|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
34-285 |
2.11e-92 |
|
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: 300.05 E-value: 2.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 34 HQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPNQRHPITNAIDGKN----TW 109
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpTW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 110 WQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGPP 189
Cdd:smart00136 76 WQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 190 SYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreID 267
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DR 220
|
250
....*....|....*...
gi 1622930585 268 PIVTRRYYYSVKDISVGG 285
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
39-285 |
4.59e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 287.17 E-value: 4.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 39 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 114
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 115 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 193
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 194 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 271
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1622930585 272 RRYYYSVKDISVGG 285
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 ... |
1593-1852 |
7.06e-87 |
|
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: 285.08 E-value: 7.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1593 VMSIN-LTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERT 1671
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEGLL 1751
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1752 KKVKKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENT 1831
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1622930585 1832 LKEGNDILDEANRLADEINSI 1852
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1231-1364 |
7.98e-50 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 173.60 E-value: 7.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1231 EPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGFSTYNPQVIIRGGtptHARIIVRHMAAPLIGQLTRHEIEMTEKE 1310
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 1311 WKYYGddprvHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQ 1364
Cdd:smart00281 79 WQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2037-2173 |
2.14e-49 |
|
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: 172.67 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2037 VKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2116
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2117 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVN 2173
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2793-2921 |
2.31e-46 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 163.64 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2793 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDGQWHKIKIMRSKQEGILYVDG-ASNRTI 2871
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2872 SPRKADI-LDVVGMLYVGGLPINYTTRRIGPVTYSIDGCIRNLHMAEAPAD 2921
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1234-1378 |
7.74e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 159.74 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1234 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGFSTYNPQVIIRGGtptHARIIVRHMA--APLIGQLTRHEIEMTEKEW 1311
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1312 KYygddpRVHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQGRRtavTPPAHLIE 1378
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-710 |
1.50e-42 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 152.80 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 578 LPHSYYWSAPASYLGNKLPAVGGQLTFTISYDLeeeEEDTEHVLQFMIILEGNDLRISTAQdEVYLHPSEEHVNVLLLKE 657
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 658 ESFTIHGtHFPVSRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVS 710
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
583-722 |
2.16e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 147.03 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 583 YWSAPASYLGNKLPAVGGQLTFTISYDLEEEEEDTehVLQFMIILEGNDLRISTAQDE-VYLHPSEEHVNVLLLKEESFT 661
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 662 iHGTHFPVSRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVSYPTdGSVAAAVE 722
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2368-2507 |
5.80e-40 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 145.54 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2368 FRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISivdIDTNQEE 2447
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2448 NIATSSSGNNfglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLKDIEISRTPYN 2507
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2766-2915 |
5.86e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 140.63 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2766 FGLSRNSHIAIAFDDTKvKNHLTIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDG 2845
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2846 QWHKIKIMRSKQEGILYVDG-ASNRTISPRKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2915
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2915 |
6.07e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.00 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2788 TIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMI-PTKINDGQWHKIKIMRSKQEGILYVDG- 2865
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2866 ASNRTISPRKADILDVVGMLYVGGLPINYtTRRIGPVTYSIDGCIRNLHM 2915
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2941-3093 |
8.37e-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: 131.39 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2941 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAvydaGVPGH 3019
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 3020 LCDGQWHKVTANKIKHRIELTVDGNQVEAQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2174-2314 |
3.50e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.97 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2174 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIMASRTGRNGTISVRALDGPka 2253
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2254 sivpstyHSTSPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDNKPIG 2314
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2964-3093 |
2.61e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 123.60 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2964 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAVYDagvPGHLCDGQWHKVTANKIKHRIELTVD 3042
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 3043 GNQVEAQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2340-2501 |
1.19e-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: 122.53 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2340 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2419
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2420 GKWKSFTLSRIQKQANISIvdidtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDI 2499
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1622930585 2500 EI 2501
Cdd:cd00110 149 KV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2554-2695 |
8.94e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 119.34 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2554 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARtmrKIVVRPEPNLfHDGREHSVHVERTRG 2633
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2634 IFTVQVDENRR--YMQNLTVEQPLEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCVWNLVINSVPMD 2695
Cdd:pfam00054 66 SGTLSVDGEARptGESPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2363-2503 |
7.89e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 116.67 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2363 TVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIvdi 2441
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2442 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDIEISR 2503
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2528-2690 |
1.07e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 110.97 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2528 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARTm 2606
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2607 rkIVVRPePNLFHDGREHSVHVERTRGIFTVQVDENR--RYMQNLTVEQPLEVKKLFVGGAPPEFQPSPLRNIPPFEGCV 2684
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1622930585 2685 WNLVIN 2690
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2169-2311 |
8.83e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2169 NIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIMASRTGRNGTISVral 2248
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2249 DGPKASIVpstyhsTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2150-2309 |
4.25e-25 |
|
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: 103.65 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2150 SGGDCIRtYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2229
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2230 YRIMASRTGRNGTISVralDGPKasivpsTYHSTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2309
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2968-3093 |
7.76e-25 |
|
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: 102.11 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2968 FRTTRTTGVLLGISSQKMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagVPGHLCDGQWHKVTANKIKHRIELTVDGNQVE 3047
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622930585 3048 AQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2549-2692 |
2.67e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.88 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2549 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVVRPEPNLFHDGREHSVHV 2628
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2629 ERTRGIFTVQVD-ENRRYMQNLTVEQPLEVK-KLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2692
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1612-2164 |
1.04e-22 |
|
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: 106.64 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLlspqrapERLIQLAEGNLNTLVTEMNELLTRATKVTadgEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR04523 49 LKNKEKELKNL-------DKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VN---------EKAIKLNETLGTR--DEAF--ERNLEGLQKEIDQMIKElrRKNLETQKEIAEDELVAAEGLLKKVK--- 1755
Cdd:TIGR04523 119 KNklevelnklEKQKKENKKNIDKflTEIKkkEKELEKLNNKYNDLKKQ--KEELENELNLLEKEKLNIQKNIDKIKnkl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1756 -----KLFG--ESRGKNEEMEK---DLREKLADYKNKVDDAWDLLREATNKIREA----NRLFAVNQKNMTALEKKKEAV 1821
Cdd:TIGR04523 197 lklelLLSNlkKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1822 ESGKRQIENTLKEGNDILDE------------ANRLADEINSIIDYVEDIQTKLPPMSE---ELNNKIDDLSQEI----- 1881
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEisdlnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnses 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1882 ----KDRKLAEKVSQAESHAAQlNDSSavldgiLDEAKNISFNAtaafkaySNIKDYIDEAEKVAKEaKDlaheaTKLAT 1957
Cdd:TIGR04523 357 enseKQRELEEKQNEIEKLKKE-NQSY------KQEIKNLESQI-------NDLESKIQNQEKLNQQ-KD-----EQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1958 gprgllKEDAKGSLQKSF-RILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQA 2036
Cdd:TIGR04523 417 ------LQQEKELLEKEIeRLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2037 VKDKARQA---NDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKL 2113
Cdd:TIGR04523 491 LKSKEKELkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2114 KPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKK 2164
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1669-2149 |
5.76e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.29 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1669 ERTNTRAKSLGEFIKELARDAEAVnEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELR---------RKNLETQKEI 1739
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1740 AED------ELVAAEGLLKKVKKLFGESRGKNEEMEK---DLREKLADYKN--KVDDAWDLLREATNKIREANR------ 1802
Cdd:PRK03918 237 KEEieelekELESLEGSKRKLEEKIRELEERIEELKKeieELEEKVKELKElkEKAEEYIKLSEFYEEYLDELReiekrl 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1803 -----LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNdILDEANRLADEINSIIDYVEDIQTKLPPMS-EELNNKIDD 1876
Cdd:PRK03918 317 srleeEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1877 LS---QEIKD--RKLAEKVSQAESHAAQLNDSSAVLDGI----------LDE--AKNIsfnataafkaysnIKDYIDEAE 1939
Cdd:PRK03918 396 LEkakEEIEEeiSKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEehRKEL-------------LEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1940 KVAKEAKDLAHEATKLatgpRGLLKEdAKGSLQKSFRILNEaKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDT 2019
Cdd:PRK03918 463 RIEKELKEIEEKERKL----RKELRE-LEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2020 LGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLK-KNYDKLADSVAKTnavvkDPSKNKIIadadaT 2098
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKEL-----EPFYNEYL-----E 606
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2099 VKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVS 2149
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1718-2077 |
1.75e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1718 QKEIDQMIK---ELRRKNLE---------TQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEK--DLREKLADYKNKV 1783
Cdd:TIGR02168 143 QGKISEIIEakpEERRAIFEeaagiskykERRKETERKLERTRENLDRLEDILNELERQLKSLERqaEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1784 DDA-WDLLreaTNKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEgndiLDEA-NRLADEINSIIDYVEDIQT 1861
Cdd:TIGR02168 223 RELeLALL---VLRLEELR-------EELEELQEELKEAEEELEELTAELQE----LEEKlEELRLEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1862 KLppmsEELNNKIDDLSQEIkdRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisFNATAAFKAYSNIKDYIDEAEKV 1941
Cdd:TIGR02168 289 EL----YALANEISRLEQQK--QILRERLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1942 AKEAKDLAHEATKLATGPRGLLKEDAKgslqKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALND--- 2018
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEael 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 2019 -----TLGKLSAIPNDTAAKLQAV----------KDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVA 2077
Cdd:TIGR02168 436 kelqaELEELEEELEELQEELERLeealeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1670-2228 |
1.94e-15 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 83.41 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1670 RTNTRAKSLGEFIKELARDAEAVNEKAIklnetLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAE-DELVAAE 1748
Cdd:PRK01156 94 RREAYIKKDGSIIAEGFDDTTKYIEKNI-----LGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEiNSLERNY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKlfgesrgkneemekDLREKLADYknkvDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQI 1828
Cdd:PRK01156 169 DKLKDVID--------------MLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1829 ENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLpPMSEELNNKIDDLSQEIKdrklaekvsQAESHAAQLNdSSAVLD 1908
Cdd:PRK01156 231 MDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNNYYKELEERHM---------KIINDPVYKN-RNYIND 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1909 GILDEAKNISFNataafKAYSNIKDYIDEAEKVAKEAKDlaheatklatgprglLKEDAKGSLQKSFRiLNEAKKLANDV 1988
Cdd:PRK01156 300 YFKYKNDIENKK-----QILSNIDAEINKYHAIIKKLSV---------------LQKDYNDYIKKKSR-YDDLNNQILEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1989 KENEDHLNG-------LKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQN 2061
Cdd:PRK01156 359 EGYEMDYNSylksiesLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2062 LDGLKKNYDKL-ADSVA----------KTNAVVKDPSKNKIIADADatVKNLEQEADRLIDKLKPIKELEDNLKKniSEI 2130
Cdd:PRK01156 439 LDELSRNMEMLnGQSVCpvcgttlgeeKSNHIINHYNEKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLES--EEI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2131 KELINQ------ARKQANSIKVSVSSGGDciRTYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:PRK01156 515 NKSINEynkiesARADLEDIKIKINELKD--KHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEI 592
|
570 580
....*....|....*....|....*..
gi 1622930585 2205 SF-LWDVGSGVGRVE--YPDltiDDSY 2228
Cdd:PRK01156 593 KKqLNDLESRLQEIEigFPD---DKSY 616
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1703-2096 |
2.18e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 81.10 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1703 LGTRDEAFERNLEGLQKEIDQMIKELrrknletqKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKdLREKLADYKNK 1782
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAAL--------SEQLRKALFELDKLQEELEQLREELEQAREELEQ-LEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1783 VDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTK 1862
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1863 LppmsEELNNKIDDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVA 1942
Cdd:COG4372 152 L----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1943 KEAKDLaheaTKLATGPRGLLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDL-LRALNDTLG 2021
Cdd:COG4372 221 LEAKDS----LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEaLEEAALELK 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 2022 KLSAIPNDTAAKLQAVKDKARQANdtAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADAD 2096
Cdd:COG4372 297 LLALLLNLAALSLIGALEDALLAA--LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1705-1990 |
4.63e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1705 TRDEAFERNLEGLQKEIDQM---IKELRRKNLETQKEIAEdelVAAE--GLLKKVKKLFGESRGKNEEMeKDLREKLADY 1779
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1780 KNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEN---TLKEGNDILDEANRLADEInsiidyv 1856
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKEL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1857 EDIQtklppMSEELNNKIDDLSQEIKD---------RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisfnataafKA 1927
Cdd:COG1340 150 EKAK-----KALEKNEKLKELRAELKElrkeaeeihKKIKELAEEAQELHEEMIELYKEADELRKEAD----------EL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 1928 YSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKsfrILNEAKKLANDVKE 1990
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREK---EKEELEEKAEEIFE 274
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
917-965 |
5.60e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 68.53 E-value: 5.60e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 917 PCRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGLQS-ARGCV 965
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
918-964 |
2.51e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 918 CRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGLQ--SARGC 964
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1612-2147 |
2.69e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertNTRAKSLGEF-IKELARDAE 1690
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE--------------EEKEKKLQEEeLKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1691 AVNEKAIKLnetlGTRDEAFERNLEGLQKEIDQMIKELrrknLETQKEIAEDElvaaegllkKVKKLFGESRGKNEEMEK 1770
Cdd:pfam02463 297 ELKSELLKL----ERRKVDDEEKLKESEKEKKKAEKEL----KKEKEEIEELE---------KELKELEIKREAEEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1771 DLREKLADYKNKVDDAWDLLREATNKIREANRLFavNQKNMTALEKKKEAvesgKRQIENTLKEGNDILDEANRLADEIN 1850
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEA----QLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1851 SIIDYVEDIQTKLPPMSEEL-------NNKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFN--- 1920
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELekqelklLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvll 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1921 -----------------------ATAAFKAY---------SNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAK 1968
Cdd:pfam02463 514 alikdgvggriisahgrlgdlgvAVENYKVAistavivevSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1969 GSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTA 2048
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2049 KDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADadatvknLEQEADRLIDKLKPIKELEDNLKKNIS 2128
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-------EELLADRVQEAQDKINEELKLLKQKID 746
|
570
....*....|....*....
gi 1622930585 2129 EIKELINQARKQANSIKVS 2147
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEE 765
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
918-964 |
3.99e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 3.99e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 918 CRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGlQSARGC 964
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
967-1011 |
2.89e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.48 E-value: 2.89e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930585 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSFQEGGC 1011
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1649-2142 |
9.15e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 71.40 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1649 ELLTRATKVTADGEQTgqdAERTNTRAKSLGEFIKELARDAEAVNEKAIKlnetlGTRDEAfERNLEGLQKEIDQmikEL 1728
Cdd:NF041483 510 EAIERATTLRRQAEET---LERTRAEAERLRAEAEEQAEEVRAAAERAAR-----ELREET-ERAIAARQAEAAE---EL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1729 RRKNLEtqkeiAEDELVAAEGLLkkvkklfGESRGKNEEMEKDLREKLadyknkvddawDLLR-EATNKIR--------E 1799
Cdd:NF041483 578 TRLHTE-----AEERLTAAEEAL-------ADARAEAERIRREAAEET-----------ERLRtEAAERIRtlqaqaeqE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1800 ANRL-----------------FAVNQKNMTALEK---KKEAVESGKR-------QIENTLKEGNDIL----DEANRL--- 1845
Cdd:NF041483 635 AERLrteaaadasaaraegenVAVRLRSEAAAEAerlKSEAQESADRvraeaaaAAERVGTEAAEALaaaqEEAARRrre 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1846 ADEI-NSIIDYVEDIQTKLPPMSEEL----NNKIDDLSQEIK------DRKLAEKVSQAESHAAQLNDSSAvldGILDEA 1914
Cdd:NF041483 715 AEETlGSARAEADQERERAREQSEELlasaRKRVEEAQAEAQrlveeaDRRATELVSAAEQTAQQVRDSVA---GLQEQA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1915 KN-ISFNATAAFKAYSNIK-DYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILN----EAKKLANDV 1988
Cdd:NF041483 792 EEeIAGLRSAAEHAAERTRtEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaiaEAERLRSDA 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1989 KENEDhlnglKTRIENADAR---NGDLLRALNDTLGKLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIKELHQNLDGL 2065
Cdd:NF041483 872 SEYAQ-----RVRTEASDTLasaEQDAARTRADAREDANRIRSDAAA--QADRLIGEATSEAERLTAEARAEAERLRDEA 944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2066 KKNYDKL-ADSVAKTNAVVKDPSKN--KIIADADATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNISEIKELINQA 2137
Cdd:NF041483 945 RAEAERVrADAAAQAEQLIAEATGEaeRLRAEAAETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEAREEADRTLDEA 1024
|
....*
gi 1622930585 2138 RKQAN 2142
Cdd:NF041483 1025 RKDAN 1029
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
966-1012 |
3.64e-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: 3.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 966 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSF--QEGGCT 1012
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-916 |
4.64e-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: 60.06 E-value: 4.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 864 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDARNCQ 916
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-805 |
5.17e-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: 60.06 E-value: 5.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 756 PCQCFGHA---ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPTKGtsEDCQ 805
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1420-1466 |
1.38e-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: 58.90 E-value: 1.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1420 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1466
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1612-1902 |
1.62e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLiqlaegnLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRDE---AFERNLEGL------------QKEIDQMIKELRR------------KNLETQKEIAEDE- 1743
Cdd:TIGR02169 756 VKSELKELEARIEELEEdlhKLEEALNDLearlshsripeiQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1744 --LVAAEGLLKKVKKLFG----ESRGKNEEME----------KDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVN 1807
Cdd:TIGR02169 836 qeLQEQRIDLKEQIKSIEkeieNLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1808 QKNMTALEKKKEAVESGKRQIENTLKEGNDIldeanrlADEINSIIDYVEDIQTKLPPMS--EELNNK-IDDLSQEIKDR 1884
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEI-------PEEELSLEDVQAELQRVEEEIRalEPVNMLaIQEYEEVLKRL 988
|
330
....*....|....*....
gi 1622930585 1885 K-LAEKVSQAESHAAQLND 1902
Cdd:TIGR02169 989 DeLKEKRAKLEEERKAILE 1007
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1060-1108 |
1.76e-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: 58.52 E-value: 1.76e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYPRCNLCDC 1108
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1527-1574 |
2.57e-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: 2.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKHWHAREGWECVFC 1574
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1527-1570 |
2.97e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKHWHAREGWE 1570
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
967-1014 |
3.05e-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: 57.75 E-value: 3.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSFQEGGCTAC 1014
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1106-1163 |
3.75e-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: 57.36 E-value: 3.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGLDAKNPLGC 1163
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1419-1467 |
6.02e-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: 56.98 E-value: 6.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1419 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1467
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1014-1057 |
6.63e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.63e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 1014 CECS---HLGNNCDPKTGQCICPPNTIGEKCSKCAPNTWGHSiTTGC 1057
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1059-1101 |
7.32e-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: 7.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622930585 1059 ACNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1013-1058 |
7.39e-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: 7.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1013 ACECSHLG---NNCDPKTGQCICPPNTIGEKCSKCAPNTWGH-SITTGCK 1058
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1106-1163 |
1.28e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGldaKNPLGC 1163
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1106-1163 |
1.60e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGlDAKNPLGC 1163
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1014-1057 |
1.81e-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: 55.44 E-value: 1.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 1014 CECSHLG---NNCDPKTGQCICPPNTIGEKCSKCAPNTWGHSITTGC 1057
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1527-1562 |
3.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 3.16e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKH 1562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
414-471 |
3.32e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 3.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 414 CHCNPVGSLNEVCVkdekharrgLAPGSCHCKTGFGGVSCDRCARGYTGYPDCKACNC 471
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-797 |
5.52e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 5.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 757 CQCFGHA---ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPT 797
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
865-908 |
8.12e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 8.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 865 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 908
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1857-2146 |
9.50e-09 |
|
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: 59.69 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1857 EDIQTKLP---PMSEELNNKIDDL---SQEIKDrklaekvsqaesHAAQLNDSsaVLDGILDEAKNIS-FNATAAFKAYS 1929
Cdd:cd22656 26 EEYRKRLGissDIDDKLSSDFDPLldaYKSIKD------------HCTDFKDD--TYPSIVSLAGDIYnYAQNAGGTIDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1930 NIKDYIDEAEKVAKEAKDLAHEAtklatgprglLKEDAKGSLQKsfrILNEAKKLANDVKENEDHLNGLKTRIENADARN 2009
Cdd:cd22656 92 YYAEILELIDDLADATDDEELEE----------AKKTIKALLDD---LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2010 GDLLRALNDTLGK-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsk 2088
Cdd:cd22656 159 ETLEKALKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD--- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 2089 nkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2146
Cdd:cd22656 227 ---LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1060-1101 |
1.53e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622930585 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1616-2112 |
1.77e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.23 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1616 TQELKHLlspqrapERLIQLAEGNLNTLVTEMNELLTratkvtadgeqtgqdAERTN-TRAKSLGEFIKELARDaeaVNE 1694
Cdd:PRK04778 104 KHEINEI-------ESLLDLIEEDIEQILEELQELLE---------------SEEKNrEEVEQLKDLYRELRKS---LLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1695 KAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKNLETQKEI---AEDELVAAEGLLKKVKKLFgesrgknEEMEKD 1771
Cdd:PRK04778 159 NRFSFGPAL----DELEKQLENLEEEFSQFVELTESGDYVEAREIldqLEEELAALEQIMEEIPELL-------KELQTE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1772 LREKLADyknkvddawdlLREATNKIREANRLFAVNQknmtaLEKKKEAVESGKRQIENTLKEGNdiLDEANRLADEINS 1851
Cdd:PRK04778 228 LPDQLQE-----------LKAGYRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1852 IIDYVEDIqtklppmseelnnkiddLSQEIKDRKLAEKVSqaeshaaqlndssavldgildeaknisfnataafkaySNI 1931
Cdd:PRK04778 290 RIDQLYDI-----------------LEREVKARKYVEKNS-------------------------------------DTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1932 KDYIDEAEKVAKEakdLAHEATklatgprgllkedakgSLQKSFRI----LNEAKKLANDVKENEDHLNGLKTRIENADA 2007
Cdd:PRK04778 316 PDFLEHAKEQNKE---LKEEID----------------RVKQSYTLneseLESVRQLEKQLESLEKQYDEITERIAEQEI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2008 RNGDLLRALNDTLGKLSAIPN---DTAAKLQAVKDKARQANDTAKDVLAQIKELH-----QNLDGLKKNY-DKLADSVAK 2078
Cdd:PRK04778 377 AYSELQEELEEILKQLEEIEKeqeKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylekSNLPGLPEDYlEMFFEVSDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622930585 2079 TNAVVKDPSKNKI--------IADADATVKNLEQEADRLIDK 2112
Cdd:PRK04778 457 IEALAEELEEKPInmeavnrlLEEATEDVETLEEETEELVEN 498
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
865-914 |
2.28e-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: 52.36 E-value: 2.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 865 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDARN 914
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
413-465 |
3.82e-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: 51.97 E-value: 3.82e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 413 PCHCNPVGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTGYPD 465
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-799 |
8.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 8.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930585 757 CQC--FGHA-ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPTKG 799
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. |
469-515 |
8.91e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 8.91e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 469 CNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNLQEDNWKGC 515
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
414-466 |
1.36e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 414 CHCNPVGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTG--YPDC 466
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1962-2146 |
1.54e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1962 LLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDL---LRALNDTLGKLSAIPNDTAAKLQAVK 2038
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2039 DKARQANdtakdvlAQIKELHQNLDGLKKNYDKLADSVAKTnavvkdpskNKIIADADATVKNLEQEADRLIDKLKPIKE 2118
Cdd:COG4372 108 EEAEELQ-------EELEELQKERQDLEQQRKQLEAQIAEL---------QSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190
....*....|....*....|....*....|
gi 1622930585 2119 LEDNLKKN--ISEIKELINQARKQANSIKV 2146
Cdd:COG4372 172 ELQALSEAeaEQALDELLKEANRNAEKEEE 201
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1630-1847 |
2.08e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.14 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTNTRAKSLGEFIKELAR------------DA 1689
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEATVEGNSLVEKARtdadellvgarrDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1690 EAVNEKAiklnETLGTRDEAfernleglqkEIDQMIKELRRKNLETQKEIAE--DELV-AAEgllkkvkklfgESRGKNE 1766
Cdd:NF041483 1117 TAIRERA----EELRDRITG----------EIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1767 EMEKDLREKLADYKNK-----VDDAWDLLREATNK----IREANRLFAvnqknmTALEKKKEAVESGKRQIENTLKEGND 1837
Cdd:NF041483 1172 AKAKELVSDANSEASKvriaaVKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRELDVLVRRRED 1245
|
250
....*....|
gi 1622930585 1838 ILDEANRLAD 1847
Cdd:NF041483 1246 INAEISRVQD 1255
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1420-1466 |
9.04e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 9.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1420 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1466
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1826-2066 |
9.36e-07 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 53.06 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1826 RQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSE------ELNNKIDDLSQEIKDR--KLAEKVSQAESHA 1897
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAAtaqsaaEAAEEGREAVEDAITAmdQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1898 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfKAysnikdyiDEAEK----VAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1965 E------DAKGSLQKSFRILNEAKKLANDVKENedhLNGLKTRIENADARNGDLLRALND---TLGKLSAIPNDTAAKLQ 2035
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDA---LEEIVDSVEEIADLVQEIAAATDEqaaGSEEVNAAIDEIAQVTQ 231
|
250 260 270
....*....|....*....|....*....|.
gi 1622930585 2036 AVKDKARQANDTAKDVLAQIKELHQNLDGLK 2066
Cdd:smart00283 232 ETAAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| auto_Ata |
NF033481 |
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ... |
1665-2204 |
1.64e-06 |
|
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 54.49 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1665 GQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET-----------------LGTRDEAFERNLEGLQKeiDQMIKE 1727
Cdd:NF033481 642 GKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENavavgqgaqslveggvaLGARSKVEAKNSVALGQ--DAVATE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1728 LRRKNLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREkLADYKNKVDdawdllREATNKIREANRLFAVN 1807
Cdd:NF033481 720 ATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQ-LKNVDSRVN------QNTSNIGKNTQNITNLN 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1808 QK-NMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPM----SEELNNKIDDLSQEIK 1882
Cdd:NF033481 793 QKlDDTKTNLGNQITDTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTELNNTigntKTELNTKIDNTKTELE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1883 D--------------RKLAEKV-----SQAESHAAQLNDSSAVL----DGI----LDEAK---------NISFNATAAFK 1926
Cdd:NF033481 873 NkglnfagnsgadvhRKLGDKLnivggAAASTPAAKTSGENVITrttqDGIqielLKDSKfdsvttgntTLNTNGLTIKE 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1927 AYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILNEAKK-LANDVKENEDHLNGLKTRIENa 2005
Cdd:NF033481 953 GPSITKQGINAGSKQITNVADGINAKDAVNVDQLTKVKENLNGRITDTNNQLNDAKKdLGNQIADTNKNLNDAKKDLGD- 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2006 daRNGDLLRALNDTLGKLSAIPNDTAAKLQAV--KDKARQANDTAKDVLAQIKELHQNLdGLKKNYDKLADSVAKTNAVV 2083
Cdd:NF033481 1032 --QITDTNTKLNNTKDQLTTQINDTKTELNNTigNTKTELENKGLNFAGNSGADVHRKL-GDKLNIVGGAAASTPAAKTS 1108
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2084 KDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcirtyKPEIK 2163
Cdd:NF033481 1109 GENVITRTTKDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINAGGKQITNVADGINA--------KDAVN 1180
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622930585 2164 KGSYNNIVvnVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:NF033481 1181 KGQLDNLA--AKQNATDDAAVKYDDAKTKDKVTLKGKDGTV 1219
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
287-334 |
1.75e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 287 CICYGHA---RACplDPATnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 334
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
807-862 |
1.81e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 807 CACPLNIPSnnfSPTCHldrSLGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGSC 862
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1684-1885 |
1.87e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 51.29 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1684 ELARDAEAV----NEKAIKLNETLGTRD-----------EAFERNLEGLQKEIDQMIkelrrknlETQKEIAEDELVAAE 1748
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKLfgesrgknEEMEKDLREKLADYKNKVDDAWDLLR------EATNKIREANRLFAVN---------QKNMTA 1813
Cdd:cd00176 76 EIQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQffrdadDLEQWLEEKEAALASEdlgkdlesvEELLKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1814 LEKKKEAVESGKRQIENTLKEGNDILDEANRLADeinsiidyvEDIQTKLppmsEELNNKIDDLSQEIKDRK 1885
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEKL----EELNERWEELLELAEERQ 206
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
806-863 |
3.75e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 3.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 806 PCACPLNIpsnNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGsCQ 863
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1469-1524 |
1.09e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.04 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 1469 CACPLISSSnnfSPSCVTEGlddYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1524
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1847-2145 |
1.12e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 50.38 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1847 DEINSIIDYVEDIQ---TKLPPMSEELN-NKIDDLSQEIKD-RKLAEKVSQaesHAaqlNDSSAVLDGILDEAKNISfNA 1921
Cdd:NF033928 6 EDWISIQKYVQAALalpTTLEEVESYLGyPKDGIPGLEPKDlLDLFQNIRN---HA---RSWSNLEPKIKQLANDLA-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1922 TAAFKAYSN-IKDYIDEAeKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKsfrILneaKKLANDVKENEDHLNGLKT 2000
Cdd:NF033928 79 ARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---EDLKNDIKDYQQKADDVKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2001 RIenadarnGDLLRALNDTLgklsaipndtAAKLQAVKDKAR--QANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAK 2078
Cdd:NF033928 152 EL-------DDFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEKEIEQLNKEYDDYVKLSFT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2079 T----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLKKNISEIKELINQARKQAN 2142
Cdd:NF033928 215 GlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQTSLDDILTRMEDALPALK 287
|
...
