD---PHNK 1755
Cdd:pfam01576 71 QELEEILHELESRLEEeeersqqLQNE-KKKMQQHiqdleeqldEEEAARQKLQlekvTTEA---KIKKLEEDillLEDQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1756 TNDLNLEVKdklrHFQDKLEDVLDMLREARGKIRESNHLSaiNKHN--MTALEGHKQAVEKGKKETENTLNESDdimTEV 1833
Cdd:pfam01576 147 NSKLSKERK----LLEERISEFTSNLAEEEEKAKSLSKLK--NKHEamISDLEERLKKEEKGRQELEKAKRKLE---GES 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 1834 NNLAQNINEAENELMDINKELPQLTERLNVKINNLTDE-IQTRDLPEQVLQAELHAAQLTE 1893
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtAQKNNALKKIRELEAQISELQE 278
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1602-1868 |
4.66e-05 |
|
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: 49.25 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1602 SIENETQELKHLLSPQRAPERLLQ----LAQNNQDTLVIEIDELLNRAAKVSAD-GEQTGKDAERTNErAKQLKNFvKDI 1676
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDeqikKLQQEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKELI-IKNLDNT-RES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1677 LQTSKDIYDKAVKLNETlgiqnkTLEKSLQELQKDVDKMmaelrrRMFKNQEKAAADELK----AAEGLLNRVKKL---F 1749
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQ------NLEQKQKELKSKEKEL------KKLNEEKKELEEKVKdltkKISSLKEKIEKLeseK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1750 QDPHNKTNDLNLEV-KDKLRHFQDKLEDVLDMLREargKIRESnhlsainKHNMTALE-GHKQAVEKGKKETEntlnESD 1827
Cdd:TIGR04523 534 KEKESKISDLEDELnKDDFELKKENLEKEIDEKNK---EIEEL-------KQTQKSLKkKQEEKQELIDQKEK----EKK 599
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2019522063 1828 DIMTEVNNLAQNINEAENELMDINKElpqlTERLNVKINNL 1868
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKE----NEKLSSIIKNI 636
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1755-2112 |
4.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1755 KTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNhlsainkhnmTALEGHKQAVEKGKKETENTLNESDDIMTEVN 1834
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR----------EELEQLEEELEQARSELEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1835 NLAQNINEAENELMDINKELPQLT---ERLNVKINNLTDEIQTRDLPEQVLQAELHA--AQLTESSRMLDGILAEAKNL- 1908
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEreEELKELEEQLESLQEELAALe 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1909 -SLNATAAFNAYSNIKKLIDNADDAAKEAKakaneavELVTGPQGPLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELA 1987
Cdd:COG4372 171 qELQALSEAEAEQALDELLKEANRNAEKEE-------ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1988 AMKDKLQNADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDV 2067
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2019522063 2068 AKTNAVVKVDNVTDAGERVKLLEKEADRLLDKLKPIKELQDNLGK 2112
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1632-2131 |
4.87e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.44 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1632 DTLVIEIDELLNRAAKVSA-------DGEQT--GKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLG---IQNK 1699
Cdd:PTZ00440 2068 ESINPSLDELLKKGHKIEIsrytsiiDNVQTkiSNDSKNINDIEKKAQIYLAYIKNNYNSIKKDISTLNEYFDekqVSNY 2147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1700 TL------EKSLQELQK---DVDKMMAELRRRMFKNQEkaaADELKAAEGLLNRVKKLFQDPHNKTNDLNLEVK----DK 1766
Cdd:PTZ00440 2148 ILtnidkaNKLSSELSEavtNSEEIIENIKKEIIEINE---NTEMNTLENTADKLKELYENLKKKKNIINNIYKkinfIK 2224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1767 LRHFQDKLEDVLDmLREARGKIRESNHLS-AINKHNMTALEGHKQAVEKG--------KKETENTLNES-DDIMTEVNNL 1836
Cdd:PTZ00440 2225 LQEIENSSEKYND-ISKLFNNVVETQKKKlLDNKNKINNIKDKINDKEKElinvdssfTLESIKTFNEIyDDIKSNIGDL 2303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1837 A--QNINEAENELMDINKE-LPQLTERLNVKINNLTDEIQTRDLpeQVLQAEL------HAAQLTESSRMLDGILAEA-K 1906
Cdd:PTZ00440 2304 YklEDTNNDELKKVKLYIEnITHLLNRINTLINDLDNYQDENYG--KDKNIELnnennsYIIKTKEKINNLKEEFSKLlK 2381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1907 NLSLNATAAFNaySNIKKLIDNADDAAKEAKAKANEAvelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENEL 1986
Cdd:PTZ00440 2382 NIKRNNTLCNN--NNIKDFISNIGKSVETIKQRFSSN----------LPEKEKLHQIEENLNEIKNIMNETKRISNVDAF 2449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1987 AAMKDKLQNADEKNVNLVRALNDTlgklsaipNDTIVKIQTAKDKVKQANDTANDVLARIKDLNLNllgLKQNYSALKED 2066
Cdd:PTZ00440 2450 TNKILQDIDNEKNKENNNMNAEKI--------DDLIENVTSHNEKIKSELLIINDALRRVKEKKDE---MNKLFNSLTEN 2518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 2067 VAKTN--AVVKVDNVTDAgerVKLLEKEADRLLDKL----KPIKELQDNLGKNISQIKelINQARKQANSI 2131
Cdd:PTZ00440 2519 NNNNNnsAKNIVDNSTYI---INELESHVSKLNELLsyidNEIKELENEKLKLLEKAK--IEESRKERERI 2584
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1459-1516 |
5.75e-05 |
|
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: 42.73 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2019522063 1459 PCACPLHIASNnfsPTCIMQgtnDYRCTaCPQGYEGQYCERCASGYTGNPSIPGGsCQ 1516
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1653-1853 |
6.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1653 EQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLE--KSLQELQK--DVDKMMAELRRRMfKNQE 1728
