|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1856-2113 |
4.53e-107 |
|
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: 343.24 E-value: 4.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1856 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1935
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1936 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2015
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2016 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2095
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 2217316812 2096 ADSSLLQTNIALQLMEKS 2113
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.25e-102 |
|
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: 327.78 E-value: 5.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 2217316812 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.09e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 2217316812 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2297-2425 |
2.38e-43 |
|
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: 155.34 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2297 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2367
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2368 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2425
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1527-1661 |
1.44e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1527 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1604
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316812 1605 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1661
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1523-1650 |
9.00e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1523 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1602
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 1603 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1650
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3003-3143 |
4.08e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3003 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3080
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316812 3081 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3143
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3020-3145 |
7.24e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3020 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3096
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 3097 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3145
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2611-2751 |
2.34e-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: 104.42 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2611 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2687
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2688 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2630-2751 |
2.32e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2630 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2706
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 2707 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3027-3145 |
1.16e-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: 92.87 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3027 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3103
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217316812 3104 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3145
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2778-2910 |
1.17e-20 |
|
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: 90.94 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2778 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2854
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 2855 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2910
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3167-3255 |
2.99e-16 |
|
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: 78.23 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3167 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3245
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90
....*....|
gi 2217316812 3246 CDGQWHSVAA 3255
Cdd:cd00110 78 NDGQWHSVSV 87
|
|
| LamG |
smart00282 |
Laminin G domain; |
2803-2912 |
4.74e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2803 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2878
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217316812 2879 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2912
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1275-1323 |
8.19e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.54 E-value: 8.19e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1275 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1323
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2637-2751 |
5.25e-15 |
|
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: 73.99 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2637 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2715
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2217316812 2716 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1847-2350 |
2.99e-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: 79.29 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1908
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1909 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1978
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1979 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2054
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2055 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2134
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2135 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2213
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2214 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2287
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2288 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2348
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 2217316812 2349 NK 2350
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1274-1316 |
3.13e-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: 69.31 E-value: 3.13e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 1274 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1316
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1275-1316 |
1.27e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.27e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217316812 1275 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1316
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3195-3253 |
3.38e-12 |
|
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: 65.90 E-value: 3.38e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316812 3195 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSV 3253
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSV 58
|
|
| LamG |
smart00282 |
Laminin G domain; |
3190-3254 |
3.72e-12 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 66.21 E-value: 3.72e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316812 3190 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVA 3254
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVA 65
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1365-1416 |
5.10e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 5.10e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1416
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
6.11e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 6.11e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
8.51e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 8.51e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1365-1410 |
9.67e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 9.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1410
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1365-1411 |
1.93e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.93e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1411
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2444-2579 |
2.05e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2444 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2517
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 2518 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2579
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1413-1463 |
2.13e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1413 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1463
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1695-1741 |
2.47e-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: 60.83 E-value: 2.47e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1695 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1741
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.53e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1838-2172 |
6.48e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1838 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1916
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1988
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1989 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2057
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2058 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2131
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217316812 2132 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2172
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1743-1793 |
7.49e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1743 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1793
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2399-2577 |
8.20e-11 |
|
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: 62.82 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2399 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2478
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2479 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2552
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 2217316812 2553 PPDFKLPSRLSFPPYKGCIELDDLN 2577
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1414-1462 |
1.21e-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: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1414 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1462
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.47e-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: 1.47e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217316812 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.81e-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: 58.52 E-value: 1.81e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.87e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 2.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217316812 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
6.34e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 6.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1742-1794 |
6.80e-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: 6.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 1742 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1794
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.22e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1696-1743 |
1.38e-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: 55.82 E-value: 1.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1696 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1743
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1414-1456 |
2.01e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.01e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 1414 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1456
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1743-1786 |
2.33e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 1743 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1786
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.93e-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: 4.93e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2806-2910 |
7.19e-09 |
|
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: 56.27 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2806 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2880
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217316812 2881 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2910
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.67e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1696-1738 |
2.69e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 1696 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1738
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. |
631-681 |
5.02e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 5.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
5.04e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 5.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1865-2361 |
7.83e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1865 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1943
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1944 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2023
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2024 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2103
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2104 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2159
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2160 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2239
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2240 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2319
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217316812 2320 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2361