gi 1622930585 2143 SIK 2145
Cdd:NF033928 288 KLK 290
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
469-515 |
1.13e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 469 CNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNlqeDNWKGC 515
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
468-515 |
1.22e-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: 44.65 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 468 ACNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNLQEdNWKGC 515
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1929-2270 |
1.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1929 SNIKDYIDEAEKVAKEAKDLAHEAtklatgprgllkEDAKGSLQKsfrILNEAKKLANDVKENEDHLNGLKTRIENADAR 2008
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAEL------------EELNEEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2009 NGDLLRAL---NDTLGKLSAI-----PNDTAAKLQAVKdkarQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTN 2080
Cdd:COG3883 88 LGERARALyrsGGSVSYLDVLlgsesFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2081 AVVKDpSKNKI---IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRT 2157
Cdd:COG3883 164 AELEA-AKAELeaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2158 YKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIemrKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIMASRT 2237
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA---GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGA 319
|
330 340 350
....*....|....*....|....*....|....
gi 1622930585 2238 GR-NGTISVRALDGPKASIVPSTYHSTSPPGYTI 2270
Cdd:COG3883 320 GAvVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
807-855 |
2.03e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 807 CACPlniPSNNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQP 855
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1971-2133 |
3.97e-05 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 48.88 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1971 LQKSFrilNEAKKLAndvKENEDHLNGLKTRIEnADARNGDLLRA----LNDTLGKLSAIPNDTAAKLQAVKDKARQAND 2046
Cdd:cd08915 75 IEQSF---KELSKLR---QNVEELLQECEELLE-EEAAEDDQLRAkfgtLRWRRPSSDEAAKELYEKVTKLRGYLEQASN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2047 TAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNaVVKDPSKNKIIADADAT---VKNLEQEADRLIDKLKpIKELEDN- 2122
Cdd:cd08915 148 SDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLlneVSELEKERERFISELE-IKSRNNDi 225
|
170
....*....|.
gi 1622930585 2123 LKKNISEIKEL 2133
Cdd:cd08915 226 LPKLITEYKKN 236
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1639-1913 |
6.30e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 47.67 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1639 NLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQ 1718
Cdd:smart00283 19 ELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV----EELEESSDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1719 kEIDQMIKEL-RRKNL-------------ETQKEIAedeLVAAEgllkkVKKLFGESRgkneemekdlrekladyknkvd 1784
Cdd:smart00283 95 -EIVSVIDDIaDQTNLlalnaaieaaragEAGRGFA---VVADE-----VRKLAERSA---------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1785 dawdllrEATNKIRE-ANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKl 1863
Cdd:smart00283 144 -------ESAKEIESlIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAG- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 1864 ppmSEELN---NKIDDLSQEIKDrkLAEKVSQAeshAAQLNDSSAVLDGILDE 1913
Cdd:smart00283 216 ---SEEVNaaiDEIAQVTQETAA--MSEEISAA---AEELSGLAEELDELVER 260
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
306-330 |
3.34e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.34e-04
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1469-1525 |
3.41e-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: 40.80 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1469 CACPLISSSNnfsPSCVTEGLddyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1525
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1997-2145 |
7.19e-04 |
|
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: 45.40 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1997 GLKTRIENADARNGDLLRalndtlgKLSAIPNDTAAKLQAVKDKARQANDTAKDVLA---QIKELHQNL----DGLKKNY 2069
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEK-------KLKTIKNELKNKEKELKNLDKNLNKDEEKINNsnnKIKILEQQIkdlnDKLKKNK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2070 DKL----ADSVaKTNAVVKDPSKNKIiadadatvkNLEQEadrlIDKL-KPIKELEDNLKKNISEIKELINQARKQANSI 2144
Cdd:TIGR04523 96 DKInklnSDLS-KINSEIKNDKEQKN---------KLEVE----LNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKY 161
|
.
gi 1622930585 2145 K 2145
Cdd:TIGR04523 162 N 162
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1469-1517 |
9.38e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 1469 CACPLissSNNFSPSCVtegLDDYRCTaCPRGYEGQYCERCAPGYTGSP 1517
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
785-919 |
1.89e-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: 41.52 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 785 CDKCLPGFYGDPTKGTSEDCQPCA-CPLNIPsnnfsPTCHLDRSLGLICdgcpvgytgprceRCAEGYFgqPSVPGGSCQ 863
Cdd:cd13416 35 CEPCLDGVTFSDVVSHTEPCQPCTrCPGLMS-----MRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 864 PCQcndnldfsipgSCDSLSGSCLICKPGTTGRyCELCADGYFGDAVDARN-CQPCR 919
Cdd:cd13416 95 PCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDpCLPCT 139
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1380-1407 |
9.56e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 9.56e-03
10 20
....*....|....*....|....*...
gi 1622930585 1380 CDCPLGYSGLSCEACLPGFYRLRSQPGG 1407
Cdd:pfam00053 20 CLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
34-285 |
2.11e-92 |
|
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: 300.05 E-value: 2.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 34 HQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPNQRHPITNAIDGKN----TW 109
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpTW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 110 WQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGPP 189
Cdd:smart00136 76 WQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 190 SYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreID 267
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DR 220
|
250
....*....|....*...
gi 1622930585 268 PIVTRRYYYSVKDISVGG 285
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
39-285 |
4.59e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 287.17 E-value: 4.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 39 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 114
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 115 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 193
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 194 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 271
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1622930585 272 RRYYYSVKDISVGG 285
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 ... |
1593-1852 |
7.06e-87 |
|
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: 285.08 E-value: 7.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1593 VMSIN-LTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERT 1671
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEGLL 1751
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1752 KKVKKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENT 1831
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1622930585 1832 LKEGNDILDEANRLADEINSI 1852
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1231-1364 |
7.98e-50 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 173.60 E-value: 7.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1231 EPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGFSTYNPQVIIRGGtptHARIIVRHMAAPLIGQLTRHEIEMTEKE 1310
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 1311 WKYYGddprvHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQ 1364
Cdd:smart00281 79 WQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2037-2173 |
2.14e-49 |
|
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: 172.67 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2037 VKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2116
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2117 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVN 2173
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2793-2921 |
2.31e-46 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 163.64 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2793 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDGQWHKIKIMRSKQEGILYVDG-ASNRTI 2871
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2872 SPRKADI-LDVVGMLYVGGLPINYTTRRIGPVTYSIDGCIRNLHMAEAPAD 2921
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1234-1378 |
7.74e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 159.74 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1234 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGFSTYNPQVIIRGGtptHARIIVRHMA--APLIGQLTRHEIEMTEKEW 1311
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1312 KYygddpRVHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQGRRtavTPPAHLIE 1378
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-710 |
1.50e-42 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 152.80 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 578 LPHSYYWSAPASYLGNKLPAVGGQLTFTISYDLeeeEEDTEHVLQFMIILEGNDLRISTAQdEVYLHPSEEHVNVLLLKE 657
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 658 ESFTIHGtHFPVSRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVS 710
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
583-722 |
2.16e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 147.03 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 583 YWSAPASYLGNKLPAVGGQLTFTISYDLEEEEEDTehVLQFMIILEGNDLRISTAQDE-VYLHPSEEHVNVLLLKEESFT 661
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 662 iHGTHFPVSRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVSYPTdGSVAAAVE 722
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2368-2507 |
5.80e-40 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 145.54 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2368 FRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISivdIDTNQEE 2447
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2448 NIATSSSGNNfglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLKDIEISRTPYN 2507
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2766-2915 |
5.86e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 140.63 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2766 FGLSRNSHIAIAFDDTKvKNHLTIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDG 2845
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2846 QWHKIKIMRSKQEGILYVDG-ASNRTISPRKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2915
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2915 |
6.07e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.00 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2788 TIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMI-PTKINDGQWHKIKIMRSKQEGILYVDG- 2865
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2866 ASNRTISPRKADILDVVGMLYVGGLPINYtTRRIGPVTYSIDGCIRNLHM 2915
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2941-3093 |
8.37e-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: 131.39 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2941 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAvydaGVPGH 3019
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 3020 LCDGQWHKVTANKIKHRIELTVDGNQVEAQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2174-2314 |
3.50e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.97 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2174 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIMASRTGRNGTISVRALDGPka 2253
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2254 sivpstyHSTSPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDNKPIG 2314
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2964-3093 |
2.61e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 123.60 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2964 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAVYDagvPGHLCDGQWHKVTANKIKHRIELTVD 3042
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 3043 GNQVEAQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2340-2501 |
1.19e-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: 122.53 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2340 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2419
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2420 GKWKSFTLSRIQKQANISIvdidtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDI 2499
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1622930585 2500 EI 2501
Cdd:cd00110 149 KV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2554-2695 |
8.94e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 119.34 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2554 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARtmrKIVVRPEPNLfHDGREHSVHVERTRG 2633
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2634 IFTVQVDENRR--YMQNLTVEQPLEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCVWNLVINSVPMD 2695
Cdd:pfam00054 66 SGTLSVDGEARptGESPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2363-2503 |
7.89e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 116.67 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2363 TVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIvdi 2441
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2442 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDIEISR 2503
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2528-2690 |
1.07e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 110.97 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2528 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARTm 2606
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2607 rkIVVRPePNLFHDGREHSVHVERTRGIFTVQVDENR--RYMQNLTVEQPLEVKKLFVGGAPPEFQPSPLRNIPPFEGCV 2684
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1622930585 2685 WNLVIN 2690
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2793-2915 |
5.96e-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: 107.89 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2793 VRTEAESGLLFYMARINHaDFATVQLRNGLPYFSYDLGSGDTNTM-IPTKINDGQWHKIKIMRSKQEGILYVDGASNRTI 2871
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622930585 2872 S-PRKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2915
Cdd:pfam02210 80 LpPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2169-2311 |
8.83e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2169 NIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIMASRTGRNGTISVral 2248
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2249 DGPKASIVpstyhsTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2150-2309 |
4.25e-25 |
|
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: 103.65 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2150 SGGDCIRtYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2229
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2230 YRIMASRTGRNGTISVralDGPKasivpsTYHSTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2309
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2968-3093 |
7.76e-25 |
|
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: 102.11 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2968 FRTTRTTGVLLGISSQKMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagVPGHLCDGQWHKVTANKIKHRIELTVDGNQVE 3047
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622930585 3048 AQSLNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCVRSLKL 3093
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2549-2692 |
2.67e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.88 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2549 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVVRPEPNLFHDGREHSVHV 2628
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2629 ERTRGIFTVQVD-ENRRYMQNLTVEQPLEVK-KLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2692
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1612-2164 |
1.04e-22 |
|
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: 106.64 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLlspqrapERLIQLAEGNLNTLVTEMNELLTRATKVTadgEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR04523 49 LKNKEKELKNL-------DKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VN---------EKAIKLNETLGTR--DEAF--ERNLEGLQKEIDQMIKElrRKNLETQKEIAEDELVAAEGLLKKVK--- 1755
Cdd:TIGR04523 119 KNklevelnklEKQKKENKKNIDKflTEIKkkEKELEKLNNKYNDLKKQ--KEELENELNLLEKEKLNIQKNIDKIKnkl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1756 -----KLFG--ESRGKNEEMEK---DLREKLADYKNKVDDAWDLLREATNKIREA----NRLFAVNQKNMTALEKKKEAV 1821
Cdd:TIGR04523 197 lklelLLSNlkKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1822 ESGKRQIENTLKEGNDILDE------------ANRLADEINSIIDYVEDIQTKLPPMSE---ELNNKIDDLSQEI----- 1881
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEisdlnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnses 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1882 ----KDRKLAEKVSQAESHAAQlNDSSavldgiLDEAKNISFNAtaafkaySNIKDYIDEAEKVAKEaKDlaheaTKLAT 1957
Cdd:TIGR04523 357 enseKQRELEEKQNEIEKLKKE-NQSY------KQEIKNLESQI-------NDLESKIQNQEKLNQQ-KD-----EQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1958 gprgllKEDAKGSLQKSF-RILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQA 2036
Cdd:TIGR04523 417 ------LQQEKELLEKEIeRLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2037 VKDKARQA---NDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKL 2113
Cdd:TIGR04523 491 LKSKEKELkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2114 KPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKK 2164
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2968-3102 |
1.25e-22 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 95.85 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2968 FRTTRTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagvPGHLCDGQWHKVTANKIKHRIELTVDGNQV 3046
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQtERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 3047 E-AQSLNPASTSADTNDPVFVGGFPDD-LKQFGLTTSIPFRGCVRSLKLtkgTGKPLE 3102
Cdd:pfam00054 77 PtGESPLGATTDLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIV---NGKPLD 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1606-2164 |
4.33e-22 |
|
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: 104.72 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1606 YKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKV----TADgEQTGQDAERTNTRAKSLGEF 1681
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknklLKL-ELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQ---MIKELRRKNLETQKeiAEDELVAAEGLLKKVK-KL 1757
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQ--NNKKIKELEKQLNQLKsEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1758 FGESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFA-----VNQKNMTALEKKKEaVESGKRQIENTL 1832
Cdd:TIGR04523 298 SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkeLTNSESENSEKQRE-LEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1833 KEGNDILDEANRLADEINSIIDYVEDiQTKLppmSEELNNKI-------DDLSQEIKDrkLAEKVSQAESHAAQLNDSSA 1905
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN-QEKL---NQQKDEQIkklqqekELLEKEIER--LKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1906 VLDGILDEAKNIsfnaTAAFKaySNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEdaKGSLQKSFRILNEAKKLa 1985
Cdd:TIGR04523 451 VKELIIKNLDNT----RESLE--TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--KKELEEKVKDLTKKISS- 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1986 ndVKENEDHLNGLKTRIENAdarngdlLRALNDTLGKLSAipNDTAAKLQAVKDKARQandtakdvlaQIKELHQNLDGL 2065
Cdd:TIGR04523 522 --LKEKIEKLESEKKEKESK-------ISDLEDELNKDDF--ELKKENLEKEIDEKNK----------EIEELKQTQKSL 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2066 KKNYDKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEAD-------RLIDKLKPIKELEDNLKKNISEIKELINQAR 2138
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKD--LIKEIEEKEKKISSLEKELEkakkeneKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622930585 2139 -KQAN---SIKVSVSSGGDCIRT-----------YKPEIKK 2164
Cdd:TIGR04523 659 nKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2368-2501 |
2.01e-21 |
|
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: 92.10 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2368 FRTFSSSALLMYlATRDLRDFMSVELTDGHIKVSYDLGSG-MASVVSNQNHNDGKWKSFTLSRIQKQANISIvdidtNQE 2446
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSV-----DGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 2447 ENIATSSSGNNFGLDLKADdkIYFGGLPTLRNLSmkarPEVNLKKYSGCLKDIEI 2501
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLP----ALPVRAGFVGCIRDVRV 123
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1669-2149 |
5.76e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.29 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1669 ERTNTRAKSLGEFIKELARDAEAVnEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELR---------RKNLETQKEI 1739
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1740 AED------ELVAAEGLLKKVKKLFGESRGKNEEMEK---DLREKLADYKN--KVDDAWDLLREATNKIREANR------ 1802
Cdd:PRK03918 237 KEEieelekELESLEGSKRKLEEKIRELEERIEELKKeieELEEKVKELKElkEKAEEYIKLSEFYEEYLDELReiekrl 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1803 -----LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNdILDEANRLADEINSIIDYVEDIQTKLPPMS-EELNNKIDD 1876
Cdd:PRK03918 317 srleeEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1877 LS---QEIKD--RKLAEKVSQAESHAAQLNDSSAVLDGI----------LDE--AKNIsfnataafkaysnIKDYIDEAE 1939
Cdd:PRK03918 396 LEkakEEIEEeiSKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEehRKEL-------------LEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1940 KVAKEAKDLAHEATKLatgpRGLLKEdAKGSLQKSFRILNEaKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDT 2019
Cdd:PRK03918 463 RIEKELKEIEEKERKL----RKELRE-LEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2020 LGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLK-KNYDKLADSVAKTnavvkDPSKNKIIadadaT 2098
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKEL-----EPFYNEYL-----E 606
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2099 VKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVS 2149
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2554-2692 |
5.64e-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: 79.39 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2554 FSTKNESGIILLGSGGtpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVVRPEPNLFHDGREHSVHVERTRG 2633
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG------------GSDFLALELVNGRLVLRYDLGSGP---ESLLSSGKNLNDGQWHSVRVERNGN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2634 IFTVQVD--ENRRYMQNLTVEQPLEVKKLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2692
Cdd:pfam02210 66 TLTLSVDgqTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2174-2311 |
1.25e-16 |
|
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: 78.62 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2174 VKTAVADNLLFYLGSAKfIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIMASRTGRNGTISVralDGpka 2253
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DG--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 2254 sivpsTYHSTSPPGYTILDVDANAMLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:pfam02210 74 -----QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1587-2133 |
2.49e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1587 ARLEQMVMSINLTGP-LPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTG 1665
Cdd:PRK03918 200 KELEEVLREINEISSeLPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1666 QDAERTNTRAKSLGEFIKeLARDAEAVNEKAIKLNETLGTrdeaFERNLEGLQKEIDQM------IKELRRKNLETQKEI 1739
Cdd:PRK03918 280 EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSR----LEEEINGIEERIKELeekeerLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1740 AEDE------------LVAAEGLLK--------KVKKLFGESRGKNEEMEKDLRE---KLADYKNKVDDawdlLREATNK 1796
Cdd:PRK03918 355 EELEerhelyeeakakKEELERLKKrltgltpeKLEKELEELEKAKEEIEEEISKitaRIGELKKEIKE----LKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1797 IREANRLFAVNQKNMTAlEKKKEAVESGKRQ---IENTLKEGNDILDEANRLADEINSIIDYVEDIqTKLPPMSEELNNK 1873
Cdd:PRK03918 431 LKKAKGKCPVCGRELTE-EHRKELLEEYTAElkrIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1874 IDDLSqEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNIsfnataafKAYSNIKDYIDEA-EKVAKEAKDLAHEA 1952
Cdd:PRK03918 509 EEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL--------EELKKKLAELEKKlDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1953 TKLATGPRGLLKE-------------DAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDT 2019
Cdd:PRK03918 580 EELGFESVEELEErlkelepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2020 lgklsaipndtaaKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKtnavvkdpsknkiIADADATV 2099
Cdd:PRK03918 660 -------------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE-------------REKAKKEL 713
|
570 580 590
....*....|....*....|....*....|....*
gi 1622930585 2100 KNLEQEADRLIDKLKPIKELEDNLKKN-ISEIKEL 2133
Cdd:PRK03918 714 EKLEKALERVEELREKVKKYKALLKERaLSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1650-2141 |
8.30e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1650 LLTRATKVTADGEQTGQ----DAERTNTRAKSLGEFIKELAR-DAEA-VN---------EKAIklNETLGTRdeafernl 1714
Cdd:PRK02224 82 HIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRmDAEAfVNcayvrqgevNKLI--NATPSDR-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1715 eglQKEIDQMikeLRRKNLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEME-KDLREKLADYKNKVDDawdlLREA 1793
Cdd:PRK02224 152 ---QDMIDDL---LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAE----LDEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1794 TNKIrEANRLFAVNQKN-----MTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSE 1868
Cdd:PRK02224 222 IERY-EEQREQARETRDeadevLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1869 ELNnkIDDLSQEIkdrkLAEKVSQAESHAAQLNDSsavldgiLDEAKnisfnaTAAFKAYSNIKDYIDEAEKVAKEAKDL 1948
Cdd:PRK02224 301 EAG--LDDADAEA----VEARREELEDRDEELRDR-------LEECR------VAAQAHNEEAESLREDADDLEERAEEL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1949 AHEATKLATGprgllKEDAKGSLQKSFRILNEakkLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLsaipN 2028
Cdd:PRK02224 362 REEAAELESE-----LEEAREAVEDRREEIEE---LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE----A 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2029 DTAAKLQAVKDKARQAN---------------------DTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKdps 2087
Cdd:PRK02224 430 ELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE--- 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 2088 knkiiadadatvknLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2141
Cdd:PRK02224 507 --------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1766-2145 |
1.36e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.96 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1766 EEMEKDLRE--KLADYKNkvddAWDLLREAtnkIREANRLfavnqknMTALEKKKEAVESGKRQIENTLKEGNDILDEAN 1843
Cdd:PRK03918 145 ESREKVVRQilGLDDYEN----AYKNLGEV---IKEIKRR-------IERLEKFIKRTENIEELIKEKEKELEEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1844 RLADEINSIIDYVEDIQTKLPPMsEELNNKIDDLSQEIKD-----RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNIS 1918
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESlegskRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1919 FNAtaafKAYSNIK----DYIDEAEKVAKEAKDLAHEAtklatgpRGLLKEDAKGSLQKSfrilnEAKKLANDVKENEDH 1994
Cdd:PRK03918 290 EKA----EEYIKLSefyeEYLDELREIEKRLSRLEEEI-------NGIEERIKELEEKEE-----RLEELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1995 LNGLKTRienadARNGDLLRALNDTLGKLSA-----IPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNY 2069
Cdd:PRK03918 354 LEELEER-----HELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930585 2070 DKLADSVAKT---NAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQaRKQANSIK 2145
Cdd:PRK03918 429 EELKKAKGKCpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLK 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1718-2077 |
1.75e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1718 QKEIDQMIK---ELRRKNLE---------TQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEK--DLREKLADYKNKV 1783
Cdd:TIGR02168 143 QGKISEIIEakpEERRAIFEeaagiskykERRKETERKLERTRENLDRLEDILNELERQLKSLERqaEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1784 DDA-WDLLreaTNKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEgndiLDEA-NRLADEINSIIDYVEDIQT 1861
Cdd:TIGR02168 223 RELeLALL---VLRLEELR-------EELEELQEELKEAEEELEELTAELQE----LEEKlEELRLEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1862 KLppmsEELNNKIDDLSQEIkdRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisFNATAAFKAYSNIKDYIDEAEKV 1941
Cdd:TIGR02168 289 EL----YALANEISRLEQQK--QILRERLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1942 AKEAKDLAHEATKLATGPRGLLKEDAKgslqKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALND--- 2018
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEael 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 2019 -----TLGKLSAIPNDTAAKLQAV----------KDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVA 2077
Cdd:TIGR02168 436 kelqaELEELEEELEELQEELERLeealeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1670-2228 |
1.94e-15 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 83.41 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1670 RTNTRAKSLGEFIKELARDAEAVNEKAIklnetLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAE-DELVAAE 1748
Cdd:PRK01156 94 RREAYIKKDGSIIAEGFDDTTKYIEKNI-----LGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEiNSLERNY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKlfgesrgkneemekDLREKLADYknkvDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQI 1828
Cdd:PRK01156 169 DKLKDVID--------------MLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1829 ENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLpPMSEELNNKIDDLSQEIKdrklaekvsQAESHAAQLNdSSAVLD 1908
Cdd:PRK01156 231 MDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNNYYKELEERHM---------KIINDPVYKN-RNYIND 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1909 GILDEAKNISFNataafKAYSNIKDYIDEAEKVAKEAKDlaheatklatgprglLKEDAKGSLQKSFRiLNEAKKLANDV 1988
Cdd:PRK01156 300 YFKYKNDIENKK-----QILSNIDAEINKYHAIIKKLSV---------------LQKDYNDYIKKKSR-YDDLNNQILEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1989 KENEDHLNG-------LKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQN 2061
Cdd:PRK01156 359 EGYEMDYNSylksiesLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2062 LDGLKKNYDKL-ADSVA----------KTNAVVKDPSKNKIIADADatVKNLEQEADRLIDKLKPIKELEDNLKKniSEI 2130
Cdd:PRK01156 439 LDELSRNMEMLnGQSVCpvcgttlgeeKSNHIINHYNEKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLES--EEI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2131 KELINQ------ARKQANSIKVSVSSGGDciRTYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:PRK01156 515 NKSINEynkiesARADLEDIKIKINELKD--KHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEI 592
|
570 580
....*....|....*....|....*..
gi 1622930585 2205 SF-LWDVGSGVGRVE--YPDltiDDSY 2228
Cdd:PRK01156 593 KKqLNDLESRLQEIEigFPD---DKSY 616
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1703-2096 |
2.18e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 81.10 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1703 LGTRDEAFERNLEGLQKEIDQMIKELrrknletqKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKdLREKLADYKNK 1782
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAAL--------SEQLRKALFELDKLQEELEQLREELEQAREELEQ-LEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1783 VDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTK 1862
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1863 LppmsEELNNKIDDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVA 1942
Cdd:COG4372 152 L----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1943 KEAKDLaheaTKLATGPRGLLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDL-LRALNDTLG 2021
Cdd:COG4372 221 LEAKDS----LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEaLEEAALELK 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 2022 KLSAIPNDTAAKLQAVKDKARQANdtAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADAD 2096
Cdd:COG4372 297 LLALLLNLAALSLIGALEDALLAA--LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1705-1990 |
4.63e-15 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 78.80 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1705 TRDEAFERNLEGLQKEIDQM---IKELRRKNLETQKEIAEdelVAAE--GLLKKVKKLFGESRGKNEEMeKDLREKLADY 1779
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1780 KNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEN---TLKEGNDILDEANRLADEInsiidyv 1856
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKEL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1857 EDIQtklppMSEELNNKIDDLSQEIKD---------RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisfnataafKA 1927
Cdd:COG1340 150 EKAK-----KALEKNEKLKELRAELKElrkeaeeihKKIKELAEEAQELHEEMIELYKEADELRKEAD----------EL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 1928 YSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKsfrILNEAKKLANDVKE 1990
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREK---EKEELEEKAEEIFE 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1717-2207 |
7.83e-15 |
|
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: 81.65 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1717 LQKEIDQMIK----ElRRKNLETQKEIAE--DELVAAEGLLKKVKKLFGESRGKNEEMEKDLrEKLADYKNKVDDAWDLL 1790
Cdd:TIGR02169 140 LQGDVTDFISmspvE-RRKIIDEIAGVAEfdRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1791 REatnkIREANRLFAVNQKNmtALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEE- 1869
Cdd:TIGR02169 218 KE----KREYEGYELLKEKE--ALERQKEAIE---RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEe 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1870 ---LNNKIDDLSQEIK--DRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfnataafkaySNIKDYIDEAEKVAKE 1944
Cdd:TIGR02169 289 qlrVKEKIGELEAEIAslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE----------REIEEERKRRDKLTEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1945 AKDLAHEATKLatgprgllkedakgslqksfriLNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRA---LNDTLG 2021
Cdd:TIGR02169 359 YAELKEELEDL----------------------RAELEEVDKEFAETRDELKDYREKLEKLKREINELKREldrLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2022 KLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSV----AKTNAVVKDPSK-NKIIADAD 2096
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlkEEYDRVEKELSKlQRELAEAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2097 ATVKNLEQEAdrlIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSsggdcirtykpeikkGSYNNIVVNvKT 2176
Cdd:TIGR02169 497 AQARASEERV---RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---------------NRLNNVVVE-DD 557
|
490 500 510
....*....|....*....|....*....|.