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekKKAEELKKaeEENKIKAEEAKKE-AEED 1742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1729 KAAADELKAAEGLLNRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAI--NKHNMTALE 1806
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIegGKEGNLVIN 1822
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 1807 GHKQAVEKGKKETENT----LNESDDIMTEVNNLAQNINEAENELMDINKE 1853
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSknmqLEEADAFEKHKFNKNNENGEDGNKEADFNKE 1873
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1677-2108 |
8.34e-05 |
|
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: 48.68 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1677 LQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMfkNQEKAAADE-LKAAEGLLNRV---KKLFQDP 1752
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL--NGELSAADAaVAKDRSELEALedqHGAFLDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1753 HNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKI-RESNHL-SAINKHNMTALEGHKQAVEKGKKETENTLN-ESDDI 1829
Cdd:pfam12128 338 DIETAAADQEQLPSWQSELENLEERLKALTGKHQDVtAKYNRRrSKIKEQNNRDIAGIKDKLAKIREARDRQLAvAEDDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1830 MTEVNNLAQNINEAENELMDINKELPQLTERLNVKINNLTDEiqtrdlPEQVLQAE-----LHAAQLTESSRM-----LD 1899
Cdd:pfam12128 418 QALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT------PELLLQLEnfderIERAREEQEAANaeverLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1900 GILAEAKNLSLNATAAFNAYSnikklidnaddAAKEAKAKANEAVELVTGPQGP-----LKDKAKSFIQKSFRVHTDAKT 1974
Cdd:pfam12128 492 SELRQARKRRDQASEALRQAS-----------RRLEERQSALDELELQLFPQAGtllhfLRKEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1975 QSLDL--------KEKENELAAMKDKLQNADeknVNLVRALNDTL-GKLSAIPNDtivkIQTAKDKVKQANDTANDVLAR 2045
Cdd:pfam12128 561 HRTDLdpevwdgsVGGELNLYGVKLDLKRID---VPEWAASEEELrERLDKAEEA----LQSAREKQAAAEEQLVQANGE 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 2046 IKDLNLNLLGLKQNYSALKED-----VAKTNAVVKVDNVTD-----AGERVKLLEKEADRLLDKLKPIKELQD 2108
Cdd:pfam12128 634 LEKASREETFARTALKNARLDlrrlfDEKQSEKDKKNKALAerkdsANERLNSLEAQLKQLDKKHQAWLEEQK 706
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1641-1921 |
1.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1641 LLNRAAKVSADGEQTGKDAErTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGiQNKTLEKSLQELQKDVDKMMAELR 1720
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKE-LSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1721 RRMfknqekaaaDELKaaegllNRVKKLFQDPhNKTNDLN--LEVKDklrhfqdkLEDVLDmlreargkiRESNhLSAIN 1798
Cdd:COG3883 83 ERR---------EELG------ERARALYRSG-GSVSYLDvlLGSES--------FSDFLD---------RLSA-LSKIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1799 KHNMTALEGHKQA---VEKGKKETENTLNEsddimtevnnLAQNINEAENELmdinKELPQLTERLNVKINNLTDEIQTR 1875
Cdd:COG3883 129 DADADLLEELKADkaeLEAKKAELEAKLAE----------LEALKAELEAAK----AELEAQQAEQEALLAQLSAEEAAA 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2019522063 1876 DLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSN 1921
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
464-510 |
1.27e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 464 CNCSVPGSINeDPCvDP----CICKENVAGNNCDVCKHSYFNlkrDNPRGC 510
Cdd:smart00180 1 CDCDPGGSAS-GTC-DPdtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1598-2131 |
1.57e-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: 47.73 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1598 RMLFSIENETQELKHLLSPQRAPERLLQL-AQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERtnerakQLKNFVKDI 1676
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLqADRHQEHIRARDSLIQSLATRLELDGFERGPFSER------QIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1677 LQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRMFK-----NQEKAAADELKAAEGLLNRVKKLFQD 1751
Cdd:TIGR00606 400 IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIlekkqEELKFVIKELQQLEGSSDRILELDQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1752 PHNKTNDLNLEVKDKL--------RHFQDKLEDVLDMLREARGKIRESNH-------LSAINKHNMTALEGHKQAVEKG- 1815
Cdd:TIGR00606 480 LRKAERELSKAEKNSLtetlkkevKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqMEMLTKDKMDKDEQIRKIKSRHs 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1816 ------------KKETENTL----NESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVKINNLTD-------EI 1872
Cdd:TIGR00606 560 deltsllgyfpnKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgsqdeES 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1873 QTRDLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLNATAA----FNAYSNIKKLIDNADDAAKEAKAKANEAVELVT 1948
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvFQTEAELQEFISDLQSKLRLAPDKLKSTESELK 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1949 GpqgplKDKAKSFIQksfrVHTDAKTQSLDLKEKenELAAMKDKLQNAdekNVNLVRALNDtLGKlsaipNDTIvkIQTA 2028
Cdd:TIGR00606 720 K-----KEKRRDEML----GLAPGRQSIIDLKEK--EIPELRNKLQKV---NRDIQRLKND-IEE-----QETL--LGTI 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2029 KDKVKQANDTANDVlARIKDLNLNllgLKQNYSALKEDVAKTNAVVKVDNVTDAGERVKLLEKEADRLLDKLKPIKELQD 2108
Cdd:TIGR00606 778 MPEEESAKVCLTDV-TIMERFQME---LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
570 580
....*....|....*....|...