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.27e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.27e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217316812 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.15e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2066-2384 |
1.37e-06 |
|
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: 54.19 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2066 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2145
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2146 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2225
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2226 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2302
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2303 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2378
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 2217316812 2379 MDRIRE 2384
Cdd:COG5185 529 FMRARG 534
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1980-2252 |
4.87e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1980 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2055
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2056 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2124
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2125 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2196
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316812 2197 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2252
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
7.09e-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: 45.42 E-value: 7.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.71e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 7.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.14e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1865-2396 |
2.06e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1865 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1944
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1945 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2024
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2025 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2088
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2089 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2161
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2162 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2223
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2224 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2296
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2297 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2364
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 2217316812 2365 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2396
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1847-2384 |
2.39e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1916
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1995
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1996 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2067
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2068 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2138
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2139 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2217
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2218 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2295
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2296 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2375
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 2217316812 2376 SDNMDRIRE 2384
Cdd:PRK02224 697 RERREALEN 705
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2101-2265 |
4.23e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.55 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2101 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2178
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2179 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2253
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 2217316812 2254 LNNLQQTLNIVT 2265
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2446-2572 |
5.55e-05 |
|
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: 45.10 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2446 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2521
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 2522 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2572
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 5.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.32e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.51e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
7.15e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217316812 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
7.23e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 7.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217316812 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.41e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1674-1797 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1674 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1749
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 1750 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1797
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1867-2185 |
5.76e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1867 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1943
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1944 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2010
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2011 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2082
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2083 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2156
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217316812 2157 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2185
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2100-2196 |
6.21e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2100 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2173
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 2217316812 2174 GDELvrcavdaATAYENILNAIK 2196
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1856-2113 |
4.53e-107 |
|
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: 343.24 E-value: 4.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1856 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1935
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1936 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2015
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2016 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2095
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 2217316812 2096 ADSSLLQTNIALQLMEKS 2113
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.25e-102 |
|
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: 327.78 E-value: 5.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 2217316812 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.09e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 2217316812 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2297-2425 |
2.38e-43 |
|
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: 155.34 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2297 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2367
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2368 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2425
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1527-1661 |
1.44e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1527 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1604
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316812 1605 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1661
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1523-1650 |
9.00e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1523 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1602
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 1603 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1650
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3003-3143 |
4.08e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3003 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3080
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316812 3081 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3143
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3020-3145 |
7.24e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3020 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3096
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 3097 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3145
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2611-2751 |
2.34e-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: 104.42 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2611 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2687
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2688 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2630-2751 |
2.32e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2630 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2706
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 2707 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3027-3145 |
1.16e-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: 92.87 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3027 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3103
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217316812 3104 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3145
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2778-2910 |
1.17e-20 |
|
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: 90.94 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2778 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2854
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 2855 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2910
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3027-3147 |
3.40e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3027 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3102
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 3103 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3147
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3167-3255 |
2.99e-16 |
|
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: 78.23 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3167 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3245
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90
....*....|
gi 2217316812 3246 CDGQWHSVAA 3255
Cdd:cd00110 78 NDGQWHSVSV 87
|
|
| LamG |
smart00282 |
Laminin G domain; |
2803-2912 |
4.74e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2803 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2878
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217316812 2879 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2912
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1275-1323 |
8.19e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.54 E-value: 8.19e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1275 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1323
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2637-2751 |
5.25e-15 |
|
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: 73.99 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2637 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2715
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2217316812 2716 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2751
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1847-2350 |
2.99e-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: 79.29 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1908
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1909 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1978
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1979 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2054
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2055 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2134
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2135 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2213
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2214 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2287
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2288 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2348
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 2217316812 2349 NK 2350
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1274-1316 |
3.13e-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: 69.31 E-value: 3.13e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 1274 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1316
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1844-2295 |
3.28e-13 |
|
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: 76.31 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1844 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVns 1922
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1923 rkaqtlnnnvnraTQSAKELDVKIKNVIRNVHILLKQISgTDGEGNNvpsgdfsREWAE-------AQRMMRELRNRNFG 1995
Cdd:pfam15921 369 -------------SQESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1996 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGL 2064
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2065 NQENERALGAIQRQVKEINS---LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2141
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2142 AG-----KTSLVEEAEKHARSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2197
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2198 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTT 2277
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMK 727
|
490 500
....*....|....*....|.