gi 1622930585 2177 AVAdnllfylgsAKFIDFLAiEMRKGKVSFL 2207
Cdd:TIGR02169 558 AVA---------KEAIELLK-RRKAGRATFL 578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1630-2150 |
8.63e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNEL--------------LTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEK 1695
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLeqqkqilrerlanlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1696 AIKLNETLgtrdeafeRNLEGLQKEIDQMIKELRRK----------------NLETQKEIAEDEL---------VAAEGL 1750
Cdd:TIGR02168 360 LEELEAEL--------EELESRLEELEEQLETLRSKvaqlelqiaslnneieRLEARLERLEDRRerlqqeieeLLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1751 LKKVKKLFGESRGKNEEMEkDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEN 1830
Cdd:TIGR02168 432 EAELKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1831 TLKEGNDILDEANRLADEINSIIDYVEDIQTKLppmSEELNNKIDDLSQEIKD------RKLAEKVSQAE--SHAAQLND 1902
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSELISVDEGYEAAIEAAL---GGRLQAVVVENLNAAKKaiaflkQNELGRVTFLPldSIKGTEIQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1903 SS-----AVLDGILDEAKNISFNATAAFKAYSN------IKDYIDEAEKVAKEakdLAHEATkLAT------GPRGLL-K 1964
Cdd:TIGR02168 588 GNdreilKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKK---LRPGYR-IVTldgdlvRPGGVItG 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1965 EDAKGS---LQKSFRILN---EAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTA---AKLQ 2035
Cdd:TIGR02168 664 GSAKTNssiLERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVE 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2036 AVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNkiIADADATVKNLEQEADRLIDKLKP 2115
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE--LKALREALDELRAELTLLNEEAAN 821
|
570 580 590
....*....|....*....|....*....|....*
gi 1622930585 2116 IKELEDNLKKNISEIKELINQARKQANSIKVSVSS 2150
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1705-2145 |
1.13e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.45 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1705 TRDEAFERNLEGLQKEIDQmiKELRRKNLEtqkeiaedelvaaEGLLKKVKKlFGESRGKNEEME---KDLREKLADYKN 1781
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKN--KEKELKNLD-------------KNLNKDEEK-INNSNNKIKILEqqiKDLNDKLKKNKD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1782 KVDDawdLLREATNKIREANrlfaVNQKNMTALEKKkeaVESGKRQIENTLKEGNDILDEANRLADEInsiidyvediqt 1861
Cdd:TIGR04523 97 KINK---LNSDLSKINSEIK----NDKEQKNKLEVE---LNKLEKQKKENKKNIDKFLTEIKKKEKEL------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1862 klppmsEELNNKIDDLSQEI-------------------------------------------KDRKLAEKVSQAESHAA 1898
Cdd:TIGR04523 155 ------EKLNNKYNDLKKQKeelenelnllekeklniqknidkiknkllklelllsnlkkkiqKNKSLESQISELKKQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1899 QLNDSSavldgildEAKNISFNA-TAAFK-AYSNIKDYIDEAEKVAKEAKDLAHEATKLATgprgLLKEDAKG--SLQKS 1974
Cdd:TIGR04523 229 QLKDNI--------EKKQQEINEkTTEISnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK----KIKELEKQlnQLKSE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1975 FRILNEAKK--LANDVKEN-------------------------EDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIP 2027
Cdd:TIGR04523 297 ISDLNNQKEqdWNKELKSElknqekkleeiqnqisqnnkiisqlNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2028 NDTAAKLQAVKDKARQAND----------TAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKD-----PSKNKII 2092
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDleskiqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDltnqdSVKELII 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 2093 ADADATVKNLEQEADRLIDKLKPIK-ELEDN---LKKNISEIKELINQARKQANSIK 2145
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKqNLEQKqkeLKSKEKELKKLNEEKKELEEKVK 513
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
917-965 |
5.60e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 68.53 E-value: 5.60e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 917 PCRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGLQS-ARGCV 965
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1700-2147 |
1.24e-13 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 77.95 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1700 NETLGTRDEAFERN---LEGLQKEIDQMIKELRRKNLETQKEIAEDELVAA--EGLLKKVKKLFGESRGKNEEMEKDLRE 1774
Cdd:PTZ00440 360 LEMLSMLDSLLIKKekiLNNLFNKLFGDLKEKIETLLDSEYFISKYTNIISlsEHTLKAAEDVLKENSQKIADYALYSNL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1775 KLADYKNKVDDAWDLLREATNK-------IREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLAD 1847
Cdd:PTZ00440 440 EIIEIKKKYDEKINELKKSINQlktlisiMKSFYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNN 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDYVEDIqtklppmsEELNNKIDDLSQEIKDRKLA-EKVSQAESHAAQLNDSsavldgILDEAKNISFNATAAFK 1926
Cdd:PTZ00440 520 NFKNIEDYYITI--------EGLKNEIEGLIELIKYYLQSiETLIKDEKLKRSMKND------IKNKIKYIEENVDHIKD 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1927 AYS---NIKDYIDEAEKVAKEA----KDLAHEATKLATGPRGLLKEDAKGSLQ--------------KSFR--------- 1976
Cdd:PTZ00440 586 IISlndEIDNIIQQIEELINEAlfnkEKFINEKNDLQEKVKYILNKFYKGDLQelldelshflddhkYLYHeakskedlq 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1977 -ILNEAK----KL-----------ANDVKENEDHLNGLKTRI--ENADARNGDLLRALNDTLGKLSAIP---NDTAAKLQ 2035
Cdd:PTZ00440 666 tLLNTSKneyeKLefmksdnidniIKNLKKELQNLLSLKENIikKQLNNIEQDISNSLNQYTIKYNDLKssiEEYKEEEE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2036 AVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLAdsvakTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKP 2115
Cdd:PTZ00440 746 KLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFL-----QYKDTILNKENKISNDINILKENKKNNQDLLNSYNIL 820
|
490 500 510
....*....|....*....|....*....|..
gi 1622930585 2116 IKELEDNLKKNISEIKELINQARKQANSIKVS 2147
Cdd:PTZ00440 821 IQKLEAHTEKNDEELKQLLQKFPTEDENLNLK 852
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1635-2076 |
2.12e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1635 LAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETL-GTRDEAFERn 1713
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDR- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1714 lEGLQKEIDQMIKELRRK--NLETQKEIAEDELvaaegllkkvkklfgesrgkneemeKDLREKLADYKNKVDDAWDLLR 1791
Cdd:PRK02224 383 -REEIEELEEEIEELRERfgDAPVDLGNAEDFL-------------------------EELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1792 EATNKIREANRLFAVNQ-----------KNMTALEKKKEAVESGKRQIEntlkegnDILDEANRLADEINSIIDYVEdiq 1860
Cdd:PRK02224 437 TARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELE-------DLEEEVEEVEERLERAEDLVE--- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1861 tkLPPMSEELNNKIDDLSQEIKDRK--LAEKVSQAEShaaqLNDSSAVLDGILDEAKNisfnatAAFKAYsnikdyiDEA 1938
Cdd:PRK02224 507 --AEDRIERLEERREDLEELIAERRetIEEKRERAEE----LRERAAELEAEAEEKRE------AAAEAE-------EEA 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1939 EKVAKEAKDLaheatklatgprgllkEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNgDLLRalnD 2018
Cdd:PRK02224 568 EEAREEVAEL----------------NSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN-DERR---E 627
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930585 2019 TLGKLSAIPNDTAAKLQAVK-DKARQANDTAKDVLAQIKElhqNLDGLKKNYDKLADSV 2076
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEE---KLDELREERDDLQAEI 683
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
918-964 |
2.51e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 918 CRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGLQ--SARGC 964
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-2135 |
2.56e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLN--------ETLGTRDEAFERNLEGLQKEID---QMIKELRRKNLETQKEIA--EDELVAAEGLLKKVKKLF 1758
Cdd:TIGR02168 433 AELKELQAEleeleeelEELQEELERLEEALEELREELEeaeQALDAAERELAQLQARLDslERLQENLEGFSEGVKALL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1759 GESRGKN------------EE-----MEKDLREKLADY----KNKVDDAWDLLREAtNKIREAnrLFAVNQKNMTALEKK 1817
Cdd:TIGR02168 513 KNQSGLSgilgvlselisvDEgyeaaIEAALGGRLQAVvvenLNAAKKAIAFLKQN-ELGRVT--FLPLDSIKGTEIQGN 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1818 KEavesgkrqieNTLKEGNDILDEANRL---ADEINSIIDY-------VEDIQT------KLPPM--------------- 1866
Cdd:TIGR02168 590 DR----------EILKNIEGFLGVAKDLvkfDPKLRKALSYllggvlvVDDLDNalelakKLRPGyrivtldgdlvrpgg 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1867 -----SEELNNKIDDLSQEIKDrkLAEKVSQAESHAAQLNDSSAVLDGILDEAKN-----------ISFNATAAFKAYSN 1930
Cdd:TIGR02168 660 vitggSAKTNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELEELEEeleqlrkeleeLSRQISALRKDLAR 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1931 IKDyidEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSfRILNEAKKLANDVKENEDHLNGLKTRIENADARNG 2010
Cdd:TIGR02168 738 LEA---EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2011 DLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVL---AQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPS 2087
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2088 KNKI-----IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELIN 2135
Cdd:TIGR02168 894 SELEelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1612-2147 |
2.69e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertNTRAKSLGEF-IKELARDAE 1690
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE--------------EEKEKKLQEEeLKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1691 AVNEKAIKLnetlGTRDEAFERNLEGLQKEIDQMIKELrrknLETQKEIAEDElvaaegllkKVKKLFGESRGKNEEMEK 1770
Cdd:pfam02463 297 ELKSELLKL----ERRKVDDEEKLKESEKEKKKAEKEL----KKEKEEIEELE---------KELKELEIKREAEEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1771 DLREKLADYKNKVDDAWDLLREATNKIREANRLFavNQKNMTALEKKKEAvesgKRQIENTLKEGNDILDEANRLADEIN 1850
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEA----QLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1851 SIIDYVEDIQTKLPPMSEEL-------NNKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFN--- 1920
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELekqelklLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvll 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1921 -----------------------ATAAFKAY---------SNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAK 1968
Cdd:pfam02463 514 alikdgvggriisahgrlgdlgvAVENYKVAistavivevSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1969 GSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTA 2048
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2049 KDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADadatvknLEQEADRLIDKLKPIKELEDNLKKNIS 2128
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-------EELLADRVQEAQDKINEELKLLKQKID 746
|
570
....*....|....*....
gi 1622930585 2129 EIKELINQARKQANSIKVS 2147
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEE 765
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1656-2184 |
3.25e-13 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 76.41 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1656 KVTADGEQTGQdAERTNTRAKSLG---EFIKELARDAEAVNEKAIKLNETLGTRDEaFERNLeglqkeIDQMIKELRRKN 1732
Cdd:PTZ00440 1111 VVNADKEKNKQ-TEHYNKKKKSLEkiyKQMEKTLKELENMNLEDITLNEVNEIEIE-YERIL------IDHIVEQINNEA 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1733 LETQKEIAEDELVAAEGLLKKvKKLFGESRGKNEEME-KDLREKLADYKNKVDDawdLLREATNKIREANRlfavnQKNM 1811
Cdd:PTZ00440 1183 KKSKTIMEEIESYKKDIDQVK-KNMSKERNDHLTTFEyNAYYDKATASYENIEE---LTTEAKGLKGEANR-----STNV 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1812 TALEKKKEAVESGKRQ-------IENTLKE------------GNDILDE-----------ANRLADEINSIIDYVEDIQT 1861
Cdd:PTZ00440 1254 DELKEIKLQVFSYLQQvikennkMENALHEiknmyeflisidSEKILKEilnstkkaeefSNDAKKELEKTDNLIKQVEA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1862 KLPPMSEELN---------------NKIDDLSQEIKDRKLA---------EKVSQAESHAAQLNDSSAVLDgILDEAKNI 1917
Cdd:PTZ00440 1334 KIEQAKEHKNkiygsledkqiddeiKKIEQIKEEISNKRKEinkylsnikSNKEKCDLHVRNASRGKDKID-FLNKHEAI 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1918 SFNATAAFKAySNIKDYIDEAEKVAKEAKDLA-------------------------------------HEATKLATGPR 1960
Cdd:PTZ00440 1413 EPSNSKEVNI-IKITDNINKCKQYSNEAMETEnkadenndsiikyekeitnilnnssilgkktklekkkKEATNIMDDIN 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1961 G---LLKEDAKgSLQKSFRILNEAKklanDVKENEDHLNGLKTRIENadarngdLLRALNdtLGKL-SAIPNdtaakLQA 2036
Cdd:PTZ00440 1492 GehsIIKTKLT-KSSEKLNQLNEQP----NIKREGDVLNNDKSTIAY-------ETIQYN--LGRVkHNLLN-----ILN 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2037 VKDKAR----QANDTAKDVL--AQIKElHQNLDGLKK---NYDKLADSVAKTNAVVKDpSKNKIIaDADATVKNLEQEAD 2107
Cdd:PTZ00440 1553 IKDEIEtilnKAQDLMRDISkiSKIVE-NKNLENLNDkeaDYVKYLDNILKEKQLMEA-EYKKLN-EIYSDVDNIEKELK 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2108 RL-----IDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSsggdcIRTYKPE------IKK---------GSY 2167
Cdd:PTZ00440 1630 KHkknyeIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFY-----LNKYNINenlekyKKKlneiynefmESY 1704
|
650
....*....|....*..
gi 1622930585 2168 NNIVVNVKTAVADNLLF 2184
Cdd:PTZ00440 1705 NIIQEKMKEVSNDDVDY 1721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1640-2133 |
3.62e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1640 LNTLVTEMNELLT------------RATKVTADG-----EQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET 1702
Cdd:PRK02224 208 LNGLESELAELDEeieryeeqreqaRETRDEADEvleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1703 LGTRDEAFERNLEGLQ-KEIDQMIKELRRKNLETQKEIAEDELV-----------AAEGLLKKVKKLFGESRGKNEEMEk 1770
Cdd:PRK02224 288 LEELEEERDDLLAEAGlDDADAEAVEARREELEDRDEELRDRLEecrvaaqahneEAESLREDADDLEERAEELREEAA- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1771 DLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQI-------ENTLKEGNDILDEAN 1843
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELrereaelEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1844 RLADEIN-----------SIIDYVEDIQTKLPPMSEELNN---KIDDLSQEIkDRklAEKVSQAESHAAQLNDSSAVLDG 1909
Cdd:PRK02224 447 ALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDleeEVEEVEERL-ER--AEDLVEAEDRIERLEERREDLEE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1910 ILDEAKNIsfnataafkaysnIKDYIDEAEKVAKEAKDLAHEATKlatgprgllKEDAKGSLQKsfrilnEAKKLANDVK 1989
Cdd:PRK02224 524 LIAERRET-------------IEEKRERAEELRERAAELEAEAEE---------KREAAAEAEE------EAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1990 ENEDHLNGLKTRIEnadarngdllrALNDTLGKLSAIPN--DTAAKLQAVKDKARQANDTAKDVLAQIKELHqnldglkk 2067
Cdd:PRK02224 576 ELNSKLAELKERIE-----------SLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERK-------- 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2068 nyDKLADSVaktnavvkDPSKnkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI----SEIKEL 2133
Cdd:PRK02224 637 --RELEAEF--------DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
918-964 |
3.99e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 3.99e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 918 CRCNANGSFSEICHSQTGQCECRANVQGQRCDKCKPGTFGlQSARGC 964
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1680-2168 |
2.03e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1680 EFIKElardaEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELvaaegLLKKVKKLFG 1759
Cdd:pfam02463 167 LKRKK-----KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL-----LYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1760 ESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDIL 1839
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1840 DEAN----RLADEINSIIDYVEDIQTKLppmseelnnkiddLSQEIKDRKLAEKVSQAEshaAQLNDSSAVLDGILDEAK 1915
Cdd:pfam02463 317 KESEkekkKAEKELKKEKEEIEELEKEL-------------KELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1916 NISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLA----HEATKLATgprgllKEDAKGSLQKSFRILNEAKklANDVKEN 1991
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELArqleDLLKEEKK------EELEILEEEEESIELKQGK--LTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1992 EDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKEL----HQNLDGLKK 2067
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggrIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2068 NYD--KLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNIS--EIKELINQARKQANS 2143
Cdd:pfam02463 533 DLGvaVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvlEIDPILNLAQLDKAT 612
|
490 500
....*....|....*....|....*
gi 1622930585 2144 IKVSVSSGGDCIRTYKPEIKKGSYN 2168
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKL 637
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1711-2207 |
2.13e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1711 ERNLEGL--QKEIDQMIKELRRKNLETQKEIAEDELVAAEGLLKKVKklfgESRGKNEEMEKDLREKLADYKNKVDDAWD 1788
Cdd:TIGR02168 199 ERQLKSLerQAEKAERYKELKAELRELELALLVLRLEELREELEELQ----EELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1789 LLREATNKIREAN-RLFAVNQKnMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIidyVEDIQTKLppms 1867
Cdd:TIGR02168 275 EVSELEEEIEELQkELYALANE-ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE---LAELEEKL---- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1868 EELNNKIDDLSQEIKdrklaekvsqaeshaaqlndssavldgildeaknisfnataafkaysnikdyidEAEKVAKEAKD 1947
Cdd:TIGR02168 347 EELKEELESLEAELE------------------------------------------------------ELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1948 LAHEATKLATGPRgllkedakgslQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALndtlgklsaip 2027
Cdd:TIGR02168 373 RLEELEEQLETLR-----------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL----------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2028 ndtaaklqavkdkarqandtakdVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKdpSKNKIIADADATVKNLEQEAD 2107
Cdd:TIGR02168 431 -----------------------EEAELKELQAELEELEEELEELQEELERLEEALE--ELREELEEAEQALDAAERELA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2108 RLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI-----KVSVSSGgdcirtYKPEIKK---GSYNNIVVNVKTAVA 2179
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEG------YEAAIEAalgGRLQAVVVENLNAAK 559
|
490 500
....*....|....*....|....*...
gi 1622930585 2180 DNllfylgsakfIDFLAiEMRKGKVSFL 2207
Cdd:TIGR02168 560 KA----------IAFLK-QNELGRVTFL 576
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1639-2143 |
2.20e-12 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 73.71 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1639 NLNTLVTEMNELLTRATKVTADGEQTGQ-----DAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEafern 1713
Cdd:PTZ00440 1549 NILNIKDEIETILNKAQDLMRDISKISKivenkNLENLNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDN----- 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1714 legLQKEIDQMIKELRRKNLETQKEIAEDelvaaegllkkvKKLFGESRGK--------------NEEMEK-DLREKLAD 1778
Cdd:PTZ00440 1624 ---IEKELKKHKKNYEIGLLEKVIEINKN------------IKLYMDSTKEslnslvnnfsslfnNFYLNKyNINENLEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1779 YKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRlaDEINSIIDYVED 1858
Cdd:PTZ00440 1689 YKKKLNEIYNEFMESYNIIQEKMKEVSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK--QESFRFILYMKE 1766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1859 IQTKLPPMSEELNNKIDD-------LSQEIK----DRKLAEKVSQAE---------SHAAQLNDSSAVLDGILDEAKNIS 1918
Cdd:PTZ00440 1767 KLDELSKMCKQQYNIVDEgynyikkKIEYIKtlndENNLSDSLNQAEdknkevanlTHYTNKNEAKNLLGHVVKSANFIG 1846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1919 FNATAAFkAYSNIKDyiDEAEKVAKEAKDLAHEATKLATGPRGLLK------EDAKGSLQKSFRIL-------------N 1979
Cdd:PTZ00440 1847 IKIMTGL-QPTELTP--DASLETAPELTFESENNSDLELDHLSSNKneldvyKNIQDAYKSSLQILkysddidkkqrdcN 1923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1980 EAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAI--------------PNDTAAKLQAVKDKARQAN 2045
Cdd:PTZ00440 1924 KLVEDGNEIYLKSTAINELKNMINSVKNKESAISNKIDNVSNKLSELnkitcndesydeilEKEEYEELKDLRNSFNQEK 2003
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2046 D-TAKDVlaQIKELHQNLDGLKKNYDKLADSVAKTNA------VVKDpsKNKIIADADATVKNLEQEA-------DRLID 2111
Cdd:PTZ00440 2004 AeTLNNL--KLNKIKEDFNSYKNLLDELEKSVKTLKAsenikkIVEN--KKTSIDAINTNIEDIEKEIesinpslDELLK 2079
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622930585 2112 KLKPIK-----ELEDNLKKNISEIKELINQARKQANS 2143
Cdd:PTZ00440 2080 KGHKIEisrytSIIDNVQTKISNDSKNINDIEKKAQI 2116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1676-2140 |
2.54e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.88 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1676 KS-LGEFIKELARDAeaVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKEL--------RRKNLETQKEIAEDELVA 1746
Cdd:COG4717 36 KStLLAFIRAMLLER--LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyaelqeELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1747 AEGLLKKVKKLfgESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAvnqknmtALEKKKEAVESGKR 1826
Cdd:COG4717 114 LREELEKLEKL--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-------ELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1827 QIEN-TLKEGNDILDEANRLADEINSIIDYVEDIQTKLppmsEELNNKIDDLSQEIKDRKLAEKVSQAESHAAQLNdSSA 1905
Cdd:COG4717 185 QLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIAA-ALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1906 VLDGILDEAKNISFNATAAF---------------KAYSNIKDYIDEAEKVAKEaKDLAHEATKLATGPRGLLKEDAKGS 1970
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPAL-EELEEEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1971 LQKSFRILNEAKKLANDVKENEDHLnglktRIENADARNGDLLRALNdtlgklsaipndtAAKLQAVKDKARQANDtAKD 2050
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAG-------------VEDEEELRAALEQAEE-YQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2051 VLAQIKELHQNLDGLKKNYDKLADsvaktnavvkdpsknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNLKKNISEI 2130
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLE---------------------ALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
490
....*....|
gi 1622930585 2131 KELINQARKQ 2140
Cdd:COG4717 459 EAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1813-2148 |
2.57e-12 |
|
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: 73.18 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1813 ALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKDRK-----LA 1887
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKselkeLE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1888 EKVSQAESHAAQLNDSSAVLDGILDEaknisfnataafkaySNIKDYIDEAEKVAKEAKDL--AHEATKLATGPRGLLKE 1965
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSH---------------SRIPEIQAELSKLEEEVSRIeaRLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1966 DAKGSLQKSFRILNEAKKLANDVKENEDHLNG----LKTRIENADARngdlLRALNDTLGKLSAIPNDTAAKLQAVKDKA 2041
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAA----LRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2042 RQAN---DTAKDVLAQIKELHQNLDGLKKNYDKLadsvakTNAVVKDPSKNKIIADADATVKNLE--------------Q 2104
Cdd:TIGR02169 906 EELEaqiEKKRKRLSELKAKLEALEEELSEIEDP------KGEDEEIPEEELSLEDVQAELQRVEeeiralepvnmlaiQ 979
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622930585 2105 EADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
967-1011 |
2.89e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.48 E-value: 2.89e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930585 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSFQEGGC 1011
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1637-2147 |
3.65e-12 |
|
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: 73.16 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1637 EGNLNTLVTEMNELLTRATKVTAD--GE---QTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETlgtrdeafe 1711
Cdd:TIGR01612 721 ELHLSNIENKKNELLDIIVEIKKHihGEinkDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEI--------- 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1712 RNLEGLQKEIDQMIKELRRKNLETQKE------IAEDELVAA--------EGLLKKVKKL-----------------FGE 1760
Cdd:TIGR01612 792 KNHYNDQINIDNIKDEDAKQNYDKSKEyiktisIKEDEIFKIinemkfmkDDFLNKVDKFinfennckekidseheqFAE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1761 --SRGKNEEMEkdlrEKLADYKNKVDDAWDLLREATNKIREA----NRLFAVNQKnMTALEKKKEAVES--GKRQIEN-- 1830
Cdd:TIGR01612 872 ltNKIKAEISD----DKLNDYEKKFNDSKSLINEINKSIEEEyqniNTLKKVDEY-IKICENTKESIEKfhNKQNILKei 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1831 ------TLKEGNDILDE-----ANRLADEINSIidyvEDIQTKLPPMSEELNNkiDDLSQEIKDRKLAEKVSQAESHAAQ 1899
Cdd:TIGR01612 947 lnknidTIKESNLIEKSykdkfDNTLIDKINEL----DKAFKDASLNDYEAKN--NELIKYFNDLKANLGKNKENMLYHQ 1020
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1900 LNDSSAVLDGILDEAKNISFN-ATAAFKAYSNIKDYIDEAEK-VAKEAKDLAHEatklatgprgLLKEdAKGSLqKSFRI 1977
Cdd:TIGR01612 1021 FDEKEKATNDIEQKIEDANKNiPNIEIAIHTSIYNIIDEIEKeIGKNIELLNKE----------ILEE-AEINI-TNFNE 1088
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1978 LNEAKKLAN--D-VKENE----DHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAA---KLQAVKDKArQANDT 2047
Cdd:TIGR01612 1089 IKEKLKHYNfdDfGKEENikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAqinDLEDVADKA-ISNDD 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2048 AKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATV-KNLEQEADRLIDKLKP-----IKELE- 2120
Cdd:TIGR01612 1168 PEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYgKNLGKLFLEKIDEEKKksehmIKAMEa 1247
|
570 580 590
....*....|....*....|....*....|....*
gi 1622930585 2121 -----DNLKKNISEIKELIN---QARKQANSIKVS 2147
Cdd:TIGR01612 1248 yiedlDEIKEKSPEIENEMGiemDIKAEMETFNIS 1282
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1661-2012 |
5.37e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 70.32 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1661 GEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKN-----LET 1735
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL----EQLREELEQAREELEQLEEELEQARseleqLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1736 QKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDL------REKLADYKNKVDDAWDLLREA-TNKIREANRLfavnQ 1808
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELeelqkeRQDLEQQRKQLEAQIAELQSEiAEREEELKEL----E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1809 KNMTALEKKKEAVESGKRQIENTLKEG--NDILDEANRLAdeinsiidYVEDIQTKLPPMSEELNNKIDDLSQEIKDRKL 1886
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQalDELLKEANRNA--------EKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1887 AEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKED 1966
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622930585 1967 AKGSLQKSFRILNE--AKKLANDVKENEDHLNGLKTRIENADARNGDL 2012
Cdd:COG4372 309 LIGALEDALLAALLelAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1682-2149 |
7.75e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.47 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELARDAEAVNEKAIKLNETLgtrdeafeRNLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEGLLKKVKKLFGES 1761
Cdd:PRK01156 220 IERLSIEYNNAMDDYNNLKSAL--------NELSSLEDMKNRYESEIKT--AESDLSMELEKNNYYKELEERHMKIINDP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1762 RGKNeemekdlREKLADYKNKVDDAWDL------LREATNKIREANRLFAVNQKNMTALEKKKE---------------- 1819
Cdd:PRK01156 290 VYKN-------RNYINDYFKYKNDIENKkqilsnIDAEINKYHAIIKKLSVLQKDYNDYIKKKSryddlnnqilelegye 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1820 --------AVESGKRQIENTLKEGNDILDEANRL-------ADEINSIIdyvEDIQTKLppmsEELNNKIDDLSQEIkdR 1884
Cdd:PRK01156 363 mdynsylkSIESLKKKIEEYSKNIERMSAFISEIlkiqeidPDAIKKEL---NEINVKL----QDISSKVSSLNQRI--R 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1885 KLAEKVSQAESHAAQLNDSSA--VLDGILDEAKnisfnataafkaySN--IKDYIDEAEKVAKEAKDLAHEATKLATGPR 1960
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSVcpVCGTTLGEEK-------------SNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1961 GLLKED---AKGSLQKSFRILNEAKKLANDVKENEDHLNGLK---TRIENADARN-----GDLLRALNDTLGKLSAIPNd 2029
Cdd:PRK01156 501 DLKKRKeylESEEINKSINEYNKIESARADLEDIKIKINELKdkhDKYEEIKNRYkslklEDLDSKRTSWLNALAVISL- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2030 taAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLK----KNYDKLADSVAKTNAVVKDPSKNKIIADA-DATVKNLEQ 2104
Cdd:PRK01156 580 --IDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEANNLNNKYNEIQENKILIEKlRGKIDNYKK 657
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622930585 2105 EadrlIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVS 2149
Cdd:PRK01156 658 Q----IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1649-2142 |
9.15e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 71.40 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1649 ELLTRATKVTADGEQTgqdAERTNTRAKSLGEFIKELARDAEAVNEKAIKlnetlGTRDEAfERNLEGLQKEIDQmikEL 1728
Cdd:NF041483 510 EAIERATTLRRQAEET---LERTRAEAERLRAEAEEQAEEVRAAAERAAR-----ELREET-ERAIAARQAEAAE---EL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1729 RRKNLEtqkeiAEDELVAAEGLLkkvkklfGESRGKNEEMEKDLREKLadyknkvddawDLLR-EATNKIR--------E 1799
Cdd:NF041483 578 TRLHTE-----AEERLTAAEEAL-------ADARAEAERIRREAAEET-----------ERLRtEAAERIRtlqaqaeqE 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1800 ANRL-----------------FAVNQKNMTALEK---KKEAVESGKR-------QIENTLKEGNDIL----DEANRL--- 1845
Cdd:NF041483 635 AERLrteaaadasaaraegenVAVRLRSEAAAEAerlKSEAQESADRvraeaaaAAERVGTEAAEALaaaqEEAARRrre 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1846 ADEI-NSIIDYVEDIQTKLPPMSEEL----NNKIDDLSQEIK------DRKLAEKVSQAESHAAQLNDSSAvldGILDEA 1914
Cdd:NF041483 715 AEETlGSARAEADQERERAREQSEELlasaRKRVEEAQAEAQrlveeaDRRATELVSAAEQTAQQVRDSVA---GLQEQA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1915 KN-ISFNATAAFKAYSNIK-DYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILN----EAKKLANDV 1988
Cdd:NF041483 792 EEeIAGLRSAAEHAAERTRtEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaiaEAERLRSDA 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1989 KENEDhlnglKTRIENADAR---NGDLLRALNDTLGKLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIKELHQNLDGL 2065
Cdd:NF041483 872 SEYAQ-----RVRTEASDTLasaEQDAARTRADAREDANRIRSDAAA--QADRLIGEATSEAERLTAEARAEAERLRDEA 944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2066 KKNYDKL-ADSVAKTNAVVKDPSKN--KIIADADATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNISEIKELINQA 2137
Cdd:NF041483 945 RAEAERVrADAAAQAEQLIAEATGEaeRLRAEAAETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEAREEADRTLDEA 1024
|
....*
gi 1622930585 2138 RKQAN 2142
Cdd:NF041483 1025 RKDAN 1029
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1684-2140 |
9.96e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1684 ELARDAEAVNE-KAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRknletQKEIAEDELVAAEGLLKKVKKLFGESR 1762
Cdd:PTZ00121 1221 EDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR-----QAAIKAEEARKADELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1763 GKNEEMEK-DLREKLADYKNKVDDAWDLLREA-------TNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKE 1834
Cdd:PTZ00121 1296 KKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAkkkadaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1835 GNDILDEANRLADEINSiidyVEDIQTKlppmSEELNNKIDDLSQEIKDRKLAEkvsQAESHAAQLNDSsavldgilDEA 1914
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKK----ADEAKKK----AEEDKKKADELKKAAAAKKKAD---EAKKKAEEKKKA--------DEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1915 KNisfNATAAFKAysnikdyiDEAEKVAKEAKDlAHEATKLAtgprgllkEDAKGSlqksfrilNEAKKLANDVKENEDh 1994
Cdd:PTZ00121 1437 KK---KAEEAKKA--------DEAKKKAEEAKK-AEEAKKKA--------EEAKKA--------DEAKKKAEEAKKADE- 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1995 lngLKTRIENADARNGDLLRAlndtlgklsaipndTAAKLQAvkDKARQANDTAKDVLAQIKELHQNLDGLKKNYD-KLA 2073
Cdd:PTZ00121 1488 ---AKKKAEEAKKKADEAKKA--------------AEAKKKA--DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkKKA 1548
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930585 2074 DSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKLKPIKE--LEDNLKKNISEIKELINQARKQ 2140
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1692-2145 |
1.18e-11 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 70.37 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRDEAFErnleglqkEIDQMIKELRRKNLETQKEIAEDELVAAEGLLKKVKKlfgesrgkneEMEKD 1771
Cdd:COG5185 102 YVNSLIKLPNYEWSADILIS--------LLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVET----------GIIKD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1772 LREKLADYKNKVddawdllreatNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEG-NDILDEAnrlADEIN 1850
Cdd:COG5185 164 IFGKLTQELNQN-----------LKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGsESTLLEK---AKEII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1851 SIIDYVEDIQ--TKLPPMSEELNNKIDDLSQEIKDRKLAEKVSQAEShaaqlndssavldgildeAKNISFNATAAFKAY 1928
Cdd:COG5185 230 NIEEALKGFQdpESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAES------------------SKRLNENANNLIKQF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1929 SNIKDYIDEAEKVAK------EAKDLAHEATKLATGPRGLLKEDAKgsLQKSFR-ILNEAKKLA---NDVKENEDHLNGL 1998
Cdd:COG5185 292 ENTKEKIAEYTKSIDikkateSLEEQLAAAEAEQELEESKRETETG--IQNLTAeIEQGQESLTenlEAIKEEIENIVGE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1999 KtRIENADARngdlLRALNDTLGKL-SAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNY-------D 2070
Cdd:COG5185 370 V-ELSKSSEE----LDSFKDTIESTkESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNeevskllN 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2071 KLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIK-----------ELEDNLKKNISEIKELINQark 2139
Cdd:COG5185 445 ELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIEsrvstlkatleKLRAKLERQLEGVRSKLDQ--- 521
|
....*.