gi 2019522063 2109 NLGKNISQIKELINQARKQANSI 2131
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSEKLQI 876
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1602-2140 |
1.60e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.90 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1602 SIENETQELKHLLSpqraperLLQLaqNNQDTLVIEIdelLNRAAKVSADGEQTGKDAERTNERAKQLKNFVkDILQTSK 1681
Cdd:PTZ00440 1276 KMENALHEIKNMYE-------FLIS--IDSEKILKEI---LNSTKKAEEFSNDAKKELEKTDNLIKQVEAKI-EQAKEHK 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1682 DIYDKAVKlNETLGIQNKTLEKSLQELQKDVDKMMAELRRrMFKNQEKA-----AADELKAAEGLLNRvKKLFQDPHNKT 1756
Cdd:PTZ00440 1343 NKIYGSLE-DKQIDDEIKKIEQIKEEISNKRKEINKYLSN-IKSNKEKCdlhvrNASRGKDKIDFLNK-HEAIEPSNSKE 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1757 NDLNlEVKDKLRHFQDKLEDVLDMLREArgkirESNHLSAIN-KHNMTALEGHKQAVEKGKKeTENTLNESDDIMTEVNN 1835
Cdd:PTZ00440 1420 VNII-KITDNINKCKQYSNEAMETENKA-----DENNDSIIKyEKEITNILNNSSILGKKTK-LEKKKKEATNIMDDING 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1836 LAQNINEaenELMDINKELPQLTERLNVK-------------------------------INNLTDEIqtrdlpEQVLQA 1884
Cdd:PTZ00440 1493 EHSIIKT---KLTKSSEKLNQLNEQPNIKregdvlnndkstiayetiqynlgrvkhnllnILNIKDEI------ETILNK 1563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1885 elhAAQLTESSRMLDGILAEAKNLSLNataafNAYSNIKKLIDNADDAAKEAKAKANEAVEL---VTGPQGPLKDKAKSF 1961
Cdd:PTZ00440 1564 ---AQDLMRDISKISKIVENKNLENLN-----DKEADYVKYLDNILKEKQLMEAEYKKLNEIysdVDNIEKELKKHKKNY 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1962 -IQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQ----NADEKNVNLVRALNDTLGKLSAIPNDTIVKIQTAKDKVKQAN 2036
Cdd:PTZ00440 1636 eIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSslfnNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVS 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2037 DtandvlariKDLNLNLL-GLKQNysALKEDVaktNAVVKVDNVTDAGERVKllEKEADRLLDKlkpIKELQDNLGKNIS 2115
Cdd:PTZ00440 1716 N---------DDVDYNEAkTLREE--AQKEEV---NLNNKEEEAKKYLNDIK--KQESFRFILY---MKEKLDELSKMCK 1776
|
570 580
....*....|....*....|....*
gi 2019522063 2116 QIKELINQARKQANSIKVSVSSGGD 2140
Cdd:PTZ00440 1777 QQYNIVDEGYNYIKKKIEYIKTLND 1801
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1779-2127 |
1.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1779 DMLREARGKIRESnhLSAINKHNMTALEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLT 1858
Cdd:COG4372 2 DRLGEKVGKARLS--LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1859 ERLNvKINNltdEIQTRDLPEQVLQAELHAAQltessrmldgilAEAKNLSlnataafnaySNIKKLIDNaddaakeaka 1938
Cdd:COG4372 80 EELE-ELNE---QLQAAQAELAQAQEELESLQ------------EEAEELQ----------EELEELQKE---------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1939 kaneavelvtgpQGPLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLVRA-LNDTLGKLSAI 2017
Cdd:COG4372 124 ------------RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeAEQALDELLKE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2018 PNDTIVKIQT-AKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVKVDNVTDAGERVKLLEKEADRL 2096
Cdd:COG4372 192 ANRNAEKEEElAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
330 340 350
....*....|....*....|....*....|.