gi 2217316812 2278 LRDGLHG---IQRGDIDAMIS 2295
Cdd:pfam15921 728 VAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1275-1316 |
1.27e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.27e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217316812 1275 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1316
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3195-3253 |
3.38e-12 |
|
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: 65.90 E-value: 3.38e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316812 3195 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSV 3253
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSV 58
|
|
| LamG |
smart00282 |
Laminin G domain; |
3190-3254 |
3.72e-12 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 66.21 E-value: 3.72e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316812 3190 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVA 3254
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVA 65
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1365-1416 |
5.10e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 5.10e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1416
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
6.11e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 6.11e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
8.51e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 8.51e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1365-1410 |
9.67e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 9.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1410
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1845-2387 |
1.33e-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: 70.82 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1845 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1924
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1925 AQTLNNNVNRatqSAKELDVKIKNVIRN-VHI--LLKQISGTDGEGNNVpSGDFSREWAEAQRMMRELRNRNFGKHLREA 2001
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLeVELnkLEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2002 EADKRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKE 2081
Cdd:TIGR04523 174 ELNLLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2082 INSLQSDF----TKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktS 2146
Cdd:TIGR04523 241 INEKTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2147 LVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaedaANRAASASE-SALQTVIKEDLpRKA 2225
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK-----KELTNSESEnSEKQRELEEKQ-NEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2226 KTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLRdglhgIQRGDIDAMISSAKSMVRKAN 2305
Cdd:TIGR04523 373 EKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ-----QEKELLEKEIERLKETIIKNN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2306 DITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL--------GNISD 2377
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleEKVKD 514
|
570
....*....|
gi 2217316812 2378 NMDRIRELIQ 2387
Cdd:TIGR04523 515 LTKKISSLKE 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1365-1411 |
1.93e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.93e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1365 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1411
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2444-2579 |
2.05e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2444 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2517
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 2518 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2579
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1413-1463 |
2.13e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1413 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1463
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1695-1741 |
2.47e-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: 60.83 E-value: 2.47e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1695 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1741
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1880-2168 |
2.78e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1880 RNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK---AQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHIL 1956
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1957 LKQISGTDGEgnnvpsgdfsrewAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIrtwqkthqgenNGLANSIRDS 2036
Cdd:TIGR02168 749 IAQLSKELTE-------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2037 LNEYEAKLSDLRARLQEAAAQAKQA-----------NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2105
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLerriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 2106 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2168
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1840-2396 |
3.38e-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: 69.28 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1840 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIE---GLERELTDLNQEFETLQE 1916
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRKAQTLNNNVNRATQ----------------SAKELDV-KIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREW 1979
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlSEKQKELeQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1980 AEaqrmmrELRNRNfgKHLREAEADKRESQLLLNR-------IRTWQKTHQGENNglanSIRDSLNEYEAKLSDLrarlq 2052
Cdd:TIGR04523 313 KS------ELKNQE--KKLEEIQNQISQNNKIISQlneqisqLKKELTNSESENS----EKQRELEEKQNEIEKL----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2053 eaaaqakqanglNQENERALGAIQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQE 2130
Cdd:TIGR04523 376 ------------KKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2131 LSDKVRElsrsagKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASE 2210
Cdd:TIGR04523 442 IKDLTNQ------DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2211 SALQTVIKE---------DLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV--IDTNLTTLR 2279
Cdd:TIGR04523 496 KELKKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIdeKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2280 DglhgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIkdtygrtqnEDFKKALTDADNSVNKLTNKLPDLW 2359
Cdd:TIGR04523 575 Q--------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---------SSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2217316812 2360 RKIESINQQllpLGNISDNMDRIR----ELIQQARDAASKV 2396
Cdd:TIGR04523 638 SKKNKLKQE---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.53e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1838-2172 |
6.48e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1838 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1916
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1988
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1989 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2057
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2058 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2131
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217316812 2132 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2172
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1743-1793 |
7.49e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1743 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1793
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2399-2577 |
8.20e-11 |
|