gi 1622930585 2140 QANSIK 2145
Cdd:COG5185 522 VAESLK 527
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1669-2145 |
1.32e-11 |
|
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: 71.24 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1669 ERTNTRAKSLGEFIKELARDAEAVNEKAIKL--------NETLGTRDEAFERNleGLQKEIDQMIKELRRKNLETQKEIa 1740
Cdd:TIGR01612 547 KESYELAKNWKKLIHEIKKELEEENEDSIHLekeikdlfDKYLEIDDEIIYIN--KLKLELKEKIKNISDKNEYIKKAI- 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1741 edelvaaegllkKVKKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREA------NRLFAVNQKN---- 1810
Cdd:TIGR01612 624 ------------DLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDdidalyNELSSIVKENaidn 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1811 ---MTALEKKK---------------EAVESGKRQIENTLKEGNDILDEANR-----LADEINSIidyVEDIQTKlppmS 1867
Cdd:TIGR01612 692 tedKAKLDDLKskidkeydkiqnmetATVELHLSNIENKKNELLDIIVEIKKhihgeINKDLNKI---LEDFKNK----E 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1868 EELNNKIDDLSQEiKDR--KLAEKVSQAESHaaqLNDSSAVlDGILDE------------AKNISFNATAAFKAYSNIKD 1933
Cdd:TIGR01612 765 KELSNKINDYAKE-KDElnKYKSKISEIKNH---YNDQINI-DNIKDEdakqnydkskeyIKTISIKEDEIFKIINEMKF 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1934 YIDEA----------EKVAKEAKDLAHEA-TKLATGPRGLLKEDAKGSLQKSFrilNEAKKLAND----VKENEDHLNGL 1998
Cdd:TIGR01612 840 MKDDFlnkvdkfinfENNCKEKIDSEHEQfAELTNKIKAEISDDKLNDYEKKF---NDSKSLINEinksIEEEYQNINTL 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1999 KT-------------RIENADARNGDLLRALN---DTLGKLSAIPNDTAAKLQ-AVKDKARQANDTAKDVL-----AQIK 2056
Cdd:TIGR01612 917 KKvdeyikicentkeSIEKFHNKQNILKEILNkniDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDASlndyeAKNN 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2057 ELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKI---IADADATVKNLEQEADRLIDKLkpIKELEDNLKKNI----SE 2129
Cdd:TIGR01612 997 ELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIeqkIEDANKNIPNIEIAIHTSIYNI--IDEIEKEIGKNIellnKE 1074
|
570
....*....|....*.
gi 1622930585 2130 IKELINQARKQANSIK 2145
Cdd:TIGR01612 1075 ILEEAEINITNFNEIK 1090
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1680-2184 |
2.25e-11 |
|
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: 70.47 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1680 EFIKELARDAEAVNE---------KAIKLNETLGTRDEAFERNLEGlqKEIDQMIKELRR-KNLETQKEIAEDELVA-AE 1748
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDeldksekliKKIKDDINLEECKSKIESTLDD--KDIDECIKKIKElKNHILSEESNIDTYFKnAD 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKLFgesrgKNEEMEKDLREKLadYKNKVDDAWDLLREATNKIRE----ANRLFAVNQKNMTALEKKKEAVESG 1824
Cdd:TIGR01612 1447 ENNENVLLLF-----KNIEMADNKSQHI--LKIKKDNATNDHDFNINELKEhidkSKGCKDEADKNAKAIEKNKELFEQY 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1825 KRQIENTLKEGND--ILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIddlsQEIKDRKLaekvsQAESHAAQLND 1902
Cdd:TIGR01612 1520 KKDVTELLNKYSAlaIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKI----KEIKKEKF-----RIEDDAAKNDK 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1903 SSAVLDGILDEAKNISfnatAAFKAYSNIK----DYIDEAEKVAKEAKDLA--HEATKLATGPrgllkeDAKGSLQKSFR 1976
Cdd:TIGR01612 1591 SNKAAIDIQLSLENFE----NKFLKISDIKkkinDCLKETESIEKKISSFSidSQDTELKENG------DNLNSLQEFLE 1660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1977 ILNEAKKLANDVKENEDHLNGLKTRIE---NADARNGD--LLRALNDTlgklsAIPNDTaaKLQAVKDKARQandTAKDV 2051
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELDELDSEIEKIEidvDQHKKNYEigIIEKIKEI-----AIANKE--EIESIKELIEP---TIENL 1730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2052 LAQIKElhQNLDGLKKN-------------YDKLADSVAKTNAVVKDPSKNKIIADADATVK-NLEQEADRLIDKLKPIK 2117
Cdd:TIGR01612 1731 ISSFNT--NDLEGIDPNekleeynteigdiYEEFIELYNIIAGCLETVSKEPITYDEIKNTRiNAQNEFLKIIEIEKKSK 1808
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2118 ELEDNLKknISEIKELINQARKQANSIKVSVSsggdciRTYKpEIKKGsYNNI---VVNVKTAVADNLLF 2184
Cdd:TIGR01612 1809 SYLDDIE--AKEFDRIINHFKKKLDHVNDKFT------KEYS-KINEG-FDDIsksIENVKNSTDENLLF 1868
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1702-2118 |
3.45e-11 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 68.83 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1702 TLGTRDEAFERNLEGLQKEiDQMIKELRRKNLE-TQKEIAEDELVAA-----EGLLKKVKKLFGESRGKNEEMEKDLREK 1775
Cdd:COG5185 205 NSIKESETGNLGSESTLLE-KAKEIINIEEALKgFQDPESELEDLAQtsdklEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1776 LADYKNKVDDAWDLLREAT------NKIREANRLFAVNQKNmTALEKKKEAVESG-KRQIENTLKEGNDILDEANRLADE 1848
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTksidikKATESLEEQLAAAEAE-QELEESKRETETGiQNLTAEIEQGQESLTENLEAIKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1849 INSIIDYVEdiqtklppmSEELNNKIDDLSQEIkdRKLAEKVSQAesHAAQLNDSSAVLDGILDEAKNISFNAtaafkay 1928
Cdd:COG5185 363 IENIVGEVE---------LSKSSEELDSFKDTI--ESTKESLDEI--PQNQRGYAQEILATLEDTLKAADRQI------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1929 SNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQksfrilNEAKKLANDVKENEDHLNGLKTRIENAdar 2008
Cdd:COG5185 423 EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLE------EAYDEINRSVRSKKEDLNEELTQIESR--- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2009 ngdlLRALNDTLGKLSAipnDTAAKLQAVKDKARQANDTAKDVLAQIKELHqnldgLKKNYDKLADSVAKTNavvkDPSK 2088
Cdd:COG5185 494 ----VSTLKATLEKLRA---KLERQLEGVRSKLDQVAESLKDFMRARGYAH-----ILALENLIPASELIQA----SNAK 557
|
410 420 430
....*....|....*....|....*....|
gi 1622930585 2089 NKIIADADATVKNLEQEADRLIDKLKPIKE 2118
Cdd:COG5185 558 TDGQAANLRTAVIDELTQYLSTIESQQARE 587
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
966-1012 |
3.64e-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: 3.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 966 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSF--QEGGCT 1012
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1814-2164 |
4.06e-11 |
|
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: 68.89 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1814 LEKKkeaVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEEL---NNKIDDLSQ-------EIKD 1883
Cdd:TIGR04523 38 LEKK---LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLkknKDKINKLNSdlskinsEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1884 RKlaEKVSQAESHAA----QLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKD-----------YIDEAEKVAKEAKDL 1948
Cdd:TIGR04523 115 DK--EQKNKLEVELNklekQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKqkeelenelnlLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1949 AHEATKLATgprGLLKEDAKGSLQKSFRI-LNEAKK----LANDVKENEDHLNGLKTRIENADARngdllraLNDTLGKL 2023
Cdd:TIGR04523 193 KNKLLKLEL---LLSNLKKKIQKNKSLESqISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQ-------LNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2024 SAIPNDTAAKLQAVKdkarQANDTAKDVLAQIKELHQNLDGLKKnyDKLADsvakTNAVVKDPSKN--KIIADADATVKN 2101
Cdd:TIGR04523 263 NKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEISDLNN--QKEQD----WNKELKSELKNqeKKLEEIQNQISQ 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2102 LEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcirtYKPEIKK 2164
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-------YKQEIKN 388
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-916 |
4.64e-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: 60.06 E-value: 4.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 864 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDARNCQ 916
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1630-2181 |
5.00e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 69.09 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNELLTRaTKVTADGEQTGQDAERTNtrakSLGEFIKE---LARDAEAVNEKAIKLNETLGTR 1706
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDLQEK-VKYILNKFYKGDLQELLD----ELSHFLDDhkyLYHEAKSKEDLQTLLNTSKNEY 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1707 DEAFERNLEglqkEIDQMIKELRR--KNLETQKEiaedelvaaegllKKVKKLFgesrgknEEMEKDLREKLADYKNKVD 1784
Cdd:PTZ00440 676 EKLEFMKSD----NIDNIIKNLKKelQNLLSLKE-------------NIIKKQL-------NNIEQDISNSLNQYTIKYN 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1785 DawdlLREATNKIREANRLFAVNQKNMtalEKKKEAVESGKRQIENTLKEGNDILDE-----------ANRLADEINSII 1853
Cdd:PTZ00440 732 D----LKSSIEEYKEEEEKLEVYKHQI---INRKNEFILHLYENDKDLPDGKNTYEEflqykdtilnkENKISNDINILK 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1854 DYVEDIQT----------KLPPMSEELNNKIDDLSQEIKDRKLAEKVSQAEShaaQLNDSSAVLDGILDEAKNISFNaTA 1923
Cdd:PTZ00440 805 ENKKNNQDllnsyniliqKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEK---EFNENNQIVDNIIKDIENMNKN-IN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1924 AFKAYSNIKDYIDEAEKVakeakdLAHEATKlatgprgllKEDAKGSLQKSFRILNEAKKLANDVKEN-EDHLNGLKTRI 2002
Cdd:PTZ00440 881 IIKTLNIAINRSNSNKQL------VEHLLNN---------KIDLKNKLEQHMKIINTDNIIQKNEKLNlLNNLNKEKEKI 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2003 ENadarngdllrALNDT-LGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKE----LHQNLDGLKKNYDKLAdsvA 2077
Cdd:PTZ00440 946 EK----------QLSDTkINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILN---K 1012
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2078 KTNAVVKDPsKNKIIADADATVKNLEQEADRLIDKLkpIKELEDnLKKNISEIKELINQARKQANSIKVSVSSGGDCIRT 2157
Cdd:PTZ00440 1013 KIDDLIKKQ-HDDIIELIDKLIKEKGKEIEEKVDQY--ISLLEK-MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEA 1088
|
570 580
....*....|....*....|....
gi 1622930585 2158 YKPEIKKGsyNNIVVNVKTAVADN 2181
Cdd:PTZ00440 1089 LLKKIDEN--KNKLIEIKNKSHEH 1110
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-805 |
5.17e-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: 60.06 E-value: 5.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 756 PCQCFGHA---ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPTKGtsEDCQ 805
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1612-2135 |
1.38e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.51 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKhllsPQRAPERLIQLAEGNlNTLVTEMNELLTRATkvtadgEQTGQDAERTNtRAKSLGEfikeLARDAEA 1691
Cdd:pfam01576 124 LEKVTTEAK----IKKLEEDILLLEDQN-SKLSKERKLLEERIS------EFTSNLAEEEE-KAKSLSK----LKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VN---EKAIKLNETLGTRDEAFERNLEG-----------LQKEIDQMIKELRRKNLETQKEIA--EDELVAAEGLLKKVK 1755
Cdd:pfam01576 188 MIsdlEERLKKEEKGRQELEKAKRKLEGestdlqeqiaeLQAQIAELRAQLAKKEEELQAALArlEEETAQKNNALKKIR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1756 KLFGE-------------SRGKNEEMEKDLREKLADYKNKVDDAWDL------LR--------------EATNKIREAnR 1802
Cdd:pfam01576 268 ELEAQiselqedleseraARNKAEKQRRDLGEELEALKTELEDTLDTtaaqqeLRskreqevtelkkalEEETRSHEA-Q 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1803 LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQT---KLPPMSEELNNKIDDlsQ 1879
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSE--S 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1880 EIKDRKLAEKVSQAEShaaQLNDSSAVLDGIldEAKNISFNataafkaysniKDyIDEAEKVAKEAKDLAHEAT--KLAT 1957
Cdd:pfam01576 425 ERQRAELAEKLSKLQS---ELESVSSLLNEA--EGKNIKLS-----------KD-VSSLESQLQDTQELLQEETrqKLNL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1958 GPRGLLKEDAKGSLQKSFRILNEAKK-LANDVKENEDHLNGLKTRIENaDARNGDLL-----RALNDTLGKLSAIPNDTA 2031
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRnVERQLSTLQAQLSDMKKKLEE-DAGTLEALeegkkRLQRELEALTQQLEEKAA 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2032 A--KLQAVKDKARQANDtakDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVK-----NLEQ 2104
Cdd:pfam01576 567 AydKLEKTKNRLQQELD---DLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKetralSLAR 643
|
570 580 590
....*....|....*....|....*....|.
gi 1622930585 2105 EADRLIDKlkpIKELEDNLKKNISEIKELIN 2135
Cdd:pfam01576 644 ALEEALEA---KEELERTNKQLRAEMEDLVS 671
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1420-1466 |
1.38e-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: 58.90 E-value: 1.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1420 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1466
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1612-1902 |
1.62e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLiqlaegnLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRDE---AFERNLEGL------------QKEIDQMIKELRR------------KNLETQKEIAEDE- 1743
Cdd:TIGR02169 756 VKSELKELEARIEELEEdlhKLEEALNDLearlshsripeiQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1744 --LVAAEGLLKKVKKLFG----ESRGKNEEME----------KDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVN 1807
Cdd:TIGR02169 836 qeLQEQRIDLKEQIKSIEkeieNLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1808 QKNMTALEKKKEAVESGKRQIENTLKEGNDIldeanrlADEINSIIDYVEDIQTKLPPMS--EELNNK-IDDLSQEIKDR 1884
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEI-------PEEELSLEDVQAELQRVEEEIRalEPVNMLaIQEYEEVLKRL 988
|
330
....*....|....*....
gi 1622930585 1885 K-LAEKVSQAESHAAQLND 1902
Cdd:TIGR02169 989 DeLKEKRAKLEEERKAILE 1007
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1060-1108 |
1.76e-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: 58.52 E-value: 1.76e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYPRCNLCDC 1108
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1527-1574 |
2.57e-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: 2.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKHWHAREGWECVFC 1574
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1527-1570 |
2.97e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKHWHAREGWE 1570
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
967-1014 |
3.05e-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: 57.75 E-value: 3.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFSFQEGGCTAC 1014
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1106-1163 |
3.75e-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: 57.36 E-value: 3.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGLDAKNPLGC 1163
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1700-2185 |
3.84e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 66.39 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1700 NETLGTRDEAFERNLEGLQKEIDQMIKE-LRRKN----LETQKEIAEDELVAAEGLLKKVKklfgESRGKNEEMEKDLRE 1774
Cdd:PTZ00440 134 YDDLKKYSDKINEDVEPLNEEIIKNIEQcLGNKNdldnLIIVLENPEKYNVRKTLYDEKFN----EYKNKKEAFYNCLKN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1775 KLADYKNKVDDAWDLLREATNKIREANR--------------LFAVNQKNMTA----LEKKKEAVESG-------KRQIE 1829
Cdd:PTZ00440 210 KKEDYDKKIKKINNEIRKLLKNIKCTGNmcktdtyvdmvelyLLRVNEVPSNNydnyLNRAKELLESGsdlinkiKKELG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1830 NTL---------KEGNDILDEANRLADEINSIIDYVEDIQT--KLPPMSE-ELNNKIDDLSQEIKDRKLAEKvsqaesHA 1897
Cdd:PTZ00440 290 DNKtiysinfiqEEIGDIIKRYNFHLKKIEKGKEYIKRIQNnnIPPQVKKdELKKKYFESAKHYASFKFSLE------ML 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1898 AQLNDSSAVLDGILDEAKNISFN-ATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFR 1976
Cdd:PTZ00440 364 SMLDSLLIKKEKILNNLFNKLFGdLKEKIETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEIIE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1977 ILNEAKKLANDVKENEDHLNGLKTRIENA--------DARNG--DLLRALNDTLGKLSAIPNdtaaKLQAVKDKARQAND 2046
Cdd:PTZ00440 444 IKKKYDEKINELKKSINQLKTLISIMKSFydliisekDSMDSkeKKESSDSNYQEKVDELLQ----IINSIKEKNNIVNN 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2047 TAK---DVLAQIKELHQNLDGLKKNYDKLADSVakTNAVVKDPSKNKIIADADATVKNLEQEadrlIDKLKPIKELEDNL 2123
Cdd:PTZ00440 520 NFKnieDYYITIEGLKNEIEGLIELIKYYLQSI--ETLIKDEKLKRSMKNDIKNKIKYIEEN----VDHIKDIISLNDEI 593
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2124 KKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVNVKTAVADNLLFY 2185
Cdd:PTZ00440 594 DNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLY 655
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1630-1913 |
4.64e-10 |
|
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: 65.43 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRdea 1709
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK--- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1710 fERNLEGLQKEIDQMIKELRRKNLET-----QKEIAEDELvAAEGLLKKVKKLfgESRGKNEEMEK-DLREKLADYKNKV 1783
Cdd:TIGR04523 537 -ESKISDLEDELNKDDFELKKENLEKeidekNKEIEELKQ-TQKSLKKKQEEK--QELIDQKEKEKkDLIKEIEEKEKKI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1784 ddaWDLLREATnKIREANRLFAVNQKNmtaLEKKKEAVESGKRQIENTLKE----GNDILDEANRLADEINSIIDYVEDI 1859
Cdd:TIGR04523 613 ---SSLEKELE-KAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKEirnkWPEIIKKIKESKTKIDDIIELMKDW 685
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 1860 QTKLppmSEELNNKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDE 1913
Cdd:TIGR04523 686 LKEL---SLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1617-2138 |
5.99e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 65.58 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1617 QELKHLlspQRAPERLIQLAEGNL-------NTLVTEMNELLTRATKVTADGEQTGQDAERTNtrakslgefiKELARDA 1689
Cdd:pfam01576 327 QEVTEL---KKALEEETRSHEAQLqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESEN----------AELQAEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1690 EAVNekaiklnetlGTRDEAfernlEGLQKEIDQMIKELRRKNLETQKEIAE--DELVAAEGLLKKVKKLFGESRGKNEE 1767
Cdd:pfam01576 394 RTLQ----------QAKQDS-----EHKRKKLEGQLQELQARLSESERQRAElaEKLSKLQSELESVSSLLNEAEGKNIK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1768 MEKDlrekLADYKNKVDDAWDLLREAT-NKIREANRLFAVnQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLA 1846
Cdd:pfam01576 459 LSKD----VSSLESQLQDTQELLQEETrQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1847 DEINSIIDYVEDIQTKLPPMSEELNNKIDD--------------LSQEIKDrkLAEKVSQAESHAAQLNDSSAVLDGILD 1912
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrLQQELDD--LLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1913 EAKNISfnataafKAYSNIKDYIdEAEKVAKEAKDL--------AHEATKLATGPRGLLK---ED---AKGSLQKSFRIL 1978
Cdd:pfam01576 612 EEKAIS-------ARYAEERDRA-EAEAREKETRALslaraleeALEAKEELERTNKQLRaemEDlvsSKDDVGKNVHEL 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1979 NEAKKLAndvkenEDHLNGLKTRIENADarngDLLRALNDtlGKLSAIPNDTAAKLQAVKD-KAR--QANDTAKDVLAQI 2055
Cdd:pfam01576 684 ERSKRAL------EQQVEEMKTQLEELE----DELQATED--AKLRLEVNMQALKAQFERDlQARdeQGEEKRRQLVKQV 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2056 KELHQNLDGLKKNYDKLADSVAKTNAVVKDpsknkIIADADATVKNLEqEADRLIDKLKP-IKELEDNLKKNISEIKELI 2134
Cdd:pfam01576 752 RELEAELEDERKQRAQAVAAKKKLELDLKE-----LEAQIDAANKGRE-EAVKQLKKLQAqMKDLQRELEEARASRDEIL 825
|
....