gi 2019522063 2097 LDKLKPIKELQDNLGKNISQIKELINQARKQ 2127
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
2961-3097 |
2.15e-04 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 44.66 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2961 DLLIELEFR-TTKTNGVLIGISGKkmDG---LGIEmVDG---KLLFHADNGAGRFTAVYEPEVPgsLCDGQWHKVTANKI 3033
Cdd:smart00210 53 DFSLLTTFRqTPKSRGVLFAIYDA--QNvrqFGLE-VDGranTLLLRYQGVDGKQHTVSFRNLP--LADGQWHKLALSVS 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 3034 KHRLEMIVDNKKVEASSPNAASTSTDTNDPVFVGGypedvkqFGLTTQVSFKGCIRDLKLAKGT 3097
Cdd:smart00210 128 GSSATLYVDCNEIDSRPLDRPGQPPIDTDGIEVRG-------AQAADRKPFQGDLQQLKIVCDP 184
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1582-2119 |
2.65e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1582 QMVMSVNLSGplpppyrmlFSIENETQ--ELKHLLSPQRAPERLLQLAQNNQ---DTLVIEIDEL-----LNRAAKVSAD 1651
Cdd:PTZ00440 1837 HVVKSANFIG---------IKIMTGLQptELTPDASLETAPELTFESENNSDlelDHLSSNKNELdvyknIQDAYKSSLQ 1907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1652 GEQTGKDAERTNERAKQLKNFVKDILQTSKDIYDKAVKLNETLGIQNKTLEK------SLQELQK------DVDKMMA-- 1717
Cdd:PTZ00440 1908 ILKYSDDIDKKQRDCNKLVEDGNEIYLKSTAINELKNMINSVKNKESAISNKidnvsnKLSELNKitcndeSYDEILEke 1987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1718 ---EL-RRRMFKNQEKAA-ADELKaaeglLNRVKKLFQDPHNKTNDLNLEVKDKLRHFQDKlEDVLDmlreargkirESN 1792
Cdd:PTZ00440 1988 eyeELkDLRNSFNQEKAEtLNNLK-----LNKIKEDFNSYKNLLDELEKSVKTLKASENIK-KIVEN----------KKT 2051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1793 HLSAINKhNMTALE--------GHKQAVEKGKKeTENTLNES--DDIMTEVNNLAQNINEAE-----------NELMDIN 1851
Cdd:PTZ00440 2052 SIDAINT-NIEDIEkeiesinpSLDELLKKGHK-IEISRYTSiiDNVQTKISNDSKNINDIEkkaqiylayikNNYNSIK 2129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1852 KELpqlterlnVKINNLTDEIQ-TRDLPEQVLQAELHAAQLTE----SSRMLDGILAEAKNLSLNATAAF--NAYSNIKK 1924
Cdd:PTZ00440 2130 KDI--------STLNEYFDEKQvSNYILTNIDKANKLSSELSEavtnSEEIIENIKKEIIEINENTEMNTleNTADKLKE 2201
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1925 LIDNADDAAKEAKAKANEaVELVTGPQgpLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEKNVNLV 2004
Cdd:PTZ00440 2202 LYENLKKKKNIINNIYKK-INFIKLQE--IENSSEKYNDISKLFNNVVETQKKKLLDNKNKINNIKDKINDKEKELINVD 2278
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2005 RALN-DTLGKLSAIPNDTIVKIQtakdKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDV---------AKTNAVV 2074
Cdd:PTZ00440 2279 SSFTlESIKTFNEIYDDIKSNIG----DLYKLEDTNNDELKKVKLYIENITHLLNRINTLINDLdnyqdenygKDKNIEL 2354
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2019522063 2075 KVDN---VTDAGERVKLLEKEADRLLDKLKP---------IKELQDNLGKNISQIKE 2119
Cdd:PTZ00440 2355 NNENnsyIIKTKEKINNLKEEFSKLLKNIKRnntlcnnnnIKDFISNIGKSVETIKQ 2411
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1674-1883 |
2.65e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1674 KDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAELRRRmfkNQEKAAadeLKAAEGLLNRVKKLFQDPH 1753
Cdd:PHA02562 212 GENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL---NTAAAK---IKSKIEQFQKVIKMYEKGG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1754 ---------NKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGHKQAVekgkketENTLN 1824
Cdd:PHA02562 286 vcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL-------ITLVD 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1825 ESDDIMTEvnnlaqnINEAENELMDINKELPQLTERLNVKINNLTD---EIQTRDLPEQVLQ 1883
Cdd:PHA02562 359 KAKKVKAA-------IEELQAEFVDNAEELAKLQDELDKIVKTKSElvkEKYHRGIVTDLLK 413
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1600-1928 |
2.82e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1600 LFSIENETQELKHLLSPQraperlLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDI--- 1676
Cdd:COG4372 15 LFGLRPKTGILIAALSEQ------LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELneq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1677 LQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAElrrrmfKNQEKAAADELKAAegLLNRVKKLfQDPHNKT 1756
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ------RKQLEAQIAELQSE--IAEREEEL-KELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1757 NDLNLEV----KDKLRHFQDKLEDVLD-MLREARGKIRESNHLSAINKHNMTALEGHKQAVEKGKKETENTLNESDDIMT 1831
Cdd:COG4372 160 ESLQEELaaleQELQALSEAEAEQALDeLLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1832 EVNNLAQNINEAENElmdinkELPQLTERLNVKINNLTDEIQTRDLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLN 1911
Cdd:COG4372 240 DALELEEDKEELLEE------VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330
....*....|....*..