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: 62.82 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2399 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2478
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2479 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2552
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 2217316812 2553 PPDFKLPSRLSFPPYKGCIELDDLN 2577
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1414-1462 |
1.21e-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: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217316812 1414 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1462
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.47e-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: 1.47e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217316812 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.81e-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: 58.52 E-value: 1.81e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.87e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 2.87e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217316812 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
6.34e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 6.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1742-1794 |
6.80e-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: 6.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 1742 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1794
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.22e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1696-1743 |
1.38e-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: 55.82 E-value: 1.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1696 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1743
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1838-2385 |
1.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1838 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1917
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1918 AQVNSRKAQTLNNNVNRATQ---SAKELDVKIKNVIRNVHILLK---QISGTDG---EGNNVPSGdFSR--EWAEAQRM- 1985
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEG-YEAaiEAALGGRLq 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1986 MRELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQE 2053
Cdd:TIGR02168 549 AVVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2054 AAAQAKQANGLNQENERAL------------GAIQRQ-VKEINSLQS------DFTKYLTTADSSLLQTNIALQLMEKSQ 2114
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRivtldgdlvrpgGVITGGsAKTNSSILErrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2115 KEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAA 2185
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIE 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2186 TAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EV 2250
Cdd:TIGR02168 786 ELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2251 SPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVE 2323
Cdd:TIGR02168 858 AAEIEELEELieeleseLEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217316812 2324 RIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2385
Cdd:TIGR02168 933 GLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1414-1456 |
2.01e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.01e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217316812 1414 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1456
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1743-1786 |
2.33e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 1743 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1786
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1847-2194 |
3.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1926
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1927 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEgnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEAD-K 2005
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----------LEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2006 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAAqakqangLNQENERALGAIQRQVKEINSL 2085
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLER-------LEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2086 QSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSdkvRELSRSAGKTSLVEEAEKHARSLQELAKQL 2165
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340
....*....|....*....|....*....
gi 2217316812 2166 EEIKRNASGDELVRCAVDAATAYENILNA 2194
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.93e-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: 4.93e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2806-2910 |
7.19e-09 |
|
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: 56.27 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2806 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2880
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217316812 2881 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2910
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1865-2163 |
1.47e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1865 LLEQMRHMETQAKDLRNQLlnyrSAISNHgskIEGLERELTDLNQEFETLQEK-AQVNSRKAQTLNNNVNRATQSAKELD 1943
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL----ASLEEE---LEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1944 VKIKNVIRNVHILLKQISGTDGEGNNVPSgDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL--LLNRIRTWQKT 2021
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2022 HQgennglanSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL- 2100
Cdd:TIGR02169 380 FA--------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIk 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2101 -----LQTNIALqlMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2163
Cdd:TIGR02169 452 kqewkLEQLAAD--LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1862-2391 |
1.47e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.96 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1862 SAGLLEQMRHMETQAKDLRNQLLNYRSAIS-------NHGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLNNNVN 1933
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQklqlekvTTEAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1934 RATQSAKELDvKIKN----VIRNVHILLKQISGT-----------DGEgnnvpSGDFSREWAEAQRMMRELRnrnfgkhl 1998
Cdd:pfam01576 170 EEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1999 reAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARLqeaaaqakqanglnqENERALGAIQ 2076
Cdd:pfam01576 236 --AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDL---------------ESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2077 RQVK-----EINSLQsdfTKYLTTADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2151
Cdd:pfam01576 291 EKQRrdlgeELEALK---TELEDTLDT----TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2152 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2221
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2222 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTVQKEVIDTNLTTLRDGLHGIQrgdidamis 2295
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2296 saksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2375
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 2217316812 2376 SDNMDRIRELIQQARD 2391
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1977-2398 |
1.62e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1977 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaa 2056