gi 1622930585 2135 NQAR 2138
Cdd:pfam01576 826 AQSK 829
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1419-1467 |
6.02e-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: 56.98 E-value: 6.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1419 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1467
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1712-1902 |
6.16e-10 |
|
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: 62.25 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1712 RNLEGLQkEIDQMIKELRRKNLETQKEIA--EDELVAAEGLLKKVKKLFgesrgkneemeKDLREKLADYKNKVDDAWDL 1789
Cdd:COG1579 7 RALLDLQ-ELDSELDRLEHRLKELPAELAelEDELAALEARLEAAKTEL-----------EDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1790 LREATNKIREANrlfavNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIdyvEDIQTKLppmsEE 1869
Cdd:COG1579 75 IKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAEL----EE 142
|
170 180 190
....*....|....*....|....*....|...
gi 1622930585 1870 LNNKIDDLSQEIkDRKLAEKVSQAESHAAQLND 1902
Cdd:COG1579 143 KKAELDEELAEL-EAELEELEAEREELAAKIPP 174
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1014-1057 |
6.63e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.63e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 1014 CECS---HLGNNCDPKTGQCICPPNTIGEKCSKCAPNTWGHSiTTGC 1057
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1059-1101 |
7.32e-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: 7.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622930585 1059 ACNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1013-1058 |
7.39e-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: 7.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1013 ACECSHLG---NNCDPKTGQCICPPNTIGEKCSKCAPNTWGH-SITTGCK 1058
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1861-2164 |
7.56e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1861 TKLPPMSEELNNKIDDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNI-----SFNAtaafkaysNIKD 1933
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1934 YIDEAEKVAKEAKDLAHEATKLatgprgllkedakgslqksFRILNEAKKLANDVKENEDHLNGLKTRIENADARngdlL 2013
Cdd:COG1340 76 LKEERDELNEKLNELREELDEL-------------------RKELAELNKAGGSIDKLRKEIERLEWRQQTEVLS----P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2014 RALNDTLGKLSAIpndtAAKLQAVKdKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTnavvkdpsKNKIIa 2093
Cdd:COG1340 133 EEEKELVEKIKEL----EKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--------HEEMI- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2094 dadatvkNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2164
Cdd:COG1340 199 -------ELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK----LRKKQRALKR 258
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1614-1806 |
9.91e-10 |
|
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: 61.48 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1614 NMTQELKHLLSPQRAPERLIQLAEgNLNTLVTEMNELLTRATKVTADgeqtgqdAERTNTRAKSLGEFIKELARDAEAVN 1693
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEH-RLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1694 EKAIKLNETLGT----RD-EAFERNLEGLQKEIDQM---IKEL--RRKNLETQKEIAEDELVAAEGLLKKVKKLFGESRG 1763
Cdd:COG1579 73 ARIKKYEEQLGNvrnnKEyEALQKEIESLKRRISDLedeILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622930585 1764 KNEEMEKDLREKLADYKNKVDDawDLLReATNKIREANRLFAV 1806
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP--ELLA-LYERIRKRKNGLAV 192
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1680-2176 |
1.26e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 64.47 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1680 EFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEG-------LQKEIDQMIKE---LRRKNLETQKEIAEDELVAAEG 1749
Cdd:PTZ00440 952 TKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKekdewehFKSEIDKLNVNyniLNKKIDDLIKKQHDDIIELIDK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1750 LLKkvkklfgesrgkneEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAvesgkrqIE 1829
Cdd:PTZ00440 1032 LIK--------------EKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEA-------LL 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1830 NTLKEGNDILDEANRLADE---------INSIIDY------VEDIQTKLPPMSEELNNK--------------------- 1873
Cdd:PTZ00440 1091 KKIDENKNKLIEIKNKSHEhvvnadkekNKQTEHYnkkkksLEKIYKQMEKTLKELENMnleditlnevneieieyeril 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1874 IDDLSQEIKDRKLAEKV--SQAESHAAQLNDSSA-VLDGILDEAKNISFNA--TAAFKAYSNIKDYIDEAeKVAKEAKDL 1948
Cdd:PTZ00440 1171 IDHIVEQINNEAKKSKTimEEIESYKKDIDQVKKnMSKERNDHLTTFEYNAyyDKATASYENIEELTTEA-KGLKGEANR 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1949 AHEATKLATgprglLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTR-----IENADARNGDLLRALNDTLGKL 2023
Cdd:PTZ00440 1250 STNVDELKE-----IKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEkilkeILNSTKKAEEFSNDAKKELEKT 1324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2024 SAIpndtaakLQAVKDKARQANDTAKDVLAQI--KELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKiiADADATVKN 2101
Cdd:PTZ00440 1325 DNL-------IKQVEAKIEQAKEHKNKIYGSLedKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNK--EKCDLHVRN 1395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2102 LEQEADrLIDKLKPIKELEDNLKK--NISEIKELINQARK---QANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVNVKT 2176
Cdd:PTZ00440 1396 ASRGKD-KIDFLNKHEAIEPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSILGKKT 1474
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1106-1163 |
1.28e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGldaKNPLGC 1163
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1639-2162 |
1.44e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 64.30 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1639 NLNTLVTEMNELLTRATKVTADGEQTgqDAERTNTRAKSL-GEFIKELARDAEAVN-----EKAIKLNETLGTRDEAFER 1712
Cdd:TIGR01612 861 KIDSEHEQFAELTNKIKAEISDDKLN--DYEKKFNDSKSLiNEINKSIEEEYQNINtlkkvDEYIKICENTKESIEKFHN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1713 NLEGLQKEIDQMIKELRRKNL--ETQKEIAEDELVAAEGLLKKVKK--LFGESRGKNEEMEK---DLREKLADYK-NKVD 1784
Cdd:TIGR01612 939 KQNILKEILNKNIDTIKESNLieKSYKDKFDNTLIDKINELDKAFKdaSLNDYEAKNNELIKyfnDLKANLGKNKeNMLY 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1785 DAWDLLREATN----KIREANR------------LFAVNQ-------KNMTALE----KKKEAVESGKRQIENTLKEGN- 1836
Cdd:TIGR01612 1019 HQFDEKEKATNdieqKIEDANKnipnieiaihtsIYNIIDeiekeigKNIELLNkeilEEAEINITNFNEIKEKLKHYNf 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1837 -DILDEAN-RLADEINSIIDyveDIQTklppMSEELNNKIDDLsQEIKdRKLAEKVSQAEshaAQLNDSSAVLDGIL--D 1912
Cdd:TIGR01612 1099 dDFGKEENiKYADEINKIKD---DIKN----LDQKIDHHIKAL-EEIK-KKSENYIDEIK---AQINDLEDVADKAIsnD 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1913 EAKNISfnataafKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLlkEDAKG-------SLQKSF--RILNEAKK 1983
Cdd:TIGR01612 1167 DPEEIE-------KKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSL--EEVKGinlsygkNLGKLFleKIDEEKKK 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1984 LANDVKENEDHLNGLktrienadarngDLLRALNDTLGKLSAIPNDTAAKLQAVKdkarQANDTAKDvlaqikelHQNLD 2063
Cdd:TIGR01612 1238 SEHMIKAMEAYIEDL------------DEIKEKSPEIENEMGIEMDIKAEMETFN----ISHDDDKD--------HHIIS 1293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2064 glKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADR----------LIDKLKPIKELeDNLKKNISEIKEL 2133
Cdd:TIGR01612 1294 --KKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKhnsdinlylnEIANIYNILKL-NKIKKIIDEVKEY 1370
|
570 580
....*....|....*....|....*....
gi 1622930585 2134 INQARKQANSIKVSVSSGGDCIRTYKPEI 2162
Cdd:TIGR01612 1371 TKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1106-1163 |
1.60e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCQPGKFGlDAKNPLGC 1163
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1717-2148 |
1.66e-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: 63.44 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1717 LQKEIDQMIKELRRKNLETQKEIAEDELVAAEGLLKK------VKKLFGESRG-KNEEMEKDL----------REKLADY 1779
Cdd:COG5185 2 VQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTlvfitiLFFPLGISRDsLRVTLRSVInvldglnyqnDVKKSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1780 KNKVDDAWDLLREATNKIREANRLFAVNQkNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDyVE-- 1857
Cdd:COG5185 82 SVKARKFLKEKKLDTKILQEYVNSLIKLP-NYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGE-VEtg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1858 ---DIQTKLPPMSEELNNKIDDLSQEIKDRK--LAEKVSQAESHAAQLNDSSA---VLDGILDEAKNISFNATAAFKAYS 1929
Cdd:COG5185 160 iikDIFGKLTQELNQNLKKLEIFGLTLGLLKgiSELKKAEPSGTVNSIKESETgnlGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1930 NIKDYIDEAEKVAKEAKDLAHEATKLatgprgllKEDAKGSLQKSFRILNEAKKlaNDVKENEDHlnglKTRIENADARN 2009
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDL--------RLEKLGENAESSKRLNENAN--NLIKQFENT----KEKIAEYTKSI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2010 gDLLRALNDTlgklsaipNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLadsVAKTNAVVKDPSKN 2089
Cdd:COG5185 306 -DIKKATESL--------EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI---KEEIENIVGEVELS 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 2090 KIIADADATVKNLEQEADRLIDKLKPIKE--------LEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:COG5185 374 KSSEELDSFKDTIESTKESLDEIPQNQRGyaqeilatLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1014-1057 |
1.81e-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: 55.44 E-value: 1.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930585 1014 CECSHLG---NNCDPKTGQCICPPNTIGEKCSKCAPNTWGHSITTGC 1057
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1712-2080 |
1.93e-09 |
|
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: 63.93 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1712 RNLEGLQKEIDQMIKELRR-KNLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREKLAdyknkvddawDLL 1790
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRiENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS----------SLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1791 REATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQI-ENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEE 1869
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1870 LNNKIDDLSQEIKDRKLAEKVSQAESHAaqLNDSSAVLDGILDEAKNisfnataafkaysNIKDYIDEAEKVAKEAKDLa 1949
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIEN--LNGKKEELEEELEELEA-------------ALRDLESRLGDLKKERDEL- 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1950 heatklatgprgllkeDAKGSLQKsfrilNEAKKLANDVKENEDHLNGLKTRIENADARngdlLRALNDTLGKLSAIPND 2029
Cdd:TIGR02169 895 ----------------EAQLRELE-----RKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEEIPEE 949
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 2030 TAA--KLQAVKDKARQA-------NDTA----KDVLAQIKELHQNLDGLKKNYDKLADSVAKTN 2080
Cdd:TIGR02169 950 ELSleDVQAELQRVEEEiralepvNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1645-2175 |
2.92e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 63.31 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1645 TEMNEL---LTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELarDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKE- 1720
Cdd:PTZ00440 1990 EELKDLrnsFNQEKAETLNNLKLNKIKEDFNSYKNLLDELEKSV--KTLKASENIKKIVENKKTSIDAINTNIEDIEKEi 2067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1721 --IDQMIKEL--RRKNLETQK----------EIAEDELVAAEglLKKVKKLFGESRGKNEEMEKDLREKLadykNKVDDA 1786
Cdd:PTZ00440 2068 esINPSLDELlkKGHKIEISRytsiidnvqtKISNDSKNIND--IEKKAQIYLAYIKNNYNSIKKDISTL----NEYFDE 2141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1787 WDLLREATNKIREANRLFAvnqkNMTalekkkEAVESGKRQIENTLKEGNDILDeanrlADEINSIidyvEDIQTKLPPM 1866
Cdd:PTZ00440 2142 KQVSNYILTNIDKANKLSS----ELS------EAVTNSEEIIENIKKEIIEINE-----NTEMNTL----ENTADKLKEL 2202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1867 SEELNNK---IDDLSQEIKDRKLAEKVSQAESHaaqlNDSSAVLDGILD-EAKNISFNATAafkaYSNIKDYIDEAEKva 1942
Cdd:PTZ00440 2203 YENLKKKkniINNIYKKINFIKLQEIENSSEKY----NDISKLFNNVVEtQKKKLLDNKNK----INNIKDKINDKEK-- 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1943 keakdlaheatKLATGPRGLLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADarngDLLRALNDTLGK 2022
Cdd:PTZ00440 2273 -----------ELINVDSSFTLESIKTFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENIT----HLLNRINTLIND 2337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2023 LSAIPNDtaaklQAVKDKARQANdtaKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVKNL 2102
Cdd:PTZ00440 2338 LDNYQDE-----NYGKDKNIELN---NENNSYIIKTKEKINNLKEEFSKLLKNIKRNNTLCNNNNIKDFISNIGKSVETI 2409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2103 EQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQANsikVSVSSGgdcIRTYKPEIKKGSYNNIVVNVK 2175
Cdd:PTZ00440 2410 KQR----FSSNLPEKEKLHQIEENLNEIKNIMNETKRISN---VDAFTN---KILQDIDNEKNKENNNMNAEK 2472
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1527-1562 |
3.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 3.16e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1622930585 1527 CECDPYGSLPVPCDPVTGICTCRPGATGRKCDGCKH 1562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
414-471 |
3.32e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 3.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 414 CHCNPVGSLNEVCVkdekharrgLAPGSCHCKTGFGGVSCDRCARGYTGYPDCKACNC 471
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1612-2140 |
3.84e-09 |
|
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: 62.76 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQElKHLLSpQRAPERLIQLAEGNLNTLVTEMN------ELLTRATKVTADGEQTGQDAE------------RTNT 1673
Cdd:TIGR00606 328 LEKLNKE-RRLLN-QEKTELLVEQGRLQLQADRHQEHirardsLIQSLATRLELDGFERGPFSErqiknfhtlvieRQED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1674 RAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQM---IKELR----------RKNLETQKEIA 1740
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELkfvIKELQqlegssdrilELDQELRKAER 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1741 E----DELVAAEGLLKKVKKLFGES-------RGKNEEMEKDLREK------LADYKNKVdDAWDLLREatNKIREANRL 1803
Cdd:TIGR00606 486 ElskaEKNSLTETLKKEVKSLQNEKadldrklRKLDQEMEQLNHHTttrtqmEMLTKDKM-DKDEQIRK--IKSRHSDEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1804 --FAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLppmSEELNNKIDDLSQEI 1881
Cdd:TIGR00606 563 tsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY---EDKLFDVCGSQDEES 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1882 KDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAA----FKAYSNIKDYI-----------DEAEKVAKEAK 1946
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvFQTEAELQEFIsdlqsklrlapDKLKSTESELK 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1947 DLAHEATK---LATGPRGLL--KEDAKGSLQKSFRILN-EAKKLANDVKENEDHLNGLKTRIENADARNGD--LLRALND 2018
Cdd:TIGR00606 720 KKEKRRDEmlgLAPGRQSIIdlKEKEIPELRNKLQKVNrDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtIMERFQM 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2019 TLGKLSAIPNDTAAKLQAVkdkarqandtakDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsKNKIIADADAT 2098
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGS------------DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD--QQEQIQHLKSK 865
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1622930585 2099 VKNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL---INQARKQ 2140
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLireIKDAKEQ 910
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1648-2148 |
3.87e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1648 NELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAiklnETLGTRDEAFERNLEGLQKEIDQMIK- 1726
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKKEEAKKKADAAKKKAEEKKKa 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1727 -ELRRKNLETQKEiaEDELVAAEGLLKKVKKL--FGESRGKNEEMEKDLRE--KLADYKNKVDDAwdllREATNKIREAN 1801
Cdd:PTZ00121 1394 dEAKKKAEEDKKK--ADELKKAAAAKKKADEAkkKAEEKKKADEAKKKAEEakKADEAKKKAEEA----KKAEEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1802 RLFAVNQKNMTALEKKKeaVESGKRQIENTLKEGNDI--LDEANRLADEINSiidyVEDIQTKLPPMSEELNNKIDDL-- 1877
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAkkAAEAKKKADEAKK----AEEAKKADEAKKAEEAKKADEAkk 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1878 ------SQEIK---DRKLAEKVSQAESHAAQLNDSSAVLDGIlDEAKNIS-FNATAAFKAYSNIKDYIDEAEKVAKEAKD 1947
Cdd:PTZ00121 1542 aeekkkADELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEeARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1948 LAHEATKlatgprgllKEDAKGSLQKSFRILNEAKKLANDVKENEDHlNGLK----TRIENADARNGDLLRalndtlgkl 2023
Cdd:PTZ00121 1621 KAEELKK---------AEEEKKKVEQLKKKEAEEKKKAEELKKAEEE-NKIKaaeeAKKAEEDKKKAEEAK--------- 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2024 saipndtaaklqavkdKARQANDTAKDVLAQIKELHQNLDGLKKnydKLADSVAKTNAVVKDPSKNKIIADadaTVKNLE 2103
Cdd:PTZ00121 1682 ----------------KAEEDEKKAAEALKKEAEEAKKAEELKK---KEAEEKKKAEELKKAEEENKIKAE---EAKKEA 1739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622930585 2104 QEADRLIDKLKpikeLEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:PTZ00121 1740 EEDKKKAEEAK----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-797 |
5.52e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 5.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 757 CQCFGHA---ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPT 797
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1708-2163 |
6.10e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1708 EAFERNLEGLQKEIDQMIKELRRKN--LETQKEIAEDELVAAEGLLKKV---KKLFGESRGKNEEMEKDLREKLADYKNK 1782
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNelHEKQKFYLRQSVIDLQTKLQEMqmeRDAMADIRRRESQSQEDLRNQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1783 VDDA----WDLLREATNKIREANRLF----AVNQKNMTALEKKKEAveSGKRQIE----NTL---KEGNDILDEANRLAD 1847
Cdd:pfam15921 154 LEAAkclkEDMLEDSNTQIEQLRKMMlsheGVLQEIRSILVDFEEA--SGKKIYEhdsmSTMhfrSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKDR-------------KLAEKVSQAESHAaqlNDSSAVLDGILDEA 1914
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieqliseheveitGLTEKASSARSQA---NSIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1915 KNisfNATAAFKAYSNIKDYIDEAEKVAKEAK----DLAHEATK---LATGPRGLLKEDAKGSLQKSFRILNEAKKLAND 1987
Cdd:pfam15921 309 RN---QNSMYMRQLSDLESTVSQLRSELREAKrmyeDKIEELEKqlvLANSELTEARTERDQFSQESGNLDDQLQKLLAD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1988 VKENEDHLNGLK---TRIENADARNG----DLLRALND---TLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKE 2057
Cdd:pfam15921 386 LHKREKELSLEKeqnKRLWDRDTGNSitidHLRRELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2058 LHQNLDGLKKNYDKLADSVAKTNAVVKdpSKNKIIADADATVknleQEADRLIDKLKP-IKELEDNLKKNISEIKELINQ 2136
Cdd:pfam15921 466 LTAQLESTKEMLRKVVEELTAKKMTLE--SSERTVSDLTASL----QEKERAIEATNAeITKLRSRVDLKLQELQHLKNE 539
|
490 500 510
....*....|....*....|....*....|...
gi 1622930585 2137 ------ARKQANSIKVSVSSGGDCIRTYKPEIK 2163
Cdd:pfam15921 540 gdhlrnVQTECEALKLQMAEKDKVIEILRQQIE 572
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
865-908 |
8.12e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 8.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622930585 865 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 908
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1698-2123 |
8.50e-09 |
|
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: 61.24 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1698 KLNETLGtRDEAFE-------RNLEGLQKEIDQMIKELRRknLETQKEiaeDELVAAEGLLKKVkklfGESRGKNEEMEK 1770
Cdd:pfam05622 39 KLQERLD-QLESGDdsgtpggKKYLLLQKQLEQLQEENFR--LETARD---DYRIKCEELEKEV----LELQHRNEELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1771 dlrekLADYKNKVDDAWDLLREATNKIreanrlfavnqknmtaleKKKEA-VESGKRQIE--NTLKEGNDILDEANrlAD 1847
Cdd:pfam05622 109 -----LAEEAQALKDEMDILRESSDKV------------------KKLEAtVETYKKKLEdlGDLRRQVKLLEERN--AE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDY--------------------VEDIQTKLPPMSE-------ELNN---KIDDLSQEiKDRKLAEKVSQAES-- 1895
Cdd:pfam05622 164 YMQRTLQLeeelkkanalrgqletykrqVQELHGKLSEESKkadklefEYKKleeKLEALQKE-KERLIIERDTLRETne 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1896 --HAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYID--EAE-KVAKEAKDlAHEATKLATGPRGLlkEDAKGS 1970
Cdd:pfam05622 243 elRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIrlQHEnKMLRLGQE-GSYRERLTELQQLL--EDANRR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1971 LQKsfriLNEAKKLAND-VKENEDHLNGLKTRIENADARNGD---LLRALNDTLGKLSAIpNDTAAKLQAVKDKARQAND 2046
Cdd:pfam05622 320 KNE----LETQNRLANQrILELQQQVEELQKALQEQGSKAEDsslLKQKLEEHLEKLHEA-QSELQKKKEQIEELEPKQD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2047 TAKDVlaQIKELHQNLDglKKNYDKLA------DSVAKTNAVVK--DPSKNKIIADADATVKNLEQEADRLID------- 2111
Cdd:pfam05622 395 SNLAQ--KIDELQEALR--KKDEDMKAmeerykKYVEKAKSVIKtlDPKQNPASPPEIQALKNQLLEKDKKIEhlerdfe 470
|
490
....*....|..
gi 1622930585 2112 KLKPIKELEDNL 2123
Cdd:pfam05622 471 KSKLQREQEEKL 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1684-2080 |
8.66e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1684 ELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKnlETQKEIAEDELVAAEGLLKKVKKLfgeSRG 1763
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQL---KKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1764 KNEEMEKDLREKLADYKNKVDDAwDLLREATNKIREANRLFAVNQKNMTALEK-KKEAVEsgKRQIENTLKEGNDILDEA 1842
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEE--AKKAEELKKKEAEEKKKA 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1843 NRL--ADEINSIidYVEDIQTKlppmSEELNNKIDDLSQEIKDRKLAEKVSQAESHAAQ--LNDSSAVLDGIL---DEAK 1915
Cdd:PTZ00121 1719 EELkkAEEENKI--KAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIEEELdeeDEKR 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1916 NISFNATA--AFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILNEAKKLAN---DVKE 1990
Cdd:PTZ00121 1793 RMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNkeaDFNK 1872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1991 NEDHLNGLKTRIENADA----RNGDLLRAL--NDTLGKLSAIPNDtaaKLQAVKDKARQANDTAKDVLAQIKELHQNLDG 2064
Cdd:PTZ00121 1873 EKDLKEDDEEEIEEADEiekiDKDDIEREIpnNNMAGKNNDIIDD---KLDKDEYIKRDAEETREEIIKISKKDMCINDF 1949
|
410
....*....|....*.