gi 2019522063 1912 ATAAFNAYSNIKKLIDN 1928
Cdd:COG4372 314 EDALLAALLELAKKLEL 330
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1809-2135 |
2.99e-04 |
|
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: 46.49 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1809 KQAVEKGKKETENTL------NESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVKINNLTDEIQTRdlPEQVL 1882
Cdd:COG5185 92 KKLDTKILQEYVNSLiklpnyEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDI--FGKLT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1883 QAELHAAQLTESSRMLDGILAEAKNLSLNATAAFnAYSNIKKLidnaddaakeakakaneavELVTGPQGPLKDKAKSFI 1962
Cdd:COG5185 170 QELNQNLKKLEIFGLTLGLLKGISELKKAEPSGT-VNSIKESE-------------------TGNLGSESTLLEKAKEII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1963 -----QKSFRVHT----DAKTQSLDLK---EKENELAAMK-----DKLQNADEKNVNLVRALNDTLGKLS-AIPNDTIVK 2024
Cdd:COG5185 230 nieeaLKGFQDPEseleDLAQTSDKLEklvEQNTDLRLEKlgenaESSKRLNENANNLIKQFENTKEKIAeYTKSIDIKK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2025 IQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVK--VDNVTdAGERVKLLEKEADRLLDKLKP 2102
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeIENIV-GEVELSKSSEELDSFKDTIES 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 2103 IKE-------------------LQDNLGKNISQIKELINQARKQANSIKVSV 2135
Cdd:COG5185 389 TKEsldeipqnqrgyaqeilatLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1657-1735 |
3.78e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 42.77 E-value: 3.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019522063 1657 KDAERTNERAKQLKNFVKDILQTSKDIYDKAvklnETLGIQNKTLEKSLQELQKDVDKMMAELrrRMFKNQEKAAADEL 1735
Cdd:pfam04871 4 SELESEASSLKNENTELKAELQELSKQYNSL----EQKESQAKELEAEVKKLEEALKKLKAEL--SEEKQKEKEKQSEL 76
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1603-1886 |
3.97e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1603 IENETQELKhllspqrAPERLLQLAQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNERAKQLKNFVKDILQTSKD 1682
Cdd:TIGR00618 447 ITCTAQCEK-------LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1683 IYDKAVKLNETLGIQNKTleKSLQELQKDVDKMMAELRRRM--FKNQEKAAADELKAAEGLLNRVKklfqdphnktndln 1760
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEQTY--AQLETSEEDVYHQLTSERKQRasLKEQMQEIQQSFSILTQCDNRSK-------------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1761 lEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLS------AINKHNMTALEGHKQAvEKGKKETENTLNESDDIMTEVN 1834
Cdd:TIGR00618 584 -EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQDVRLHLQQCSQ-ELALKLTALHALQLTLTQERVR 661
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 1835 NLAQNINEAENELMDINKELPQLTERLNVKINNLTDEI-QTRDLPEQVLQAEL 1886
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLaQCQTLLRELETHIE 714
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1601-1845 |
4.06e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1601 FSIENETQELKHLLspQRAPERLLQL----AQNNQDTLVIEID---ELLNR--AAKVSADGEQ--TGKDAERTNERAKQL 1669
Cdd:PRK04778 252 LDIEKEIQDLKEQI--DENLALLEELdldeAEEKNEEIQERIDqlyDILERevKARKYVEKNSdtLPDFLEHAKEQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1670 KNFVkDILQTSkdiYdkavKLNETLGIQNKTLEKSLQELQKDVDkmmaELRRRMfKNQEKA---AADELKAAEGLLNRVK 1746
Cdd:PRK04778 330 KEEI-DRVKQS---Y----TLNESELESVRQLEKQLESLEKQYD----EITERI-AEQEIAyseLQEELEEILKQLEEIE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1747 KLFQDPHNKTNDL---NLEVKDKLRHFQDKL----------------EDVLDMLREARGKIRE-SNHLSAInKHNMTALE 1806
Cdd:PRK04778 397 KEQEKLSEMLQGLrkdELEAREKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEAlAEELEEK-PINMEAVN 475
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 1807 GH----KQAVEKGKKETENTLNESddIMTE------------VNNLAQNINEAEN 1845
Cdd:PRK04778 476 RLleeaTEDVETLEEETEELVENA--TLTEqliqyanryrsdNEEVAEALNEAER 528
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-510 |
4.67e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 4.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2019522063 464 CNCSVPGSINEDpCvDP----CICKENVAGNNCDVCKHSYFNLkRDNPRGC 510
Cdd:cd00055 2 CDCNGHGSLSGQ-C-DPgtgqCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1673-1786 |
4.67e-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: 42.96 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1673 VKDILQTSKDIYDKAVKLNETLGIQNKTLEKSLQELQKDVDKMMAElRRRMFKNQEKAAADELKAAEGLLNRVKKLFQDp 1752
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKD-AATLSEAAREKKEKELQKKVQEFQRKQQKLQQ- 83
|
90 100 110
....*....|....*....|....*....|....