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2057 qakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2136
Cdd:COG4717 156 ---------EELRELEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2137 ELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2200
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2201 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnltt 2277
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2278 LRDGLHGIQRGDIDAMISSAK------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKL 2351
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2217316812 2352 TNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2398
Cdd:COG4717 452 REEL----AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.67e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1696-1738 |
2.69e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 1696 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1738
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. |
631-681 |
5.02e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 5.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
5.04e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 5.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2217316812 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2635-2751 |
5.27e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2635 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2703
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2704 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2751
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1865-2361 |
7.83e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1865 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1943
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1944 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2023
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2024 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2103
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2104 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2159
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2160 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2239
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2240 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2319
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217316812 2320 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2361
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1847-2363 |
1.04e-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: 58.13 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1925
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1926 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnNVPSGDFSREWAEAQR----MMRElRNRNFGKHLREA 2001
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG-------YFPNKKQLEDWLHSKSkeinQTRD-RLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2002 EADKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQEN 2068
Cdd:TIGR00606 604 EQNK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDEN 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2069 ERALGAIQRQVK---EINSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT 2145
Cdd:TIGR00606 677 QSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2146 -SLVEEAEKHARSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRK 2224
Cdd:TIGR00606 754 qKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2225 AKTLSSNSDKLLNEAKMTQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSM 2300
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSL 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316812 2301 VRKANDITDEVLDGLNPIQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2363
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1850-2189 |
1.72e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1850 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN 1929
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1930 NNVNRATQSAKELDvkiknvirnvhillKQISGTDGEGNNVPSgdfSREWAEAQR-MMRELRNRNFGKhLREAEADKRES 2008
Cdd:PRK02224 377 EAVEDRREEIEELE--------------EEIEELRERFGDAPV---DLGNAEDFLeELREERDELRER-EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2009 QlllNRIRtwqkthqgENNGL--------------ANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--L 2072
Cdd:PRK02224 439 R---ERVE--------EAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2073 GAIQRQVKEINSLQSDFTKYLTTADSSllqtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAE 2152
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRET---------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAE 568
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217316812 2153 KHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYE 2189
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1847-2183 |
2.39e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1926
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1927 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVpsgdfsreWAEAQRMMRELRNRNFGKHLREAEADKR 2006
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--------EQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2007 ESQL--LLNRIRTWQKTHQGENNGLANSIRDSLnEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS 2084
Cdd:COG4372 156 EEQLesLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2085 LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQ 2164
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|....*....
gi 2217316812 2165 LEEIKRNASGDELVRCAVD 2183
Cdd:COG4372 315 DALLAALLELAKKLELALA 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1847-2174 |
4.23e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSAS-AGLLEQMRHMEtqakdlrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1925
Cdd:TIGR02169 674 AELQRLRERLEGLKRElSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1926 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQIsgtdgegnNVPSGDFSRE-WAEAQRMMREL---RNRNFG------ 1995
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--------NDLEARLSHSrIPEIQAELSKLeeeVSRIEArlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1996 -----KHLREAEADKrESQLLLNRIRTWQ------KTHQGENNGLANSIRDSLNEYEAKLSDLRARLQeaaaqakqanGL 2064
Cdd:TIGR02169 819 qklnrLTLEKEYLEK-EIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLG----------DL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2065 NQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-------- 2133
Cdd:TIGR02169 888 KKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqael 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2217316812 2134 -KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2174
Cdd:TIGR02169 961 qRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1847-2167 |
4.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNhgskiegLERELTDLNQEFETLQEKAQvnsrKAQ 1926
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIK----ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1927 TLNNNVNRATQSAKELDVKIkNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNfgKHLRE------ 2000
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEeiskit 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2001 ---AEADKRESQLLLNRI-------------RTWQKTHQGEnnglansirdSLNEYEAKLSDLRARLQEAaaqakqangl 2064
Cdd:PRK03918 412 ariGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKE----------LLEEYTAELKRIEKELKEI---------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2065 nQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLNEARQELSDKVREL 2138
Cdd:PRK03918 472 -EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350
....*....|....*....|....*....|...