gi 1622930585 2065 LKKNYDKLADSVAKTN 2080
Cdd:PTZ00121 1950 SSKFCDYMKDNISSGN 1965
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1857-2146 |
9.50e-09 |
|
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: 59.69 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1857 EDIQTKLP---PMSEELNNKIDDL---SQEIKDrklaekvsqaesHAAQLNDSsaVLDGILDEAKNIS-FNATAAFKAYS 1929
Cdd:cd22656 26 EEYRKRLGissDIDDKLSSDFDPLldaYKSIKD------------HCTDFKDD--TYPSIVSLAGDIYnYAQNAGGTIDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1930 NIKDYIDEAEKVAKEAKDLAHEAtklatgprglLKEDAKGSLQKsfrILNEAKKLANDVKENEDHLNGLKTRIENADARN 2009
Cdd:cd22656 92 YYAEILELIDDLADATDDEELEE----------AKKTIKALLDD---LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2010 GDLLRALNDTLGK-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsk 2088
Cdd:cd22656 159 ETLEKALKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD--- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 2089 nkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2146
Cdd:cd22656 227 ---LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1713-2140 |
1.24e-08 |
|
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: 61.22 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1713 NLEGLQKEIDQMIKELrrKNLETQKEIAEDELVAAEGLLKKV--KKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDLL 1790
Cdd:TIGR01612 1119 DIKNLDQKIDHHIKAL--EEIKKKSENYIDEIKAQINDLEDVadKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLL 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1791 REATnKIreanrlfavnQKNMTALEKKKEAVESGKRQIENTLKEGNDilDEANRLADEINSIIDYVED---IQTKLPPMS 1867
Cdd:TIGR01612 1197 NEIA-EI----------EKDKTSLEEVKGINLSYGKNLGKLFLEKID--EEKKKSEHMIKAMEAYIEDldeIKEKSPEIE 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1868 EELNNKIDdLSQEIKDRKLAEKVSQAESHAAQLNDSSavldgiLDEAKNISFNATAAFKAYSNIKD-------YIDEAEK 1940
Cdd:TIGR01612 1264 NEMGIEMD-IKAEMETFNISHDDDKDHHIISKKHDEN------ISDIREKSLKIIEDFSEESDINDikkelqkNLLDAQK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1941 VAKEAKDLAHEATKLATgprgLLKedakgsLQKSFRILNEAKKLANDVKENEDHLNglkTRIENADArngdLLRALNDTL 2020
Cdd:TIGR01612 1337 HNSDINLYLNEIANIYN----ILK------LNKIKKIIDEVKEYTKEIEENNKNIK---DELDKSEK----LIKKIKDDI 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2021 gklsaipndtaaKLQAVKDKARQANDtAKDV---LAQIKEL-------HQNLDGLKKNYDKLADSVA-----------KT 2079
Cdd:TIGR01612 1400 ------------NLEECKSKIESTLD-DKDIdecIKKIKELknhilseESNIDTYFKNADENNENVLllfkniemadnKS 1466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2080 NAVVKDpSKNKIIADADATVKNLEQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQ 2140
Cdd:TIGR01612 1467 QHILKI-KKDNATNDHDFNINELKEH----IDKSKGCKDEADKNAKAIEKNKELFEQYKKD 1522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1883 |
1.29e-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: 61.23 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATK-------VTADGEQTGQDAERTNTRAKSLGEFIKE 1684
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1685 LARDAEAVNEKAIKLNETLG---TRDEAFERNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAEGLLKKVKK 1756
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIeslaaEIEELEELIEELESELEALLNERASLEE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1757 LFGESRGKNEEMEKDLREkladYKNKVDDAWDLLREATNKIREANRlfAVNQKNMTALEKKKEAVESGKRQIENTLKEGN 1836
Cdd:TIGR02168 888 ALALLRSELEELSEELRE----LESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 1837 DILDEANRLADEINSI--------------IDYVEDIQTKLppmsEELNNKIDDLSQEIKD 1883
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLenkikelgpvnlaaIEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1905 |
1.32e-08 |
|
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: 59.78 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELARDAEAVNEKAIKLNETLgTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEdelvaAEGLLKKVKKLFGES 1761
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQELAA-----LEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1762 RGKNEEMEKDLREKL-ADYKNKVDDAWDLL---REATNKIREANRLFAVN---QKNMTALEKKKEAVESGKRQIENTLKE 1834
Cdd:COG4942 96 RAELEAQKEELAELLrALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAparREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1835 GNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKD-RKLAEKVSQAESHAAQLNDSSA 1905
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1717-2145 |
1.43e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 60.25 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1717 LQKEIDQMIKELrrknlETQKEIAEDELVAAEglLKKVKKL--FGESRGKNEEMEKDLRE----KLADYKNKVDDAwdll 1790
Cdd:pfam06160 4 LRKKIYKEIDEL-----EERKNELMNLPVQEE--LSKVKKLnlTGETQEKFEEWRKKWDDivtkSLPDIEELLFEA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1791 REATNKIReanrLFAVNQKnMTALEKKKEAVESgkrQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKL------- 1863
Cdd:pfam06160 73 EELNDKYR----FKKAKKA-LDEIEELLDDIEE---DIKQILEELDELLESEEKNREEVEELKDKYRELRKTLlanrfsy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1864 PPMSEELNNKIDDLSQEIkdrklaekvsqaeSHAAQLNDSSAVLD--GILDEAKNisfnATAAFKAY-SNIKDYIDEAEK 1940
Cdd:pfam06160 145 GPAIDELEKQLAEIEEEF-------------SQFEELTESGDYLEarEVLEKLEE----ETDALEELmEDIPPLYEELKT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1941 VAKEAKDlaheatKLATGPRGLLKEdakGSLQKSFRILNEAKKLANDVKENEDHLNglKTRIENADARNGDL---LRALN 2017
Cdd:pfam06160 208 ELPDQLE------ELKEGYREMEEE---GYALEHLNVDKEIQQLEEQLEENLALLE--NLELDEAEEALEEIeerIDQLY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2018 DTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQN--LD----GLKKNYDKLADSVAKTNAVVKdpsknKI 2091
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSytLNenelERVRGLEKQLEELEKRYDEIV-----ER 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 2092 IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:pfam06160 352 LEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1610-2146 |
1.44e-08 |
|
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: 60.83 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1610 YGLENMTQELKHLLSPQRA---PERLIQLAEGNLNTLVTEM------NELLTRATKVTADGEQTGQDAERTNTRAKSLGE 1680
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQElrkAERELSKAEKNSLTETLKKevkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1681 FIKELARDAEAVNEKAIKLNETLGT-----RDEAFERNLEGLQKEIDQMIKELRRKNLETQK------EIAEDELVAAEG 1749
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASleqnknHINNELESKEEQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1750 LLKKVKKLFGESRGKNEEMEKD-LREKL--------------ADYKNKVDDAWDL-----------------LREATNKI 1797
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLErLKEEIeksskqramlagatAVYSQFITQLTDEnqsccpvcqrvfqteaeLQEFISDL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1798 REANRLFAVNQKNMTALEKKKEavesgkrqientlKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIDDL 1877
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKE-------------KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1878 SqeiKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLAT 1957
Cdd:TIGR00606 768 E---EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE-RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1958 GPRGLLK--EDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSaiPNDTA-AKL 2034
Cdd:TIGR00606 844 KIELNRKliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS--PLETFlEKD 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2035 QAVKD----KARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRL- 2109
Cdd:TIGR00606 922 QQEKEelisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMr 1001
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622930585 2110 -----IDKLKpIKE--LEDNL-----KKNISEIKELINQARKQANSIKV 2146
Cdd:TIGR00606 1002 lmrqdIDTQK-IQErwLQDNLtlrkrENELKEVEEELKQHLKEMGQMQV 1049
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1060-1101 |
1.53e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622930585 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1616-2112 |
1.77e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.23 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1616 TQELKHLlspqrapERLIQLAEGNLNTLVTEMNELLTratkvtadgeqtgqdAERTN-TRAKSLGEFIKELARDaeaVNE 1694
Cdd:PRK04778 104 KHEINEI-------ESLLDLIEEDIEQILEELQELLE---------------SEEKNrEEVEQLKDLYRELRKS---LLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1695 KAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKNLETQKEI---AEDELVAAEGLLKKVKKLFgesrgknEEMEKD 1771
Cdd:PRK04778 159 NRFSFGPAL----DELEKQLENLEEEFSQFVELTESGDYVEAREIldqLEEELAALEQIMEEIPELL-------KELQTE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1772 LREKLADyknkvddawdlLREATNKIREANRLFAVNQknmtaLEKKKEAVESGKRQIENTLKEGNdiLDEANRLADEINS 1851
Cdd:PRK04778 228 LPDQLQE-----------LKAGYRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1852 IIDYVEDIqtklppmseelnnkiddLSQEIKDRKLAEKVSqaeshaaqlndssavldgildeaknisfnataafkaySNI 1931
Cdd:PRK04778 290 RIDQLYDI-----------------LEREVKARKYVEKNS-------------------------------------DTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1932 KDYIDEAEKVAKEakdLAHEATklatgprgllkedakgSLQKSFRI----LNEAKKLANDVKENEDHLNGLKTRIENADA 2007
Cdd:PRK04778 316 PDFLEHAKEQNKE---LKEEID----------------RVKQSYTLneseLESVRQLEKQLESLEKQYDEITERIAEQEI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2008 RNGDLLRALNDTLGKLSAIPN---DTAAKLQAVKDKARQANDTAKDVLAQIKELH-----QNLDGLKKNY-DKLADSVAK 2078
Cdd:PRK04778 377 AYSELQEELEEILKQLEEIEKeqeKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylekSNLPGLPEDYlEMFFEVSDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622930585 2079 TNAVVKDPSKNKI--------IADADATVKNLEQEADRLIDK 2112
Cdd:PRK04778 457 IEALAEELEEKPInmeavnrlLEEATEDVETLEEETEELVEN 498
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
865-914 |
2.28e-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: 52.36 E-value: 2.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 865 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDARN 914
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
413-465 |
3.82e-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: 51.97 E-value: 3.82e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 413 PCHCNPVGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTGYPD 465
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1612-1902 |
7.31e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNET-------LGTRDE---AFERNLEGLQKEIDQMIKELRR-KNLETQKEIAEDELVAAEGLLKKVKKLFGE 1760
Cdd:COG4372 127 LEQQRKQLEAQiaelqseIAEREEelkELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1761 SRGKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILD 1840
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 1841 EANRLADEINSIIDYVEDIQTKLPPMSEE----LNNKIDDLSQEIKDRKLAEKVSQAESHAAQLND 1902
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDallaALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1638-2181 |
7.76e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1638 GNLNTLVTEM----NELLTRATKVTA---DGEQTGQDAERTNTRAKSLGEfIKELARDAEAvNEKAIKLNETLGTRDEAF 1710
Cdd:COG4913 207 GDLDDFVREYmleePDTFEAADALVEhfdDLERAHEALEDAREQIELLEP-IRELAERYAA-ARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1711 --ERNLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEGLLKKVKKLFGESRGKN-EEMEKDLREKLADyKNKVDDAW 1787
Cdd:COG4913 285 faQRRLELLEAELEELRAELAR--LEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERE-LEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1788 DLLREATNKIREANRL----FAVNQKN----MTALEKKKEAVESGKRQIENTLKEGNDildEANRLADEINSI------I 1853
Cdd:COG4913 362 ARLEALLAALGLPLPAsaeeFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLerrksnI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1854 D-YVEDIQTKLppmSEELNNKIDDL-----------------------------------------SQEIKDRKLAEKV- 1890
Cdd:COG4913 439 PaRLLALRDAL---AEALGLDEAELpfvgelievrpeeerwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLv 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1891 -SQAESHAAQLNDSSAVLDGILDEaknISFNATAaFKAYsnIKDYIDEAEKVAK--EAKDLAHEATKLaTgPRGLLKEDA 1967
Cdd:COG4913 516 yERVRTGLPDPERPRLDPDSLAGK---LDFKPHP-FRAW--LEAELGRRFDYVCvdSPEELRRHPRAI-T-RAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1968 K-GSLQKSFRIL--------NEAKK--LANDVKENEDHLNGLKTRIENADARnGDLLRALNDTLGKLSAIPND------- 2029
Cdd:COG4913 588 TrHEKDDRRRIRsryvlgfdNRAKLaaLEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWDeidvasa 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2030 --TAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVK------DPSKNKIIADADATVKN 2101
Cdd:COG4913 667 erEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeeelDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2102 LEQEADRLIDKL---KPIKELEDNLKKNISEIKELINQARKQANsikvsvssggDCIRTYKPEikkgsYNNIVVNVKTAV 2178
Cdd:COG4913 747 LRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELE----------RAMRAFNRE-----WPAETADLDADL 811
|
...
gi 1622930585 2179 ADN 2181
Cdd:COG4913 812 ESL 814
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-799 |
8.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 8.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930585 757 CQC--FGHA-ESCDDVTGECLnCKDHTDGPYCDKCLPGFYGDPTKG 799
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. |
469-515 |
8.91e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 8.91e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 469 CNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNLQEDNWKGC 515
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1682-2044 |
1.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELARDAEAVnEKAIKLNETLGTRD--------EAFERNLEGLQKEIDQMIKELRRK-----NLETQKEIAEDELVAAE 1748
Cdd:COG1196 202 LEPLERQAEKA-ERYRELKEELKELEaellllklRELEAELEELEAELEELEAELEELeaelaELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKLFGESRGK----------NEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKK 1818
Cdd:COG1196 281 LELEEAQAEEYELLAElarleqdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1819 EAVESGKRQIENTLKEgndILDEANRLADEINSIIDYVEDIQTKLppmsEELNNKIDDLSQEIkDRKLAEKVSQAESHAA 1898
Cdd:COG1196 361 AEAEEALLEAEAELAE---AEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERL-ERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1899 QLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLAtgPRGLLKEDAKGSLQ------ 1972
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA--ARLLLLLEAEADYEgflegv 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1973 KSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDT-------------LGKLSAIPNDTAAKLQAVKD 2039
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEvaaaaieylkaakAGRATFLPLDKIRARAALAA 590
|
....*
gi 1622930585 2040 KARQA 2044
Cdd:COG1196 591 ALARG 595
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1650-1905 |
1.25e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1650 LLTRATKVTADGEQTGQDAE--RTNTRAKSLGEFIKELARDAEAVNEKAIKLNEtlgtrdeaferNLEGLQKEIDQMIKE 1727
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQA-----------ELEALQAEIDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1728 LRrknlETQKEIAEdelvaaegllkkvkklfgesrgKNEEMEKDLReklADYKN-KVDDAWDLL------------REAT 1794
Cdd:COG3883 74 IA----EAEAEIEE----------------------RREELGERAR---ALYRSgGSVSYLDVLlgsesfsdfldrLSAL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1795 NKIREANR-LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNK 1873
Cdd:COG3883 125 SKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270
....*....|....*....|....*....|..
gi 1622930585 1874 IDDLSQEIKDRKLAEKVSQAESHAAQLNDSSA 1905
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
414-466 |
1.36e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 414 CHCNPVGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTG--YPDC 466
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1717-2145 |
1.42e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.15 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1717 LQKEIDQMIKELrrknlETQKEIAEDELVAAEglLKKVKKL--FGESRGKNEEMEKDLRE----KLADYKNKVDDAwdll 1790
Cdd:PRK04778 23 LRKRNYKRIDEL-----EERKQELENLPVNDE--LEKVKKLnlTGQSEEKFEEWRQKWDEivtnSLPDIEEQLFEA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1791 REATNKIReanrLFAVnQKNMTALEKKKEAVESgkrQIENTLKEGNDIL--DEANRlaDEINSIIDYVEDIQTKL----- 1863
Cdd:PRK04778 92 EELNDKFR----FRKA-KHEINEIESLLDLIEE---DIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLlanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1864 --PPMSEELNNKIDDLSQEIKD-RKLAEK--VSQAESHAAQLNDSSAVLDGILDEaknisfnataafkaysnIKDYIDEA 1938
Cdd:PRK04778 162 sfGPALDELEKQLENLEEEFSQfVELTESgdYVEAREILDQLEEELAALEQIMEE-----------------IPELLKEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1939 EKVakeakdLAHEATKLATGPRGLLKEdakGSLQKSFRILNEAKKLANDVKENEDHLNGLKtrIENADARNGDL---LRA 2015
Cdd:PRK04778 225 QTE------LPDQLQELKAGYRELVEE---GYHLDHLDIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIqerIDQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2016 LNDTLGKlsaipnDTAAKLQAVKDKARQANDTAKdVLAQIKELHQNLDGLKKNYdKLADS-VAKTNAVVKDpsKNKIIAD 2094
Cdd:PRK04778 294 LYDILER------EVKARKYVEKNSDTLPDFLEH-AKEQNKELKEEIDRVKQSY-TLNESeLESVRQLEKQ--LESLEKQ 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 2095 ADATVKNLEQEA----------DRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:PRK04778 364 YDEITERIAEQEiayselqeelEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYR 424
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1962-2146 |
1.54e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1962 LLKEDAKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDL---LRALNDTLGKLSAIPNDTAAKLQAVK 2038
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2039 DKARQANdtakdvlAQIKELHQNLDGLKKNYDKLADSVAKTnavvkdpskNKIIADADATVKNLEQEADRLIDKLKPIKE 2118
Cdd:COG4372 108 EEAEELQ-------EELEELQKERQDLEQQRKQLEAQIAEL---------QSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190
....*....|....*....|....*....|
gi 1622930585 2119 LEDNLKKN--ISEIKELINQARKQANSIKV 2146
Cdd:COG4372 172 ELQALSEAeaEQALDELLKEANRNAEKEEE 201
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1630-1847 |
2.08e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.14 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTNTRAKSLGEFIKELAR------------DA 1689
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEATVEGNSLVEKARtdadellvgarrDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1690 EAVNEKAiklnETLGTRDEAfernleglqkEIDQMIKELRRKNLETQKEIAE--DELV-AAEgllkkvkklfgESRGKNE 1766
Cdd:NF041483 1117 TAIRERA----EELRDRITG----------EIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1767 EMEKDLREKLADYKNK-----VDDAWDLLREATNK----IREANRLFAvnqknmTALEKKKEAVESGKRQIENTLKEGND 1837
Cdd:NF041483 1172 AKAKELVSDANSEASKvriaaVKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRELDVLVRRRED 1245
|
250
....*....|
gi 1622930585 1838 ILDEANRLAD 1847
Cdd:NF041483 1246 INAEISRVQD 1255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1613-1849 |
3.88e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.21 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1613 ENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAV 1692
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1693 NEKAIKLNETLGTRDEAFERNLEG---LQKEIDQMIKELR-----RKNLETQ-KEIAEDELVAAEGLLKKVKKLFGESRG 1763
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSnkkAQDKVNDIKEKVKnihgyMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEK 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1764 KNEEMEKDLREKLADY-KNKVDDAW---DL-LREATNKIREANRLFAVNQKNMTALE--KKKEAVESGKRQIENTLKEGN 1836
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIdTQKIQERWlqdNLtLRKRENELKEVEEELKQHLKEMGQMQvlQMKQEHQKLEENIDLIKRNHV 1071
|
250
....*....|...
gi 1622930585 1837 DILDEANRLADEI 1849
Cdd:TIGR00606 1072 LALGRQKGYEKEI 1084
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1617-2145 |
5.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1617 QELKHLLSPQRApERLIQLAEGNLNTLVTEMNELLTRATKVTAD-GEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEK 1695
Cdd:COG4913 275 EYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEARlDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1696 aikLNETLGTRDEaFERNLEGLQKEIDQMIKELRRknletQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREK 1775
Cdd:COG4913 354 ---LEERERRRAR-LEALLAALGLPLPASAEEFAA-----LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1776 ---LADYKN-------KVDDAWDLLREATNKIREANRLFA----VNQKN---MTALEK------------------KKEA 1820
Cdd:COG4913 425 eaeIASLERrksnipaRLLALRDALAEALGLDEAELPFVGelieVRPEEerwRGAIERvlggfaltllvppehyaaALRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1821 VES---GKR----QIENTLKEGNDILDEANRLADEI----NSIIDYVEDiqtklppmseELNNK--------IDDLSQ-- 1879
Cdd:COG4913 505 VNRlhlRGRlvyeRVRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEA----------ELGRRfdyvcvdsPEELRRhp 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1880 ----------------EIKDRKL-----------AEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIK 1932
Cdd:COG4913 575 raitragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1933 DYIDEAEKVAKEAKDLAHeatklatgprgllKEDAKGSLQKSFRILNEAKK----LANDVKENEDHLNGLKTRIENADAR 2008
Cdd:COG4913 655 EYSWDEIDVASAEREIAE-------------LEAELERLDASSDDLAALEEqleeLEAELEELEEELDELKGEIGRLEKE 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2009 NGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKT----NAVVK 2084
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWP 801
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2085 DPSknkiiADADATVKNLEQ--------EADRLIDKLKPIKELednLKKN-ISEIKELINQARKQANSIK 2145
Cdd:COG4913 802 AET-----ADLDADLESLPEylalldrlEEDGLPEYEERFKEL---LNENsIEFVADLLSKLRRAIREIK 863
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1420-1466 |
9.04e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 9.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1420 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1466
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1917-2169 |
9.06e-07 |
|
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: 54.00 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1917 ISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLK--EDAKGSLQKSFRILN-EAKKLANDVKENED 1993
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEqELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1994 HLNGLKTRIENADARNGDLLRALnDTLGKLSAI--------PNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGL 2065
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2066 KKNYDKLADSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
250 260 270
....*....|....*....|....*....|.
gi 1622930585 2146 VSVSSG-------GDCIRTYKPEIKKGSYNN 2169
Cdd:COG4942 248 FAALKGklpwpvsGRVVRRFGERDGGGGRNK 278
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1826-2066 |
9.36e-07 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 53.06 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1826 RQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSE------ELNNKIDDLSQEIKDR--KLAEKVSQAESHA 1897
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAAtaqsaaEAAEEGREAVEDAITAmdQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1898 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfKAysnikdyiDEAEK----VAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1965 E------DAKGSLQKSFRILNEAKKLANDVKENedhLNGLKTRIENADARNGDLLRALND---TLGKLSAIPNDTAAKLQ 2035
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDA---LEEIVDSVEEIADLVQEIAAATDEqaaGSEEVNAAIDEIAQVTQ 231
|
250 260 270
....*....|....*....|....*....|.
gi 1622930585 2036 AVKDKARQANDTAKDVLAQIKELHQNLDGLK 2066
Cdd:smart00283 232 ETAAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1793-2036 |
9.39e-07 |
|
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: 54.00 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1793 ATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIdyvEDIQTKLppmsEELNN 1872
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAEL----AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1873 KIDDLSQEIKDRK--LAEKVSqaeshAAQLNDSSAVLDGILDeakniSFNATAAFKAYSNIKDYIDEaekVAKEAKDLAH 1950
Cdd:COG4942 91 EIAELRAELEAQKeeLAELLR-----ALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPA---RREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1951 EATKLATgprglLKEDAKGSLQKSFRILNEA----KKLANDVKENEDHLNGLKTRIENADARNGDLLRA---LNDTLGKL 2023
Cdd:COG4942 158 DLAELAA-----LRAELEAERAELEALLAELeeerAALEALKAERQKLLARLEKELAELAAELAELQQEaeeLEALIARL 232
|
250
....*....|...
gi 1622930585 2024 SAIPNDTAAKLQA 2036
Cdd:COG4942 233 EAEAAAAAERTPA 245
|
|
| auto_Ata |
NF033481 |
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ... |
1665-2204 |
1.64e-06 |
|
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 54.49 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1665 GQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET-----------------LGTRDEAFERNLEGLQKeiDQMIKE 1727
Cdd:NF033481 642 GKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENavavgqgaqslveggvaLGARSKVEAKNSVALGQ--DAVATE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1728 LRRKNLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREkLADYKNKVDdawdllREATNKIREANRLFAVN 1807
Cdd:NF033481 720 ATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQ-LKNVDSRVN------QNTSNIGKNTQNITNLN 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1808 QK-NMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPM----SEELNNKIDDLSQEIK 1882
Cdd:NF033481 793 QKlDDTKTNLGNQITDTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTELNNTigntKTELNTKIDNTKTELE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1883 D--------------RKLAEKV-----SQAESHAAQLNDSSAVL----DGI----LDEAK---------NISFNATAAFK 1926
Cdd:NF033481 873 NkglnfagnsgadvhRKLGDKLnivggAAASTPAAKTSGENVITrttqDGIqielLKDSKfdsvttgntTLNTNGLTIKE 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1927 AYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILNEAKK-LANDVKENEDHLNGLKTRIENa 2005
Cdd:NF033481 953 GPSITKQGINAGSKQITNVADGINAKDAVNVDQLTKVKENLNGRITDTNNQLNDAKKdLGNQIADTNKNLNDAKKDLGD- 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2006 daRNGDLLRALNDTLGKLSAIPNDTAAKLQAV--KDKARQANDTAKDVLAQIKELHQNLdGLKKNYDKLADSVAKTNAVV 2083
Cdd:NF033481 1032 --QITDTNTKLNNTKDQLTTQINDTKTELNNTigNTKTELENKGLNFAGNSGADVHRKL-GDKLNIVGGAAASTPAAKTS 1108
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2084 KDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcirtyKPEIK 2163
Cdd:NF033481 1109 GENVITRTTKDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINAGGKQITNVADGINA--------KDAVN 1180
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622930585 2164 KGSYNNIVvnVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:NF033481 1181 KGQLDNLA--AKQNATDDAAVKYDDAKTKDKVTLKGKDGTV 1219
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
287-334 |
1.75e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 287 CICYGHA---RACplDPATnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 334
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
807-862 |
1.81e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 807 CACPLNIPSnnfSPTCHldrSLGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGSC 862
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1684-1885 |
1.87e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 51.29 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1684 ELARDAEAV----NEKAIKLNETLGTRD-----------EAFERNLEGLQKEIDQMIkelrrknlETQKEIAEDELVAAE 1748
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKLfgesrgknEEMEKDLREKLADYKNKVDDAWDLLR------EATNKIREANRLFAVN---------QKNMTA 1813
Cdd:cd00176 76 EIQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQffrdadDLEQWLEEKEAALASEdlgkdlesvEELLKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1814 LEKKKEAVESGKRQIENTLKEGNDILDEANRLADeinsiidyvEDIQTKLppmsEELNNKIDDLSQEIKDRK 1885
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEKL----EELNERWEELLELAEERQ 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1612-1915 |
3.24e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLaEGNLNTLVTEMNELLTRATKVT---ADGEQTGQDAERTNTRAKSLGEF------- 1681
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslatee 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 -IKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEGLL--------- 1751
Cdd:COG4717 193 eLQDLAEELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggsl 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1752 -------------------------KKVKKLFGESRGK-------NEEMEKDLREKLADYKNKVDDAWDLLREATNKIRE 1799
Cdd:COG4717 269 lsliltiagvlflvlgllallflllAREKASLGKEAEElqalpalEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1800 ANRLFA------------VNQKNMTAL----------------------EKKKEAVESGKRQIENTLKEGNDILDEAN-- 1843
Cdd:COG4717 349 LQELLReaeeleeelqleELEQEIAALlaeagvedeeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDee 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1844 RLADEINSIIDYVEDIQTKLppmsEELNNKIDDLSQEIK----DRKLAEKVSQAESHAAQLND------SSAVLDGILDE 1913
Cdd:COG4717 429 ELEEELEELEEELEELEEEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRElaeewaALKLALELLEE 504
|
..
gi 1622930585 1914 AK 1915
Cdd:COG4717 505 AR 506
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1672-1835 |
3.56e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAfERNLEGLQKEIDQM--------------------IKELRRK 1731
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIERLewrqqtevlspeeekelvekIKELEKE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1732 nLETQKEIAE-----DELVA--------AEGLLKKVKKLFGESRGKNEEMEK------DLREKLADYKNKVDDAWDLLRE 1792
Cdd:COG1340 149 -LEKAKKALEkneklKELRAelkelrkeAEEIHKKIKELAEEAQELHEEMIElykeadELRKEADELHKEIVEAQEKADE 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 1793 ATNKIREANR--------LFAVNQKNM-TALEKKKEAVESGKRQIENTLKEG 1835
Cdd:COG1340 228 LHEEIIELQKelrelrkeLKKLRKKQRaLKREKEKEELEEKAEEIFEKLKKG 279
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
806-863 |
3.75e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 3.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 806 PCACPLNIpsnNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGsCQ 863
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1844-2063 |
4.18e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 49.57 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1844 RLADEINSIIDYVEDIQTKLPPMSEE----LNNKIDDLSQEIkDRKLAEKVSQAESHAAQLNdssAVLDGILDEAKNIsf 1919
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQElvdrLEKETEALRERL-QKDLEEVRAKLEPYLEELQ---AKLGQNVEELRQR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1920 nataafkaysnIKDYIDE-AEKVAKEAKDLaheATKLATgprglLKEDAKGSLQKSfrilneakklANDVKENedhlngL 1998
Cdd:pfam01442 75 -----------LEPYTEElRKRLNADAEEL---QEKLAP-----YGEELRERLEQN----------VDALRAR------L 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 1999 KTRIENADARNGDLLRALNDTLgklsaipndtAAKLQAVKDKARQANDTAKDVLA-QIKELHQNLD 2063
Cdd:pfam01442 120 APYAEELRQKLAERLEELKESL----------APYAEEVQAQLSQRLQELREKLEpQAEDLREKLD 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1663-2114 |
4.57e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1663 QTGQDAERTNTRAKS--LGEFIKELARDAEavnEKAIKLNETLGTRD--EAFERNLEGLQKEI----------DQMIKEL 1728
Cdd:pfam10174 344 QTEVDALRLRLEEKEsfLNKKTKQLQDLTE---EKSTLAGEIRDLKDmlDVKERKINVLQKKIenlqeqlrdkDKQLAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1729 RR--KNLET------------QKEIAEDELVAAEglLKKVKKLfgESRGKNEEMEkDLREKLADYKNKVDDawdLLREAT 1794
Cdd:pfam10174 421 KErvKSLQTdssntdtalttlEEALSEKERIIER--LKEQRER--EDRERLEELE-SLKKENKDLKEKVSA---LQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1795 NKIREANRLfavnQKNMTALEKKKEAVESGKRQIENTLKEGndiLDEANRLADEINSIIDYVEDIQTKlppmsEELNNKI 1874
Cdd:pfam10174 493 EKESSLIDL----KEHASSLASSGLKKDSKLKSLEIAVEQK---KEECSKLENQLKKAHNAEEAVRTN-----PEINDRI 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1875 DDLSQEIKDRKLAEKVSQAESHAaqlndssavLDGILDEAKNisfnataafkaYSNIKD-YIDEAEKVA-KEAKDLAHEA 1952
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVER---------LLGILREVEN-----------EKNDKDkKIAELESLTlRQMKEQNKKV 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1953 TKLATGPRGLLKEDAKgslqksfrILNEAKKLANDVKEN------EDHLNGL-KTR--IENADARNGDLLRALNDTLGKL 2023
Cdd:pfam10174 621 ANIKHGQQEMKKKGAQ--------LLEEARRREDNLADNsqqlqlEELMGALeKTRqeLDATKARLSSTQQSLAEKDGHL 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2024 SAIPNDTAAKLQAVKDKARQAndtakdVLAQIKELHQNLDGLkknydKLADSVAKTNAvvkdpsknkiiadadATVKNLE 2103
Cdd:pfam10174 693 TNLRAERRKQLEEILEMKQEA------LLAAISEKDANIALL-----ELSSSKKKKTQ---------------EEVMALK 746
|
490
....*....|.