gi 2019522063 1753 hnktnDLNLEVKDKLRHFQDKLEDVLDMLREARG 1786
Cdd:smart00935 84 -----DLQKRQQEELQKILDKINKAIKEVAKKKG 112
|
|
| Cas10_III |
cd09679 |
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ... |
1612-1911 |
6.44e-04 |
|
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; MTH326-like has inactivated polymerase catalytic domain; alr1562 and slr7011 - predicted only on the basis of size, presence of HD domain, and location with RAMPs in one operon; signature gene for type III; also known as Crm2 family
Pssm-ID: 187810 [Multi-domain] Cd Length: 475 Bit Score: 45.13 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1612 HLLSPQRAPERLLQLAQNNQDTLVIEIDELLNRA-AKVSADGEQTGKDAERT-NERAKQLKNFVKDILqtskDIYDkavk 1689
Cdd:cd09679 49 VVIFPYLRGNPLFEKKLENKDNPELEIASLPNRFlAIVPGNEEEAEELKEEIeEETWESILNKVKEYL----DIEN---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1690 LNETLGIQNKTLEKSLQELQKDVDKMMAElrrrmFKNQEKAAADELKAAEGLLNRVKKLFQDphnKTNDLNLEVKDKLRH 1769
Cdd:cd09679 121 VEPFLLKSDALERISDRIEDGNEDREEAE-----ELEAARKNVRDFAPVPWIPPAPKIYIYI---VSIFNEKELSEKYKE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1770 FQDKLE--DVLDMLREARGKIRESnhlsainkhnmtaLEGHKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENEL 1847
Cdd:cd09679 193 FLLKKRngLLLDKLGGRARKEYRS-------------VCGLLAAAWKLEKETEQYSLFAKDDLEEDLKLLLEAGERLCPL 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 1848 MDINKELPQLTERLNVKINNlTDEIQTRDLPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLN 1911
Cdd:cd09679 260 CLIKRLLPERLKEKLVLIDE-VIKRSKRNREEPRLKYENFREELRELLEKEPEIVYLFIKAKKN 322
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1658-1885 |
7.99e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1658 DAERTNERAKQLKNFVKDILQTSKDIYDKAVKlNETLGIQNKTLEKSLQELQKDVDKMMAElrrrmfKNQEKAAADELK- 1736
Cdd:pfam05622 174 ELKKANALRGQLETYKRQVQELHGKLSEESKK-ADKLEFEYKKLEEKLEALQKEKERLIIE------RDTLRETNEELRc 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1737 --AAEGLLNRVKKLFQDPHNKTNDLN-----LEVKDKLRHFQ---------------DKLEDVLDMLREARgkiRESNHL 1794
Cdd:pfam05622 247 aqLQQAELSQADALLSPSSDPGDNLAaeimpAEIREKLIRLQhenkmlrlgqegsyrERLTELQQLLEDAN---RRKNEL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1795 SAINKHNMTALEGHKQAVEKGKKETENTLNESDDIMtevnNLAQNINEAENELMDINKELPQLTERL-----------NV 1863
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKALQEQGSKAEDSS----LLKQKLEEHLEKLHEAQSELQKKKEQIeelepkqdsnlAQ 399
|
250 260
....*....|....*....|..
gi 2019522063 1864 KINNLTDEIQTRDlpEQVLQAE 1885
Cdd:pfam05622 400 KIDELQEALRKKD--EDMKAME 419
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
1761-2131 |
8.57e-04 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 44.56 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1761 LEVKDKLRHFQDKLEDVLDMLREARGKIRESNH-----LSAINKhnmtaLEGHKQAVekgKKETENTLNE----SDDIMT 1831
Cdd:cd22654 58 IDLNQDMINFSQRFNNYYDKLYDLAGKINEDEQakedfLNGINK-----LQSQLQTI---QNSMEQTSSNlnrfKTLLDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1832 EVNNLAQNINEAENELMDINKELPQLTErlnvKINNLTDEIQtrdlpEQVLQAelhaaqLTESSRMLDGILaeaknlsln 1911
Cdd:cd22654 130 DSKNFSTDAKKAIDSLSGSNGEIAQLRT----QIKTINDEIQ-----EELTKI------LNRPIEVGDGSI--------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1912 ataafnaysNIKKLIDNADDAAKEAKAKANEAVELVTGPQGPLKDkaksfiqksfrvhTDAKTQSLDLKEKENELaamkd 1991
Cdd:cd22654 186 ---------NIGKQVFTITITTATTKTVDVTSIGGLINGIGNASD-------------DEVKEAANKIQQKQKEL----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1992 klqnadeknVNLVRALNDTLGKLSAIpndTIVkiqtaKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTN 2071
Cdd:cd22654 239 ---------VDLIKKLSDAEIQATQL---TLV-----EDQVNGFTELIKRQIATLENLVEDWEMLNQNMNQLQTNVNSGK 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2072 avvkVDNVTdagervkllekeadrLLDKLKPIKELQDNLGKnisqikelinQARKQANSI 2131
Cdd:cd22654 302 ----IDSKL---------------LQKQLKQIKKISDELNK----------QTKQFEDFL 332
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1604-1721 |
1.09e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 44.65 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1604 ENETQELKHL------LSpQRApERL---LQLAQNNQDTLVIEIDELLNRA---AKVSADGEQT-GKDAERTNERAKQLK 1670
Cdd:pfam10168 571 EQQLQELQSLeeerksLS-ERA-EKLaekYEEIKDKQEKLMRRCKKVLQRLnsqLPVLSDAEREmKKELETINEQLKHLA 648
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019522063 1671 NFVKDI----------LQTSKDIYDK-AVKLNETlgiQNKTLEKSLQELQKDVDKMMAELRR 1721
Cdd:pfam10168 649 NAIKQAkkkmnyqryqIAKSQSIRKKsSLSLSEK---QRKTIKEILKQLGSEIDELIKQVKD 707
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1761-1893 |
1.10e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.44 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1761 LEVKDKLRHFQDKLEDVLDMLREARGKIREsnhlsainkhnmtaLEGHKQAVEKGKKETEntlNESDDIMTEVNNLAQNI 1840
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEE--------------LEEERRQAEEEAERLE---QKRQEAEEEKERLEESA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2019522063 1841 NEAENELMDINKELPQLTErlnvKINNLTDEIQTRDLPEQVLQAELHAAQLTE 1893
Cdd:pfam20492 72 EMEAEEKEQLEAELAEAQE----EIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1664-1928 |
1.47e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1664 ERAKQLKNFVKDILQTSKDIYDKAVKLNETLG-------IQNKTLEKSLQELQKDVDKMMAElrrrmFKNQEKAAADELK 1736
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAflrrglsVQLANLEKVREGLEKVLNELKKD-----FKQLLKDLDAALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1737 AAEGLLNRVKKLFQDPHNKTNDlnlEVKDKLRHF--QDKLEDVLDMLREARGKIRE-SNHLSAINKHNMTALEGHKQAVE 1813
Cdd:pfam04108 78 RLEETLDKLRNTPVEPALPPGE---EKQKTLLDFidEDSVEILRDALKELIDELQAaQESLDSDLKRFDDDLRDLQKELE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1814 KG------KKETENTLNESDDIMTEVNNLAQNI-NEAENELMDINKELPQLTERLNVKINNltdeiqTRDLPEQVLQAEL 1886
Cdd:pfam04108 155 SLsspsesISLIPTLLKELESLEEEMASLLESLtNHYDQCVTAVKLTEGGRAEMLEVLEND------ARELDDVVPELQD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2019522063 1887 HAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSNIKKLIDN 1928
Cdd:pfam04108 229 RLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPE 270
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1818-2132 |
1.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1818 ETENTLNES-DDIMTEVNNLAQNINEAENELMDINKELPQLTERLNVKINnltdeiQTRDLPEQvlqaelhAAQLTEssr 1896
Cdd:COG1340 1 SKTDELSSSlEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------QVKELREE-------AQELRE--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1897 MLDGILAEAKNLSLNATAAFNAYSNIKKLIDNaddaakeakakaneavelvtgpqgpLKDKAKSfiqksfrvhtdAKTQS 1976
Cdd:COG1340 65 KRDELNEKVKELKEERDELNEKLNELREELDE-------------------------LRKELAE-----------LNKAG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1977 LDLKEKENELAAMKDKLQNAD---EKNVNLVralndtlgklsaipnDTIVKIQTAKDKVKQANDTANDvlarIKDLNLNL 2053
Cdd:COG1340 109 GSIDKLRKEIERLEWRQQTEVlspEEEKELV---------------EKIKELEKELEKAKKALEKNEK----LKELRAEL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2054 LGLKQNYSALKEDVAKT--NAVVKVDNVTDAGERVKLLEKEADRL-------LDKLKPIKELQDNLGKNISQIKELINQA 2124
Cdd:COG1340 170 KELRKEAEEIHKKIKELaeEAQELHEEMIELYKEADELRKEADELhkeiveaQEKADELHEEIIELQKELRELRKELKKL 249
|
....*...
gi 2019522063 2125 RKQANSIK 2132
Cdd:COG1340 250 RKKQRALK 257
|
|
| BAR |
cd07307 |
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ... |
1665-1848 |
1.81e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.
Pssm-ID: 153271 [Multi-domain] Cd Length: 194 Bit Score: 42.05 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1665 RAKQLKNFVKDILQTSKDIYDKAVKLNETlgiqNKTLEKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGLLNR 1744
Cdd:cd07307 1 KLDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPDLSNTDLGEALEKFGKIQKELEEFRDQLEQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1745 VKKLFQDPHNKTNDLNLEVKDKLRHFQDKLEDVLDMLREARGKIRESNHLSAINKHNMTALEGHKQAVEKgkketentln 1824
Cdd:cd07307 77 LENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAEAEEELQEAKEKYEE---------- 146
|
170 180
....*....|....*....|....
gi 2019522063 1825 ESDDIMTEVNNLAQNINEAENELM 1848
Cdd:cd07307 147 LREELIEDLNKLEEKRKELFLSLL 170
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1357-1460 |
3.62e-03 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 40.75 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1357 TSFTMSPKASRIEKC----ECPVGYSGLS---------CEsCSPGFYRMAPAspgrrpgptlGTCVPCQcnghsdMCDPQ 1423
Cdd:cd13416 40 DGVTFSDVVSHTEPCqpctRCPGLMSMRApctathdtvCE-CAYGYYLDEDS----------GTCEPCT------VCPPG 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 2019522063 1424 TSVCQACKHNT-TGdhCEWCAPGFYGTVRGFPDDCRPC 1460
Cdd:cd13416 103 QGVVQSCGPNQdTV--CEACPEGTYSDEDSSTDPCLPC 138
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1692-1850 |
5.13e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1692 ETLGIQNKTLeKSLQELQKDVDKMMAELRRRMFKNQEKAAADELKAAEGllnrvkklfQDPHNKTNDLNLEVKDKLRHFQ 1771
Cdd:PRK06669 18 KTHEIQKYRF-KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAE---------EDAFEIVEAAEEEAKEELLKKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1772 DKLEDVL-DMLREARGKIRESNHLSAINKHNMTAlEGHKQAVEKGKKETENTLNESDD----IMTEVNNLAQN-INEAEN 1845
Cdd:PRK06669 88 DEASSIIeKLQMQIEREQEEWEEELERLIEEAKA-EGYEEGYEKGREEGLEEVRELIEqlnkIIEKLIKKREEiLESSEE 166
|
....*
gi 2019522063 1846 ELMDI 1850
Cdd:PRK06669 167 EIVEL 171
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-325 |
5.36e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.36e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1600-1739 |
6.81e-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: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1600 LFSIENETQELKHLLspQRAPERLLQL------AQNNQDTLVIEIDELLNRAAKVSADGEQTGKDAERTNER------AK 1667
Cdd:COG1579 12 LQELDSELDRLEHRL--KELPAELAELedelaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019522063 1668 QLKNFVKDILQTSKDIY---DKAVKLNETLgiqnKTLEKSLQELQKDVDKMMAELRRRmfKNQEKAAADELKAAE 1739
Cdd:COG1579 90 EYEALQKEIESLKRRISdleDEILELMERI----EELEEELAELEAELAELEAELEEK--KAELDEELAELEAEL 158
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1848-2111 |
7.78e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1848 MD-INK----ELPQLTERLNVKINNLTDEIQT-RDLPEQvlQAELHAAQLTESSRMLDGILAEAKNLSLNATAAFNAYSN 1921
Cdd:PHA02562 168 MDkLNKdkirELNQQIQTLDMKIDHIQQQIKTyNKNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1922 IKKLIDNADDAAKeakakaneavELVTGpQGPLKDKAKSF--IQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQNADEK 1999
Cdd:PHA02562 246 LVMDIEDPSAALN----------KLNTA-AAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2000 nvnlvralndtlgklsaipndtIVKIQTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEDVAKTNAVVK--VD 2077
Cdd:PHA02562 315 ----------------------LEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEelQA 372
|
250 260 270
....*....|....*....|....*....|....