gi 1622930585 2104 QEADRLIDKLK 2114
Cdd:pfam10174 747 REKDRLVHQLK 757
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1976-2175 |
4.76e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1976 RILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSaipnDTAAKLQavKDKARQAN-DTAKDVLAQ 2054
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIK--KYEEQLGNvRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2055 IKElhqnLDGLKKNYDKLADSVAKtnavvkdpsKNKIIADADATVKNLEQEADRLIDKLkpiKELEDNLKKNISEIKELI 2134
Cdd:COG1579 95 QKE----IESLKRRISDLEDEILE---------LMERIEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622930585 2135 NQARKQANSIKVSVSSggDCIRTYKpEIKKGSYNNIVVNVK 2175
Cdd:COG1579 159 EELEAEREELAAKIPP--ELLALYE-RIRKRKNGLAVVPVE 196
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1647-1901 |
5.41e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1647 MNELLTraTKVTADGEQTGQD-------AERTNTRaksLGEFIKELA---RDAEAVNEKAIKLNETLGTRDEAFERNLEG 1716
Cdd:pfam07888 3 LDELVT--LEEESHGEEGGTDmllvvprAELLQNR---LEECLQERAellQAQEAANRQREKEKERYKRDREQWERQRRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1717 LQKEIDQMIKELRRKNLETQK-EIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDLLREATN 1795
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEElEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1796 KIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDE----ANRLADEINSIIDYVEDIQTK---LPPMSE 1868
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKeaeNEALLE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622930585 1869 ELNNKIDDL--SQ---EIKDRKLAEKVSQ-----AESH-----AAQLN 1901
Cdd:pfam07888 238 ELRSLQERLnaSErkvEGLGEELSSMAAQrdrtqAELHqarlqAAQLT 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1649-1948 |
5.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1649 ELLTRATKVTADGEQTgQDAERTNTRAKSLGEFIKELARDAEAVNekaiKLNETLGTRDEAFERNLEGLQKEIDQMIKEl 1728
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKKEAEEKKKAEELK----KAEEENKIKAAEEAKKAEEDKKKAEEAKKA- 1683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1729 rrknlETQKEIAEDELVAAEGLLKK---VKKLFGESRGKNEEMEKDLREKladyKNKVDDAWDLLREATNKIREANRlfA 1805
Cdd:PTZ00121 1684 -----EEDEKKAAEALKKEAEEAKKaeeLKKKEAEEKKKAEELKKAEEEN----KIKAEEAKKEAEEDKKKAEEAKK--D 1752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1806 VNQKNMTALEKKKE--AVESGKRQIENTLKEGNDILDEANRLADE--INSIIDYVEDIQtklppmseELNNKIDDLSQEI 1881
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEekKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkIKDIFDNFANII--------EGGKEGNLVINDS 1824
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 1882 KDRKLAEKVSQAESHAAQLNDSSAVLDGILDEaKNIS---FNATAAF-KAYSNIKDYIDEAEKvAKEAKDL 1948
Cdd:PTZ00121 1825 KEMEDSAIKEVADSKNMQLEEADAFEKHKFNK-NNENgedGNKEADFnKEKDLKEDDEEEIEE-ADEIEKI 1893
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1634-1866 |
7.03e-06 |
|
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: 50.83 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1634 QLAEGNLNTLVTEMNELLTRATKVTADGEQtgQDAertntrAKSLGEFIKELARDAEAVNEKAIKLNETLGTrdeaFERN 1713
Cdd:cd22656 83 QNAGGTIDSYYAEILELIDDLADATDDEEL--EEA------KKTIKALLDDLLKEAKKYQDKAAKVVDKLTD----FENQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1714 LEGLQKeidqmikelrrkNLETQKEIAEDELVAAEGLL--KKVKKLFGESRGKNEEMEKDLrekladyKNKVDDAWDLLR 1791
Cdd:cd22656 151 TEKDQT------------ALETLEKALKDLLTDEGGAIarKEIKDLQKELEKLNEEYAAKL-------KAKIDELKALIA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622930585 1792 EATNKIREANRLFAvnqknmtALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPM 1866
Cdd:cd22656 212 DDEAKLAAALRLIA-------DLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAA 279
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
1679-1809 |
1.06e-05 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 47.74 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1679 GEFIKELARDAeaVNEKAIKLNETLGTRD---EAFE---RNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAegllk 1752
Cdd:pfam06810 12 GKDIPKAKFDE--VNTERDTLKEQLATRDkqlKDLKkvaKDNEELQKQIDELQAKNKDAEADYEAKIADLKFDNA----- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1753 kVKKLFGESRGKNeemEKDLREKLADYKNKVDDAWDL--LREATNKIREANR-LFAVNQK 1809
Cdd:pfam06810 85 -IKLALKGAKAKN---EKAVKALLDKDKLKLKDDGTLigLDEQIEGLKESDKyLFEQEQK 140
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1612-1940 |
1.08e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLspQRAPERLIQLAegnlNTLVTEMNELltratkvtadgEQTGQDAERTNTRAKSLgEFIKELardaEA 1691
Cdd:pfam06160 184 LEEETDALEELM--EDIPPLYEELK----TELPDQLEEL-----------KEGYREMEEEGYALEHL-NVDKEI----QQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRD-EAFERNLEGLQKEIDQM------------------------IKELRRKNLETQKEI------- 1739
Cdd:pfam06160 242 LEEQLEENLALLENLElDEAEEALEEIEERIDQLydllekevdakkyveknlpeiedyLEHAEEQNKELKEELervqqsy 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1740 --AEDELVAAEGLLKKVKKLfgesRGKNEEMEKDLREKLADYKNKVDDawdllreatnkireanrlFAVNQKNMTALEKK 1817
Cdd:pfam06160 322 tlNENELERVRGLEKQLEEL----EKRYDEIVERLEEKEVAYSELQEE------------------LEEILEQLEEIEEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1818 KEAVESGKRQIENTLKEGNDILDEANRladEINSIIDYVEdiQTKLPPMSEELNNKIDDLSQEIKDrkLAEKVSQA---- 1893
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKL---ELREIKRLVE--KSNLPGLPESYLDYFFDVSDEIED--LADELNEVplnm 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1894 ESHAAQLNDSSAVLDGILDEAKNISFNATAAFKA--YSN--------IKDYIDEAEK 1940
Cdd:pfam06160 453 DEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQLiqYANryrssnpeVAEALTEAEL 509
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1469-1524 |
1.09e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.04 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 1469 CACPLISSSnnfSPSCVTEGlddYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1524
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1847-2145 |
1.12e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 50.38 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1847 DEINSIIDYVEDIQ---TKLPPMSEELN-NKIDDLSQEIKD-RKLAEKVSQaesHAaqlNDSSAVLDGILDEAKNISfNA 1921
Cdd:NF033928 6 EDWISIQKYVQAALalpTTLEEVESYLGyPKDGIPGLEPKDlLDLFQNIRN---HA---RSWSNLEPKIKQLANDLA-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1922 TAAFKAYSN-IKDYIDEAeKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKsfrILneaKKLANDVKENEDHLNGLKT 2000
Cdd:NF033928 79 ARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---EDLKNDIKDYQQKADDVKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2001 RIenadarnGDLLRALNDTLgklsaipndtAAKLQAVKDKAR--QANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAK 2078
Cdd:NF033928 152 EL-------DDFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEKEIEQLNKEYDDYVKLSFT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2079 T----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLKKNISEIKELINQARKQAN 2142
Cdd:NF033928 215 GlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQTSLDDILTRMEDALPALK 287
|
...
gi 1622930585 2143 SIK 2145
Cdd:NF033928 288 KLK 290
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
469-515 |
1.13e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 469 CNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNlqeDNWKGC 515
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1630-1884 |
1.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEgnlntLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrDEA 1709
Cdd:PRK02224 499 ERAEDLVE-----AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA---EEA 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1710 FER--NLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEGLLKKVKKLfGESRGKNEEMEKDLREKLADYKNKVDDaw 1787
Cdd:PRK02224 571 REEvaELNSKLAELKERIESLER--IRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKRERKRELEAEFDE-- 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1788 DLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEinsiIDYVEDIQTKlppmS 1867
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENR----VEALEALYDE----A 717
|
250
....*....|....*..
gi 1622930585 1868 EELNNKIDDLSQEIKDR 1884
Cdd:PRK02224 718 EELESMYGDLRAELRQR 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
468-515 |
1.22e-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: 44.65 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 468 ACNCSGLGSKNE--DPCFGPCNCKENVEGGDCSRCKSGFFNLQEdNWKGC 515
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1929-2270 |
1.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1929 SNIKDYIDEAEKVAKEAKDLAHEAtklatgprgllkEDAKGSLQKsfrILNEAKKLANDVKENEDHLNGLKTRIENADAR 2008
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAEL------------EELNEEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2009 NGDLLRAL---NDTLGKLSAI-----PNDTAAKLQAVKdkarQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTN 2080
Cdd:COG3883 88 LGERARALyrsGGSVSYLDVLlgsesFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2081 AVVKDpSKNKI---IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRT 2157
Cdd:COG3883 164 AELEA-AKAELeaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2158 YKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIemrKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIMASRT 2237
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA---GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGA 319
|
330 340 350
....*....|....*....|....*....|....
gi 1622930585 2238 GR-NGTISVRALDGPKASIVPSTYHSTSPPGYTI 2270
Cdd:COG3883 320 GAvVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1666-2134 |
1.61e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1666 QDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIK--ELRRKN-LETQKEIAED 1742
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEyvKLPELNkLHEVESKLKE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1743 ELVAAEGLLKKVKKLFGESRGKNEEMEKDLREKLADYKNKvddawDLLREATNKIREANRLFAVNQKNMtalekKKEAVE 1822
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY-----GALQESTKQLKELPVEVAELQSAS-----KIISSE 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1823 SGKRQIENTLKE-GNDILDEANRLADEINSIIDYVED--IQTKLPPMSEELNNKIDDLsqEIKDRKLAEKVSQAESHAAQ 1899
Cdd:COG5022 1039 STELSILKPLQKlKGLLLLENNQLQARYKALKLRRENslLDDKQLYQLESTENLLKTI--NVKDLEVTNRNLVKPANVLQ 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1900 LNDSSAVLDGILDEAKniSFNAtaafKAYSNIKDY---IDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKgslqKSFR 1976
Cdd:COG5022 1117 FIVAQMIKLNLLQEIS--KFLS----QLVNTLEPVfqkLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL----YQSA 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1977 ILNEAKKLA-NDVKENEDHLNGLKTRIenadaRNGDLLRALNDTLGKLSAIPNDTAAKLQAVKD----KARQANDTAKDV 2051
Cdd:COG5022 1187 LYDEKSKLSsSEVNDLKNELIALFSKI-----FSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNlnkkFDTPASMSNEKL 1261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2052 LAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDPSKNKIIADADA----TVKNLEQEADRLIDKLKPIK------ELED 2121
Cdd:COG5022 1262 LSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSlrwkSATEVNYNSEELDDWCREFEisdvdeELEE 1341
|
490 500
....*....|....*....|..
gi 1622930585 2122 N---------LKKNISEIKELI 2134
Cdd:COG5022 1342 LiqavkvlqlLKDDLNKLDELL 1363
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1930-2137 |
1.64e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.87 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1930 NIKDYIDEAEKVAKEAKDLAHEATKLATGPRG----------LLKED---AKGSLQKSFRILNEAKKLAndvKENEdhlN 1996
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAEKRAEKAEAevaalnrriqLLEEElerTEERLAEALEKLEEAEKAA---DESE---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1997 GLKTrIENADARNGDLLRALNDTLGKLSAIPNDT-------AAKLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNY 2069
Cdd:pfam00261 79 GRKV-LENRALKDEEKMEILEAQLKEAKEIAEEAdrkyeevARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2070 DKLADSVAKTNAVvKDPSKNKI-------------IADADATVKNLEQEADRLIDKLkpikELEdnlKKNISEIKELINQ 2136
Cdd:pfam00261 158 KSLEASEEKASER-EDKYEEQIrflteklkeaetrAEFAERSVQKLEKEVDRLEDEL----EAE---KEKYKAISEELDQ 229
|
.
gi 1622930585 2137 A 2137
Cdd:pfam00261 230 T 230
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1768-2136 |
1.96e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.40 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1768 MEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLAD 1847
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKdrKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKA 1927
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALL--ELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1928 YSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSLQKSFRILNEAKKLANDVKENEdhlngLKTRIEnADA 2007
Cdd:COG0840 160 AAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGD-----LTVRID-VDS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2008 RN--GDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKELHQNLDG-------LKKNYDKLADSVAK 2078
Cdd:COG0840 234 KDeiGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEEtaaameeLSATVQEVAENAQQ 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 2079 TNAVVKDPSK-----NKIIADADATVKNLEQEADRLIDKlkpIKELEDNLKKnISEIKELINQ 2136
Cdd:COG0840 314 AAELAEEASElaeegGEVVEEAVEGIEEIRESVEETAET---IEELGESSQE-IGEIVDVIDD 372
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
807-855 |
2.03e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 807 CACPlniPSNNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQP 855
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1612-1829 |
2.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRD-EAFERNLEGLQKEIDQ---MIKELR--RKNLETQKEIAEDELVAAEGLLKKVkklfgesrgkn 1765
Cdd:COG3883 98 SGGSVSYLDVLLGSESfSDFLDRLSALSKIADAdadLLEELKadKAELEAKKAELEAKLAELEALKAEL----------- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930585 1766 EEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIE 1829
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1616-1776 |
2.23e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 47.64 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1616 TQELKHLLSP--QRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQT-GQDAERTNTRAKSLGEFIKE-LARDAEA 1691
Cdd:pfam01442 13 AEELQEQLGPvaQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKlGQNVEELRQRLEPYTEELRKrLNADAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNEtlGTRDEAfERNLEGLQKEIDQMIKELRRK---NLETQKEIAEDelvAAEGLLKKVKKLFGESRGKNEEM 1768
Cdd:pfam01442 93 LQEKLAPYGE--ELRERL-EQNVDALRARLAPYAEELRQKlaeRLEELKESLAP---YAEEVQAQLSQRLQELREKLEPQ 166
|
....*...
gi 1622930585 1769 EKDLREKL 1776
Cdd:pfam01442 167 AEDLREKL 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-2145 |
2.66e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKEL----AR 1687
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1688 DAEAvnekaiklnetlgtrdeafernLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEE 1767
Cdd:COG1196 328 LEEE----------------------LEELEEELEELEEELEE--AEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1768 MEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLAD 1847
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDYVEDIQTKLppmsEELNNKIDDLSQEIKDRKLAEKVSQAESH---AAQLNDSSAVLDGILDEAKNISFNATAA 1924
Cdd:COG1196 464 LLAELLEEAALLEAAL----AELLEELAEAAARLLLLLEAEADYEGFLEgvkAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1925 FKAY--SNIKDYIDEAEKVAKEA-----KDLAHEATKL---ATGPRGLLKEDAKGSLQKSFRILNEAKKLANDVKENEDH 1994
Cdd:COG1196 540 LEAAlaAALQNIVVEDDEVAAAAieylkAAKAGRATFLpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1995 LNGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKE-----LHQNLDGLKKNY 2069
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEelaerLAEEELELEEAL 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2070 DKLADSVAKTNAVVKDPSKNKIIADADAtvKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALE--EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1987-2145 |
3.07e-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: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1987 DVKENEDHLNGLKTRIENADARngdlLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANdtakdvlAQIKELHQNLDGLK 2066
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQ-------AEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2067 KNYDKLADSVAKTNAVV---------KDPS---------------KNKIIADADATVKNLEQEADRLIDKLKPIKELEDN 2122
Cdd:COG3883 86 EELGERARALYRSGGSVsyldvllgsESFSdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180
....*....|....*....|...
gi 1622930585 2123 LKKNISEIKELINQARKQANSIK 2145
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLS 188
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1612-1955 |
3.15e-05 |
|
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: 48.92 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSpqrAPERLIQLAEGNLNTLVTEMNELL--TRATKVTADGEQTGQDAertntraKSLGEFIkelarDA 1689
Cdd:pfam04108 47 LEKVREGLEKVLN---ELKKDFKQLLKDLDAALERLEETLdkLRNTPVEPALPPGEEKQ-------KTLLDFI-----DE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1690 EAVNekaiKLNETLGTRDEAFERNLEGLQKEIDQMIKELRrknlETQKEIaeDELVAAEGLLKKVKKLFGEsrgkNEEME 1769
Cdd:pfam04108 112 DSVE----ILRDALKELIDELQAAQESLDSDLKRFDDDLR----DLQKEL--ESLSSPSESISLIPTLLKE----LESLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1770 KDLREKLadykNKVDDAWDLLREATnKIREANR--LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLAD 1847
Cdd:pfam04108 178 EEMASLL----ESLTNHYDQCVTAV-KLTEGGRaeMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLID 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1848 EINSIIDYVEDIQTKLPpmseELNNKIDDLSQEIKDRKLAekvsqAESHAAQLNDSSAVLDGILDeaknisfnataafkA 1927
Cdd:pfam04108 253 ELLSALQLIAEIQSRLP----EYLAALKEFEERWEEEKET-----IEDYLSELEDLREFYEGFPS--------------A 309
|
330 340 350
....*....|....*....|....*....|....*
gi 1622930585 1928 YsniKDYIDEA-------EKVAKEAKDLAHEATKL 1955
Cdd:pfam04108 310 Y---GSLLLEVerrrewaEKMKKILRKLAEELDRL 341
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1744-2108 |
3.41e-05 |
|
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: 48.92 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1744 LVAAEGLLKKVKKLFGESRGKNEEMEKdLREKLADYKNKVDDAWDLLReatNKIREANRLFAVNQKNMTALEKKKEAVES 1823
Cdd:pfam04108 2 LSSAQDLCRWANELLTDARSLLEELVV-LLAKIAFLRRGLSVQLANLE---KVREGLEKVLNELKKDFKQLLKDLDAALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1824 GKRQIENTLKEgndILDEANRLADEIN--SIIDYV-----EDIQTKLPPMSEELNNKIDDLSQEIKdrklaekvsqaesh 1896
Cdd:pfam04108 78 RLEETLDKLRN---TPVEPALPPGEEKqkTLLDFIdedsvEILRDALKELIDELQAAQESLDSDLK-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1897 aaQLNDSSAVLDGILDEAKNISfnataafKAYSNIKDYIDEAEKVAKEAKDLA-----H-----EATKLATGPRGLLKED 1966
Cdd:pfam04108 141 --RFDDDLRDLQKELESLSSPS-------ESISLIPTLLKELESLEEEMASLLesltnHydqcvTAVKLTEGGRAEMLEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1967 AKGSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIPndtaAKLQAVKDKARQAND 2046
Cdd:pfam04108 212 LENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYL----AALKEFEERWEEEKE 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2047 TAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVvkDPSKNKIIADADATVKNLeQEADR 2108
Cdd:pfam04108 288 TIEDYLSELEDLREFYEGFPSAYGSLLLEVERRREW--AEKMKKILRKLAEELDRL-QEEER 346
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1631-1915 |
3.50e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1631 RLIQLAEGNLNTLVTEMNElltratkVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAI--KLNETLGTRD- 1707
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNE-------INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKs 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1708 ----EAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEgllkKVKKLFGESRgkneeMEKDLREKLADYKNKV 1783
Cdd:PRK01156 468 nhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE----EINKSINEYN-----KIESARADLEDIKIKI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1784 D---DAWDLLREATNKIREANrLFAVNQKNMTALekKKEAVESGKrQIENTLKEGNDILDEANRLADEINSIIDYVEDIQ 1860
Cdd:PRK01156 539 NelkDKHDKYEEIKNRYKSLK-LEDLDSKRTSWL--NALAVISLI-DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1861 TKLPP----MSEELNN--------------------KIDDLSQEIKDRKLAEKvSQAE--SHAAQLNDSSAVLDGILDEA 1914
Cdd:PRK01156 615 SYIDKsireIENEANNlnnkyneiqenkilieklrgKIDNYKKQIAEIDSIIP-DLKEitSRINDIEDNLKKSRKALDDA 693
|
.
gi 1622930585 1915 K 1915
Cdd:PRK01156 694 K 694
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1971-2133 |
3.97e-05 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 48.88 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1971 LQKSFrilNEAKKLAndvKENEDHLNGLKTRIEnADARNGDLLRA----LNDTLGKLSAIPNDTAAKLQAVKDKARQAND 2046
Cdd:cd08915 75 IEQSF---KELSKLR---QNVEELLQECEELLE-EEAAEDDQLRAkfgtLRWRRPSSDEAAKELYEKVTKLRGYLEQASN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2047 TAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNaVVKDPSKNKIIADADAT---VKNLEQEADRLIDKLKpIKELEDN- 2122
Cdd:cd08915 148 SDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLlneVSELEKERERFISELE-IKSRNNDi 225
|
170
....*....|.
gi 1622930585 2123 LKKNISEIKEL 2133
Cdd:cd08915 226 LPKLITEYKKN 236
|
|
| YkaA |
COG1392 |
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ... |
1769-1954 |
4.34e-05 |
|
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ion transport and metabolism];
Pssm-ID: 441002 [Multi-domain] Cd Length: 205 Bit Score: 47.18 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1769 EKDLREKLADYKNKVDDAWDLLREATNKIREANRLfavnQKNMTALEKKKEAVesgKRQIENTLKEG-------NDILde 1841
Cdd:COG1392 5 EKSFFDLLEEHAEKVVEAAELLVELLEDYEDVEEL----AEEIKELEHEADEI---KREIREELNKTfitpfdrEDIL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1842 anRLADEINSIIDYVEDIqtklppmSEELNN-KIDDLSQEIkdRKLAEKVSQAeshAAQLNDSSAVLDGILDEAKnisfn 1920
Cdd:COG1392 76 --ELASALDDIADYIEDI-------AGRLVLyKIEELDEEL--LELAELLVEA---AEELVEAVKELRELLKKAE----- 136
|
170 180 190
....*....|....*....|....*....|....
gi 1622930585 1921 ataafkaysNIKDYIDEAEKVAKEAKDLAHEATK 1954
Cdd:COG1392 137 ---------EVLELIIEINRLENEADDLYREALA 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1806 |
5.23e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRaksLGEFIKELARDAEA 1691
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR---LEGLEVRIDNLQER 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1692 VNEKAIKLNETLGTRDEAFERNLEGLQKEIDQM---IKELRRKNLEtqkeiAEDElvaaeglLKKVKKLFGEsrgKNEEM 1768
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLenkIKELGPVNLA-----AIEE-------YEELKERYDF---LTAQK 1009
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622930585 1769 EkDL---REKLADYKNKVDD-AWDLLREATNKIREA-NRLFAV 1806
Cdd:TIGR02168 1010 E-DLteaKETLEEAIEEIDReARERFKDTFDQVNENfQRVFPK 1051
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1639-1913 |
6.30e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 47.67 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1639 NLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQ 1718
Cdd:smart00283 19 ELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV----EELEESSDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1719 kEIDQMIKEL-RRKNL-------------ETQKEIAedeLVAAEgllkkVKKLFGESRgkneemekdlrekladyknkvd 1784
Cdd:smart00283 95 -EIVSVIDDIaDQTNLlalnaaieaaragEAGRGFA---VVADE-----VRKLAERSA---------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1785 dawdllrEATNKIRE-ANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKl 1863
Cdd:smart00283 144 -------ESAKEIESlIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAG- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622930585 1864 ppmSEELN---NKIDDLSQEIKDrkLAEKVSQAeshAAQLNDSSAVLDGILDE 1913
Cdd:smart00283 216 ---SEEVNaaiDEIAQVTQETAA--MSEEISAA---AEELSGLAEELDELVER 260
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1683-2060 |
8.45e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.10 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1683 KELARDAEAvnEKAIKLNETLGTRD--EAFERNLEGLQKEIDQMIKELRRKNL---ETQKEIAEDELVAAEGLLKKVK-- 1755
Cdd:pfam05701 55 KKQSEAAEA--AKAQVLEELESTKRliEELKLNLERAQTEEAQAKQDSELAKLrveEMEQGIADEASVAAKAQLEVAKar 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1756 --KLFGESRGKNEEMEkDLREKLADYKNKVDDAWDLLREATNKIREANR--------LFAVNQK-------NMTALEKKK 1818
Cdd:pfam05701 133 haAAVAELKSVKEELE-SLRKEYASLVSERDIAIKRAEEAVSASKEIEKtveeltieLIATKESlesahaaHLEAEEHRI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1819 EAV---ESGKRQIENTLKEGNdilDEANRLADEINSiidyVEDIQTKLPPMSE-------ELNNKIDDLSQEIKDRKLAE 1888
Cdd:pfam05701 212 GAAlarEQDKLNWEKELKQAE---EELQRLNQQLLS----AKDLKSKLETASAllldlkaELAAYMESKLKEEADGEGNE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1889 KVSQAESHAA------QLNDSSAVLDGILDEAKNISFNATA---------------------AFKAYSNIKDYID----E 1937
Cdd:pfam05701 285 KKTSTSIQAAlasakkELEEVKANIEKAKDEVNCLRVAAASlrselekekaelaslrqregmASIAVSSLEAELNrtksE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1938 AEKVAKEAKDLAHEATKLAtgprgllkedakGSLQKSFRILNEAKKLANDVKEnedHLNGLKTRIENADArngdllraln 2017
Cdd:pfam05701 365 IALVQAKEKEAREKMVELP------------KQLQQAAQEAEEAKSLAQAARE---ELRKAKEEAEQAKA---------- 419
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622930585 2018 dtlgKLSAIpndtAAKLQAVKDKARQANDTAKDVLAQIKELHQ 2060
Cdd:pfam05701 420 ----AASTV----ESRLEAVLKEIEAAKASEKLALAAIKALQE 454
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
1813-1916 |
1.15e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 43.75 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1813 ALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEInsiidyVEDIQTKlppMSEELNNKIDDLSQEIKDRKlAEKVSQ 1892
Cdd:COG2811 6 VLKEIKEAEEEADEIIEEAKEEREERIAEAREEAEEI------IEQAEEE---AEEEAQERLEEAREEAEAEA-EEIIEE 75
|
90 100
....*....|....*....|....*
gi 1622930585 1893 AESHA-AQLNDSSAVLDGILDEAKN 1916
Cdd:COG2811 76 GEKEAeALKKKAEDKLDKAVELLVE 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1630-1859 |
1.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1630 ERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFI--KELARDAEAVNEKAIKLN------E 1701
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1702 TLGTRDEAFERNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAE-----GLLKKVKKLFGESRGKN--EEME 1769
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIgrlekELEQAEEELDELQDRLEAAEdlarlELRALLEERFAAALGDAveRELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1770 KDLREKLADYKNKVDDAWDLLREAtnkIREANRLFAVNQKNMTA--------LEKKKEAVESG----KRQIENTLKE--G 1835
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDAdleslpeyLALLDRLEEDGlpeyEERFKELLNEnsI 845
|
250 260
....*....|....*....|....
gi 1622930585 1836 NDILDEANRLADEINSIIDYVEDI 1859
Cdd:COG4913 846 EFVADLLSKLRRAIREIKERIDPL 869
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1885-2146 |
1.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1885 KLAEKVSQAESHAAQLNDSSAVLDGILDEaknisfnataafkaysNIKDYIDEAEKVAKEAKDLAHEATKLATGprgllK 1964
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSE----------------QLRKALFELDKLQEELEQLREELEQAREE-----L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1965 EDAKGSLQKS----FRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLSAIpNDTAAKLQAVKDK 2040
Cdd:COG4372 62 EQLEEELEQArselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL-EQQRKQLEAQIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2041 ARQANDTAKdvlAQIKELHQNLDGLKKNYDKLADSVaktnavvkdpsKNKIIADADATVKNLEQEADRLIDKLKPIKELE 2120
Cdd:COG4372 141 LQSEIAERE---EELKELEEQLESLQEELAALEQEL-----------QALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
250 260
....*....|....*....|....*.
gi 1622930585 2121 dnlKKNISEIKELINQARKQANSIKV 2146
Cdd:COG4372 207 ---KLIESLPRELAEELLEAKDSLEA 229
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1707-1842 |
1.75e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 44.22 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1707 DEAFERNLEGLQKeidqmIKELRRKNLETQKEIA---------EDELVAAEGLLKKVKKLFGES---RGKNEEMEK---D 1771
Cdd:pfam12718 10 ENAQERAEELEEK-----VKELEQENLEKEQEIKslthknqqlEEEVEKLEEQLKEAKEKAEESeklKTNNENLTRkiqL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930585 1772 LREKLadyknkvDDAWDLLREATNKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEGNDILDEA 1842
Cdd:pfam12718 85 LEEEL-------EESDKRLKETTEKLRETD-------VKAEHLERKVQALEQERDEWEKKYEELEEKYKEA 141
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1727-1883 |
1.82e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1727 ELRRKNLETQKEIAEDELvaaEGLLKKVKKLFgesrgKNEEMEKDLREKLADYKNKVDDAWDLLREATNKIreanrlfav 1806
Cdd:smart00787 136 EWRMKLLEGLKEGLDENL---EGLKEDYKLLM-----KELELLNSIKPKLRDRKDALEEELRQLKQLEDEL--------- 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1807 NQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEInsiidyvediqtklppmsEELNNKIDDLSQEIKD 1883
Cdd:smart00787 199 EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI------------------EDLTNKKSELNTEIAE 257
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1766-1899 |
2.78e-04 |
|
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: 42.98 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1766 EEMEKD---LREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEntlKEGNDILDEA 1842
Cdd:pfam20492 2 EEAEREkqeLEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLE---ESAEMEAEEK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1843 NRLADEInsiidyvediqtklppmsEELNNKIDDLSQEiKDRKLAEKVS-QAESHAAQ 1899
Cdd:pfam20492 79 EQLEAEL------------------AEAQEEIARLEEE-VERKEEEARRlQEELEEAR 117
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1731-1894 |
2.80e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.02 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1731 KNLETQKEIAEDELVAAEGLLKKVKKLFGESrgkneEME-KDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQK 1809
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKA-----EAEvAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1810 NMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKD-----R 1884
Cdd:pfam00261 79 GRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVvgnnlK 158
|
170
....*....|...