gi 2019522063 2078 NVTDAGERVKLLEKEADRLLDKLKPIKELQDNLG 2111
Cdd:PHA02562 373 EFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1639-2128 |
7.97e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1639 DELLNRAAKVSADGEQTGK----DAERTNERAKQLKNFVKDILQTSKDIYDKA--VKLNETlgiqNKTLEKSLQELQKDV 1712
Cdd:PRK02224 80 EYHIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRMDAEAFVNCayVRQGEV----NKLINATPSDRQDMI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1713 DKMMA-----ELRRRMfKNQEKAAADELKAAEGLLNRVK-----KLFQDPHNKTNDLNLEVKDklrhfqdkLEDVLDMLR 1782
Cdd:PRK02224 156 DDLLQlgkleEYRERA-SDARLGVERVLSDQRGSLDQLKaqieeKEEKDLHERLNGLESELAE--------LDEEIERYE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1783 EARGKIRESnhlsainkhnmtaleghKQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTER-- 1860
Cdd:PRK02224 227 EQREQARET-----------------RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERle 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1861 -LNVKINNLTDEIQTRDLPEQVLqaELHAAQLTESSRMLDGILAEAKnlslnaTAAFNAYSNIKKLIDNADDaakeakak 1939
Cdd:PRK02224 290 eLEEERDDLLAEAGLDDADAEAV--EARREELEDRDEELRDRLEECR------VAAQAHNEEAESLREDADD-------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1940 aneavelvtgpqgpLKDKAKSFIQKSFRVHTDAKTQSLDLKEKENELAAMKDKLQ--------------NADEKNVNLVR 2005
Cdd:PRK02224 354 --------------LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelrerfgdapvdlgNAEDFLEELRE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2006 ALNDTLGKLsaipNDTIVKIQTAKDKVKQAN---------------------DTANDVLARIKDLNLNLLGLKQNYSALK 2064
Cdd:PRK02224 420 ERDELRERE----AELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVE 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019522063 2065 EDVaktnavvkvdnvtDAGERVKLLEKEADRLLDKLKPIKELQDNLGKNISQIKELINQARKQA 2128
Cdd:PRK02224 496 ERL-------------ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1975-2136 |
8.60e-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: 40.68 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1975 QSLD--LKEKENELAAMKDKLQNADEKnvnlVRALNDTLGKLSAipndtivKIQTAKDKVKQANDTANDVLARIKDLNLN 2052
Cdd:COG1579 13 QELDseLDRLEHRLKELPAELAELEDE----LAALEARLEAAKT-------ELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2053 LLGLKQN--YSALKEDVAKTNAVVKV--DNVTDAGERVKLLEKEADRL---LDKLKP-IKELQDNLGKNISQIKELINQA 2124
Cdd:COG1579 82 LGNVRNNkeYEALQKEIESLKRRISDleDEILELMERIEELEEELAELeaeLAELEAeLEEKKAELDEELAELEAELEEL 161
|
170
....*....|..
gi 2019522063 2125 RKQANSIKVSVS 2136
Cdd:COG1579 162 EAEREELAAKIP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1809-2126 |
8.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1809 KQAVEKGKKETENTLNESDDIMTEVNNLAQNINEAENELMDINKELPQLTERLN-------------VKINNLTDEIQTR 1875
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEklekevkeleelkEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1876 D-----LPEQVLQAELHAAQLTESSRMLDGILAEAKNLSLNATaafnAYSNIKKLIDNADDAAKEAKAKANEAVELVTGP 1950
Cdd:PRK03918 251 EgskrkLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE----EYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 1951 QGPLKDKAKsfiqKSFRVHTDAKtqslDLKEKENELAAMKDKLQNADEknvnlVRALNDTLGKLSA-----IPNDTIVKI 2025
Cdd:PRK03918 327 EERIKELEE----KEERLEELKK----KLKELEKRLEELEERHELYEE-----AKAKKEELERLKKrltglTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019522063 2026 QTAKDKVKQANDTANDVLARIKDLNLNLLGLKQNYSALKEdvAKTNAVVKVDNVTDAgERVKLLEK---EADRLLDKLKP 2102
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEE-HRKELLEEytaELKRIEKELKE 470
|
330 340
....*....|....*....|....
gi 2019522063 2103 IKELQDNLGKNISQIKELINQARK 2126
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESE 494
|
|
| |