gi 1622930585 1885 KL---AEKVSQAE 1894
Cdd:pfam00261 159 SLeasEEKASERE 171
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
306-330 |
3.34e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.34e-04
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1469-1525 |
3.41e-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: 40.80 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 1469 CACPLISSSNnfsPSCVTEGLddyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1525
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1728-1953 |
4.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1728 LRRKNLETQKEIAEDElvaAEGLLKKVKKlfgESRGKNEEMEKDLREKLADYKNKVDDAwdlLREATNKIREA-NRLfav 1806
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKK---EAEAIKKEALLEAKEEIHKLRNEFEKE---LRERRNELQKLeKRL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1807 NQKNMTaLEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEElnnkiddlsqEIKDRKL 1886
Cdd:PRK12704 92 LQKEEN-LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----------EAKEILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1887 AEKVSQAESHAAQLndssavldgildeaknisfnataafkaysnIKDYIDEAEKVA-KEAKDLAHEAT 1953
Cdd:PRK12704 161 EKVEEEARHEAAVL------------------------------IKEIEEEAKEEAdKKAKEILAQAI 198
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1657-1956 |
4.69e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1657 VTADGEQTGQDAertntrakSLGEFIKELardaeavnEKAIKLNET-------LGT-------------RDEAFERNLE- 1715
Cdd:PHA02562 99 IYCNGKLLDESA--------SSKDFQKYF--------EQMLGMNYKsfkqivvLGTagyvpfmqlsapaRRKLVEDLLDi 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1716 GLQKEIDQMIKELRR------KNLETQKEIAEDELVAAEGLLKKVKKLFGESRGKNEEMEKDLREKLADYKNKVDDAWDl 1789
Cdd:PHA02562 163 SVLSEMDKLNKDKIRelnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTD- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1790 lrEATNKIREANRLFAVNQKNMTALEKKKEAVESGKRqIENTLKEGN-------DILDEANRladeINSIIDYVEDIQTK 1862
Cdd:PHA02562 242 --ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK-VIKMYEKGGvcptctqQISEGPDR----ITKIKDKLKELQHS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1863 LppmsEELNNKIDDLsQEIKDrKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfnaTAAFKAYSNIKDYIDEAEKVA 1942
Cdd:PHA02562 315 L----EKLDTAIDEL-EEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK---AAIEELQAEFVDNAEELAKLQ 385
|
330
....*....|....
gi 1622930585 1943 KEAKDLAHEATKLA 1956
Cdd:PHA02562 386 DELDKIVKTKSELV 399
|
|
| OspD |
pfam03207 |
Borrelia outer surface protein D (OspD); |
1971-2144 |
5.18e-04 |
|
Borrelia outer surface protein D (OspD);
Pssm-ID: 367392 [Multi-domain] Cd Length: 254 Bit Score: 44.45 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1971 LQKSFRILNEAKKLANDVKENEDHLNGLKTRIE--NADARNGDLLRALNDTLGKLSAIPNDTAAKLQAVKDKARQANDTA 2048
Cdd:pfam03207 64 LKQTTNSLKEAKNTTDNLNASNEANKVVEAVINavNLISSAADQVKSATKNMHDLAQMAEIDLEKIKNSSDKAIFASNLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2049 KDVLAQIKELHQNLDGLKKNYDKLADSVAKTnavvkDPSKNKIIADADATV----KNLEQEADRLIDKLKPIKELEDNLK 2124
Cdd:pfam03207 144 KEAYSLTKAAEQNMQKLYKEQQKISESESES-----DYSDSAEIKQAKEAVeiawKATVEAKDKLIDVENTVKETLDKIK 218
|
170 180
....*....|....*....|....*....
gi 1622930585 2125 K---------NISEIKELINQARKQANSI 2144
Cdd:pfam03207 219 TettnntklaDIKEAAELVLQIAKNAKEI 247
|
|
| 22 |
PHA02557 |
prohead core protein; Provisional |
1691-1901 |
5.46e-04 |
|
prohead core protein; Provisional
Pssm-ID: 222874 Cd Length: 271 Bit Score: 44.71 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1691 AVNEKAIKLNET----LGTR-DEAFERNLEGLQKEIDQMIKELRRKNLE--TQKEIAEDELVA--------AEGLLKKVK 1755
Cdd:PHA02557 46 AVKQHAVKLAEShiaeIAEKaEELVEEALEEAVEAIETKLAEDADKYLDhlAKEWLAENKLAVdrgikaelFESFLGGLK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1756 KLFGESrgkN-----------EEMEKDLREKladyKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESg 1824
Cdd:PHA02557 126 ELFVEH---NvvvpeekvdvvAEMEEELDEM----EEELNELFEENVALEEYINEVKREVILSEVTKDLTESQKEKVAS- 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930585 1825 krqientLKEGndiLDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKI--DDLSQEIKDRKlAEKVSQAESHAAQLN 1901
Cdd:PHA02557 198 -------LAEG---LEFSETFSKKLTAIVEMVFKSKDKEQEIIENLDTDAaaLNFEPEAVEEP-AEKEEVSPSMAAYLK 265
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1682-1902 |
6.81e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.86 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELARDAEAVNEKAI-KLNETLGTRDEAfERNLEGLQKEIDQMIKELRRKN--LETQKEIAEDELVAAEGLLKKVKKLf 1758
Cdd:pfam00261 6 IKEELDEAEERLKEAMkKLEEAEKRAEKA-EAEVAALNRRIQLLEEELERTEerLAEALEKLEEAEKAADESERGRKVL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1759 gESRGKNEEmekdlrEKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKE-GND 1837
Cdd:pfam00261 84 -ENRALKDE------EKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVvGNN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1838 I------LDEANRLADEINsiiDYVEDIQTKLPPM------SE----ELNNKIDDLSQEIKDRKLAEKVSQAESHAAqLN 1901
Cdd:pfam00261 157 LksleasEEKASEREDKYE---EQIRFLTEKLKEAetraefAErsvqKLEKEVDRLEDELEAEKEKYKAISEELDQT-LA 232
|
.
gi 1622930585 1902 D 1902
Cdd:pfam00261 233 E 233
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1997-2145 |
7.19e-04 |
|
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: 45.40 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1997 GLKTRIENADARNGDLLRalndtlgKLSAIPNDTAAKLQAVKDKARQANDTAKDVLA---QIKELHQNL----DGLKKNY 2069
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEK-------KLKTIKNELKNKEKELKNLDKNLNKDEEKINNsnnKIKILEQQIkdlnDKLKKNK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2070 DKL----ADSVaKTNAVVKDPSKNKIiadadatvkNLEQEadrlIDKL-KPIKELEDNLKKNISEIKELINQARKQANSI 2144
Cdd:TIGR04523 96 DKInklnSDLS-KINSEIKNDKEQKN---------KLEVE----LNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKY 161
|
.
gi 1622930585 2145 K 2145
Cdd:TIGR04523 162 N 162
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1469-1517 |
9.38e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622930585 1469 CACPLissSNNFSPSCVtegLDDYRCTaCPRGYEGQYCERCAPGYTGSP 1517
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1764-1971 |
1.08e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1764 KNEEMEKDLREKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEAN 1843
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1844 RLA---------------DEINSIIDYVEDIQTklppMSEELNNKIDDLSQEIKD-----RKLAEKVSQAESHAAQLNDS 1903
Cdd:COG4942 111 RALyrlgrqpplalllspEDFLDAVRRLQYLKY----LAPARREQAEELRADLAElaalrAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930585 1904 SAVLDGILDEAKNISFNATAAFKAYSN-IKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGSL 1971
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1645-1843 |
1.27e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1645 TEMNELLTRATKVTADGEQtgqDAERTNTRAKSLGEfikELARDAEAVNEKAIKLNETLGTRDEAfERNLEGLqkEIDQM 1724
Cdd:pfam00261 18 KEAMKKLEEAEKRAEKAEA---EVAALNRRIQLLEE---ELERTEERLAEALEKLEEAEKAADES-ERGRKVL--ENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1725 IKELRRKNLETQ----KEIAED----------ELVAAEGLLKKVKKLFGESRGKNEEMEKDLR----------------- 1773
Cdd:pfam00261 89 KDEEKMEILEAQlkeaKEIAEEadrkyeevarKLVVVEGDLERAEERAELAESKIVELEEELKvvgnnlksleaseekas 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1774 EKLADYKNKVDDAWDLLREATNKIREANRLFAVNQKNMTALEkkkEAVESGKRQIENTLKEGNDILDEAN 1843
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLE---DELEAEKEKYKAISEELDQTLAELN 235
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1825-2093 |
1.47e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1825 KRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNNKIDDLSQEIKDRK---------LAEKVSQAES 1895
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKaeieeltdeLLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1896 HAAQLNDssavldgildeaknisFNaTAAFKAYSNIKDYideaEKVAKEAKDLAHEAT---KLATGPRGLLKEDAKGS-L 1971
Cdd:PHA02562 253 PSAALNK----------------LN-TAAAKIKSKIEQF----QKVIKMYEKGGVCPTctqQISEGPDRITKIKDKLKeL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1972 QKSFRILNEA----KKLANDVKENEDHLNGLKTRIENadaRNGDLLRAlndtlgklsaipNDTAAKLQAVKDKARQANdt 2047
Cdd:PHA02562 312 QHSLEKLDTAidelEEIMDEFNEQSKKLLELKNKIST---NKQSLITL------------VDKAKKVKAAIEELQAEF-- 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930585 2048 aKDVLAQIKELHQNLDGLKKN--------------YDKLADSVAKTnAVVKD--PSKNKIIA 2093
Cdd:PHA02562 375 -VDNAEELAKLQDELDKIVKTkselvkekyhrgivTDLLKDSGIKA-SIIKKyiPYFNKQIN 434
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1790-2085 |
1.47e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 43.38 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1790 LREATNKIREANRLFAVnQKNMTALEKKKEAVESgkrqienTLKEGNDIL------DEANR------------------L 1845
Cdd:pfam13949 6 LREKAEEVRQQGGIERL-EKSLDDLPKLKQRNRE-------ILDEAEKLLdeeeseDEQLRakygtrwtrppsseltatL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1846 ADEINSIIDYVE-------DIQTKLppmsEELNNKIDDLSQEikDRKLAEKVSQAESHAAQLNDSSAV--LDGILDEAKN 1916
Cdd:pfam13949 78 RAEIRKYREILEqasesdsQVRSKF----REHEEDLELLSGP--DEDLEAFLPSSRRAKNSPSVEEQVakLRELLNKLNE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1917 IsfnataafkaysnikdyIDEAEKVAKEAKDLAHeatklatgprgllKEDAKGSLqksfrILNEAKKLANDVKEN--EDH 1994
Cdd:pfam13949 152 L-----------------KREREQLLKDLKEKAR-------------NDDISPKL-----LLEKARLIAPNQEEQlfEEE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1995 L---NGLKTRIENADARNGDLLRALNDTLGKLSAIPNDTAAKlQAVKDKARQANDTAKDVlaqIKELHQNLDGLKKNYDK 2071
Cdd:pfam13949 197 LekyDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEK-QRQREEALQKLENAYDK---YKELVSNLQEGLKFYND 272
|
330
....*....|....
gi 1622930585 2072 LADSVAKTNAVVKD 2085
Cdd:pfam13949 273 LTEILEKLLKKVKD 286
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1969-2146 |
1.61e-03 |
|
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: 43.17 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1969 GSLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRALNDTLGKLsaipNDTAAKLQAVKDKARQANDTA 2048
Cdd:pfam06008 9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKA----TQTLAKAQQVNAESERTLGHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2049 KDVLAQIKELHQNLDGLKKnydkladSVAKTNAVVKDPSKNKIiadadatvKNLEQEADRLIDKL------KPIKELEDN 2122
Cdd:pfam06008 85 KELAEAIKNLIDNIKEINE-------KVATLGENDFALPSSDL--------SRMLAEAQRMLGEIrsrdfgTQLQNAEAE 149
|
170 180
....*....|....*....|....
gi 1622930585 2123 LKknisEIKELINQARKQANSIKV 2146
Cdd:pfam06008 150 LK----AAQDLLSRIQTWFQSPQE 169
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
785-919 |
1.89e-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: 41.52 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 785 CDKCLPGFYGDPTKGTSEDCQPCA-CPLNIPsnnfsPTCHLDRSLGLICdgcpvgytgprceRCAEGYFgqPSVPGGSCQ 863
Cdd:cd13416 35 CEPCLDGVTFSDVVSHTEPCQPCTrCPGLMS-----MRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930585 864 PCQcndnldfsipgSCDSLSGSCLICKPGTTGRyCELCADGYFGDAVDARN-CQPCR 919
Cdd:cd13416 95 PCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDpCLPCT 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1635-1815 |
2.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1635 LAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNL 1714
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1715 EGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEgllkkvkklfgesrgknEEMEKDLREKLADYKNKVDDAWDLLREAT 1794
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEE-----------------LLEEEELLEEEALEELPEPPDLEELEREL 769
|
170 180
....*....|....*....|..
gi 1622930585 1795 NKIREA-NRLFAVnqkNMTALE 1815
Cdd:COG1196 770 ERLEREiEALGPV---NLLAIE 788
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
90-174 |
2.61e-03 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.51 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 90 SSNPNQRHPITNAIDGK-NTWWQSPSIKNGieyhyVTITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVEYKP 165
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSAWSGDDP-----QWIQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 1622930585 166 WQYHAVTDT 174
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| TNFRSF21 |
cd10583 |
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ... |
823-955 |
2.77e-03 |
|
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6); TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.
Pssm-ID: 276909 [Multi-domain] Cd Length: 159 Bit Score: 40.89 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 823 HLDRSLG--LICDGCPVG---------YTGPRCERCAEGYFGQPSVPGGSCQPCQ--CNDNLDFSIPgsCDSLSGSCLIC 889
Cdd:cd10583 4 HVDPATGtqLTCDKCPAGtyvskhcteTSLRECSPCPNGTFTRHENGIEQCHRCRkpCPAPMIEKTP--CTALTDRECTC 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 890 KPGT--TGRYC---ELCADGYF-----GDAVDARnCQPCrcnANGSFSEIcHSQTGQCECRANVQGQRCDKCKPGT 955
Cdd:cd10583 82 PPGTflSNDTCvphSVCPVGWGvrkkgTETEDVR-CKPC---PRGTFSDV-PSSVLKCKTYTDCLGLGLVVIKPGT 152
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1682-1902 |
3.14e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1682 IKELAR---DAEAVNEKAIKLNETLGTRDEAFERNleglqKEIDQMIKELRRKNLETQKEIAE----------DELVA-- 1746
Cdd:pfam13868 8 LRELNSkllAAKCNKERDAQIAEKKRIKAEEKEEE-----RRLDEMMEEERERALEEEEEKEEerkeerkryrQELEEqi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1747 ----AEGLLKKVKKLFgESRGKNEEMEKDLREKLADYKNKVDDAWDLLREatnkIREANRLfavnQKNMTALEKKKEAVE 1822
Cdd:pfam13868 83 eereQKRQEEYEEKLQ-EREQMDEIVERIQEEDQAEAEEKLEKQRQLREE----IDEFNEE----QAEWKELEKEEEREE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1823 sgKRQIENTL--KEGNDILDEANRLAD------EINSIIDYVEDIQTKLppmsEELNNKIDDLSQEIKDRKLAEK-VSQA 1893
Cdd:pfam13868 154 --DERILEYLkeKAEREEEREAEREEIeeekerEIARLRAQQEKAQDEK----AERDELRAKLYQEEQERKERQKeREEA 227
|
....*....
gi 1622930585 1894 ESHAAQLND 1902
Cdd:pfam13868 228 EKKARQRQE 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1585-1805 |
3.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1585 DLARLEQMVMSINLTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEgnlntLVTEMNELLTRAtKVTADGE-- 1662
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-----LEQEIAALLAEA-GVEDEEElr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1663 ---QTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKlnETLGTRDEAFERNLEGLQKEIDQMIKELRRknLETQKEI 1739
Cdd:COG4717 389 aalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAE--LEAELEQ 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 1740 AEDELVAAEGLLKKvkklfgesrgknEEMEKDLREKLADY-KNKVddAWDLLREATNKIRE---------ANRLFA 1805
Cdd:COG4717 465 LEEDGELAELLQEL------------EELKAELRELAEEWaALKL--ALELLEEAREEYREerlppvlerASEYFS 526
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1720-1890 |
3.86e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1720 EIDQMIKelrrkNLETQKEIAEDELVAAEGLLKKVKKLfgesrgkneemEKDLREKLADYKNKVDDAW-DLLREATNKIR 1798
Cdd:PRK00409 517 KLNELIA-----SLEELERELEQKAEEAEALLKEAEKL-----------KEELEEKKEKLQEEEDKLLeEAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1799 EANRLFAVNQKNMTALEKKKEAveSGKRQIentLKEGNDILDEANRLADEInsiidyvediqtKLPPMSEELNNKIDDls 1878
Cdd:PRK00409 581 EAKKEADEIIKELRQLQKGGYA--SVKAHE---LIEARKRLNKANEKKEKK------------KKKQKEKQEELKVGD-- 641
|
170
....*....|..
gi 1622930585 1879 qEIKDRKLAEKV 1890
Cdd:PRK00409 642 -EVKYLSLGQKG 652
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1609-1783 |
3.91e-03 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 41.08 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1609 LYGLENMTQELKHLLSpqrapERLIQLAE-GNLNTLVTEMNELLTRATKVTadgeqtgqDAERTNTRAKSLGEFIKElar 1687
Cdd:pfam12729 27 LYSLKQINDNLDTMYE-----DRLLPIKWlGDIRANLLELRANLLELILTT--------DPAERDELLKDIEELRAE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1688 daeaVNEKAIKLNETLGTRDE-----AFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELvaaegllkkvkklfgesR 1762
Cdd:pfam12729 91 ----IDKLLEKYEKTILTDEEkklfaEFKENLNAYRAVRNKVLELAKAGNKDEAYQLYKTEG-----------------R 149
|
170 180
....*....|....*....|.
gi 1622930585 1763 GKNEEMEKDLrEKLADYKNKV 1783
Cdd:pfam12729 150 PAREAMIEAL-EELVDYNLKV 169
|
|
| SerH |
pfam06873 |
Cell surface immobilization antigen SerH; This family consists of several cell surface ... |
884-1133 |
4.97e-03 |
|
Cell surface immobilization antigen SerH; This family consists of several cell surface immobilization antigen SerH proteins which seem to be specific to Tetrahymena thermophila. The SerH locus of Tetrahymena thermophila is one of several paralogous loci with genes encoding variants of the major cell surface protein known as the immobilization antigen (i-ag).
Pssm-ID: 284327 [Multi-domain] Cd Length: 418 Bit Score: 42.22 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 884 GSCLICKPGT--------TGRYCELCADGYFG--DAvdarNCQPCRCNANGSFSEICHSQTGQcECRANvqGQRCDKCKP 953
Cdd:pfam06873 123 GDCTLCNPSTpaavsdksTCVSCTACSSITSGwtDA----NCNACATTASPKGNNVFANSAGS-ACVAA--SASCGSTSR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 954 GTFGLQSArGCVPCN-----CNSFGSKSFDCEESGQCWCQPGVTGKKCDRCAH-----GYFSFQEGGCTACECSHLGnnc 1023
Cdd:pfam06873 196 GSTAWTDA-DCLACTpatpyASADKSSCVASSCAACSTVTSGWTDSDCNACATtaspaTKNLFANAAGSSCVASSAS--- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1024 dpKTGQCICPPNTIGEKCSKCAPNT------WGHSITTGCKACNCSTVGSLDFQCN--VNTGQCNCHPKF---------- 1085
Cdd:pfam06873 272 --CTTASRGTTAWTDSDCTLCTPSTpaasldASPCVVSSCVACNSITSGWTDANCNscAMTASPSTKNVFanadgsacva 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1086 SGAKCTECSRGH--WNYPRCNLCDcflpGT----------DATTCDSeTKKCSCSDQTGQ 1133
Cdd:pfam06873 350 SSYSCNQTARGSnkWTDADCALCN----GTasnanqyasaDGSSCQS-TKQSSSSTFSGQ 404
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2033-2145 |
6.00e-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: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 2033 KLQAVKDKARQANDTAKDVLAQIKELHQNLDGLKKNYDKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQ-------- 2104
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR--LELEIEEVEARIKKYEEqlgnvrnn 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930585 2105 -EADRL---IDKLKP-IKELED----------NLKKNISEIKELINQARKQANSIK 2145
Cdd:COG1579 89 kEYEALqkeIESLKRrISDLEDeilelmerieELEEELAELEAELAELEAELEEKK 144
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1612-1757 |
6.45e-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: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1612 LENMTQELKHLlspqrapERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTR---AKSLGEF------I 1682
Cdd:COG1579 26 LKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEYealqkeI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1683 KELARDAEAVNEKAIKLNETLGTRDEAF---ERNLEGLQKEIDQMIKELRRKNLETQKEIAE-----DELVAA--EGLLK 1752
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELaelEAELAELEAELEEKKAELDEELAELEAELEEleaerEELAAKipPELLA 178
|
....*
gi 1622930585 1753 KVKKL 1757
Cdd:COG1579 179 LYERI 183
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1676-1899 |
7.08e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1676 KSLGEFIKELARDAE----AVNE-KAIKLNEtlgtrDEafernLEGLQKEIDQM--IKELRRKNLETQKEIAEDElVAAE 1748
Cdd:COG0497 175 EELRADEAERARELDllrfQLEElEAAALQP-----GE-----EEELEEERRRLsnAEKLREALQEALEALSGGE-GGAL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1749 GLLKKVKKLFgesrgknEEMEkDLREKLADYKNKVDDAWDLLREATNKIR------EAN--RLFAVNQKnMTALE--KKK 1818
Cdd:COG0497 244 DLLGQALRAL-------ERLA-EYDPSLAELAERLESALIELEEAASELRryldslEFDpeRLEEVEER-LALLRrlARK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1819 EAVEsgkrqIEntlkegnDILDEANRLADEINSIIDYVEDIqtklppmsEELNNKIDDLSQEIkdRKLAEKVSQAESHAA 1898
Cdd:COG0497 315 YGVT-----VE-------ELLAYAEELRAELAELENSDERL--------EELEAELAEAEAEL--LEAAEKLSAARKKAA 372
|
.
gi 1622930585 1899 Q 1899
Cdd:COG0497 373 K 373
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
886-973 |
8.37e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 39.30 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 886 CLICKPG---------TTGRYCELCADGYFGDAVDARNCQPC-RCNANGSFSEI--C-HSQTGQCECRANVQ-------G 945
Cdd:cd13406 15 CHECPPGegmesrctgTQDTVCSPCEPGFYNEAVNYEPCKPCtQCNQRSGSEEKqkCtKTSDTVCRCRPGTQpldsykpG 94
|
90 100
....*....|....*....|....*....
gi 1622930585 946 QRCDKCKPGTFGLQSARGCVP-CNCNSFG 973
Cdd:cd13406 95 VDCVPCPPGHFSRGDNQACKPwTNCSLAG 123
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
832-1134 |
9.04e-03 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 41.83 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 832 CDGCPVGYTGPRCERCAEGYFG-----------QPSVPGGSCQpCQCNDNLdFSIPGSCDSLSGSCLICKPGT-TGryCE 899
Cdd:PTZ00214 376 CTRCSAGYLGVDGKSCSESCSGdtrgvctkvaeGSESTEVSCR-CVCKPTF-YNSSGTCTPCTDSCAVCKDGTpTG--CQ 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 900 LCADGYFGDAVDARNcQPCRCNANGSFSEIChsqtgqCECRANVQGQR-CDKCK------------PGT----FGLQSAR 962
Cdd:PTZ00214 452 QCSPGKILEFSIVSS-ESADCVDQCSVGSEC------AECGITIDGSRyCTRCKdastypfngvciPNTqrdaYCTSTAN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 963 G-CVPCNCNSF-------------GSKSFDCEESGQC-------WCQPGVTGKKCDRCAHGYFSFQEGGCTACECSHLGN 1021
Cdd:PTZ00214 525 GaCTTCSGAAFlmnggcyttehypGSTICDKQSNGKCtttkkgyGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLK 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1022 NCD-PKTGQCICPPNTI------GEKCSKCAP---NTWGHsiTTGCKACNCSTVGSLDFQcnvntgqcNCHPKFSGAKCT 1091
Cdd:PTZ00214 605 RASgAATGSCVDPGACVdgyyadGDACLPCATpgcKTCGH--ASFCTECAGELFVSLDGQ--------SCLEECTGDKVV 674
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1092 -ECSRGhwnYPRCNLCDCFLPGTD------ATTCDSETKKCSCSDQTGQC 1134
Cdd:PTZ00214 675 gEVSGG---VRRCWCERGFLPALDrsgcvlPTECPPDMPSCAACDESGRC 721
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1811-1944 |
9.20e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.93 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 1811 MTALEKKKEAVesgkrqIENTLKEGNDILDEANRLADEInsiidyVEDIQTKLppmSEELNNKIDDLSQEIKdRKLAEKV 1890
Cdd:COG1390 1 MMSLEKIIEEI------LEEAEAEAEEILEEAEEEAEKI------LEEAEEEA---EEIKEEILEKAEREAE-REKRRII 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930585 1891 SQA--ESHAAQLNDSSAVLDGILDEAKN--ISFNATAAFKAYsnIKDYIDEAEKVAKE 1944
Cdd:COG1390 65 SSAelEARKELLEAKEELIEEVFEEALEklKNLPKDPEYKEL--LKKLLKEAAEELGS 120
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1380-1407 |
9.56e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 9.56e-03
10 20
....*....|....*....|....*...
gi 1622930585 1380 CDCPLGYSGLSCEACLPGFYRLRSQPGG 1407
Cdd:pfam00053 20 CLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| TNFRSF9 |
cd13410 |
Tumor necrosis factor receptor superfamily member 9 (TNFRSF9), also known as CD137; TNFRSF9 ... |
948-1060 |
9.92e-03 |
|
Tumor necrosis factor receptor superfamily member 9 (TNFRSF9), also known as CD137; TNFRSF9 (also known as CD137, ILA, 4-1BB) plays a role in the immunobiology of human cancer where it is preferentially expressed on tumor-reactive subset of tumor-infiltrating lymphocytes. It can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. It transduces signals that lead to the activation of NF-kappaB, mediated by the TRAF adaptor proteins. CD137 contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. CD137 is modulated by SAHA treatment in breast cancer cells, suggesting that the combination of SAHA with this receptor could be a new therapeutic approach for the treatment of tumors.
Pssm-ID: 276915 [Multi-domain] Cd Length: 138 Bit Score: 38.95 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930585 948 CDKCKPGTF-GLQSARGCVPCNCNSFGSKsfdceeSGQCWCQpgvtgkKCDRCAhGYFSFQEggctacECSHLGNncdpk 1026
Cdd:cd13410 6 CSNCPAGTFcGKNKDQTCIPCPPNSFSST------GGQQTCD------ICRKCE-GVFRTKK------PCSSTSN----- 61
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622930585 1027 tGQCICPP--NTIGEKCSKCAPN-TWGHSIT-TGCKAC 1060
Cdd:cd13410 62 -AECECVPgfHCLGPGCSMCEPDcKQGQELTkEGCKDC 98
|
|
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