gi 2217316812 2139 SRSAG----KTSLVEEAEKHARSLQELAKQLEE 2167
Cdd:PRK03918 549 EKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.27e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.27e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217316812 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1957-2170 |
5.34e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1957 LKQISGTDgegnnvpsgDFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2034
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2035 DSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTTADSSLLQTNIA-LQLMEKS 2113
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 2114 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2170
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRleeeINGIEERIKELEEKEERLEELKKKLKELEK 352
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.15e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217316812 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
3009-3147 |
1.15e-06 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3009 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3082
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217316812 3083 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3147
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2066-2384 |
1.37e-06 |
|
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: 54.19 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2066 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2145
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2146 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2225
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2226 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2302
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2303 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2378
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 2217316812 2379 MDRIRE 2384
Cdd:COG5185 529 FMRARG 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1808-2262 |
2.44e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1808 HPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRN 1881
Cdd:TIGR00618 279 LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1882 QLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA-TQSAKELDVKIKNVIRNVHILLKQI 1960
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1961 SGTDGE--GNNVPSGDFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANS 2032
Cdd:TIGR00618 439 YAELCAaaITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2033 IRdslnEYEAKLSDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQ 2102
Cdd:TIGR00618 510 CI----HPNPARQDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2103 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LV 2178
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2179 RCAVDAATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQ 2258
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
....
gi 2217316812 2259 QTLN 2262
Cdd:TIGR00618 743 QSLK 746
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1980-2252 |
4.87e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1980 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2055
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2056 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2124
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2125 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2196
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316812 2197 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2252
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1846-2251 |
6.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1846 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSAISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrkA 1925
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ-----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1926 QTLNNNVNRATQSAKELDVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEADK 2005
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2006 RESQLLLNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGAIQR 2077
Cdd:COG4717 185 QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2078 QVKEINSLQSDFTKYLTTAdSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-KVRELSRSAG-----KTSLVEEA 2151
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLV-LGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGlppdlSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2152 EKHARSLQELAKQLEEIKR------------------NASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESAL 2213
Cdd:COG4717 343 LDRIEELQELLREAEELEEelqleeleqeiaallaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2217316812 2214 QTVIKEDLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEVS 2251
Cdd:COG4717 423 EALDEEELEEELEELEEELEELeeeLEELREELAELEAELE 463
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
7.09e-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: 45.42 E-value: 7.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.71e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 7.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.14e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1867-2177 |
1.29e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1867 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLNNNVNRATQSA 1939
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1940 KELDVKIKNVIRNVHILLKQISGTDGEGNNVPS--------------GDFSREW-----AEAQRMMRELRNRnfgKHLRE 2000
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtEVLSPEEekelvEKIKELEKELEKA---KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2001 AEADKREsqlLLNRIRTWQKthqgenngLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneralgaIQRQVK 2080
Cdd:COG1340 158 KNEKLKE---LRAELKELRK--------EAEEIHKKIKELAEEAQELHEEMIE----------LYKE-------ADELRK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2081 EINSLQSDFTKYLTTADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHARSLqe 2160
Cdd:COG1340 210 EADELHKEIVEAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAEEI-- 272
|
330
....*....|....*....
gi 2217316812 2161 lakqLEEIKRNA--SGDEL 2177
Cdd:COG1340 273 ----FEKLKKGEklTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1918-2285 |
1.41e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1918 AQVNSRKAQTLNNnVNRATQSAKELDVKIKNVIRNVHILLKQisgtdgegnnvpsgdfsREWAEA-QRMMRELRNRNFGK 1996
Cdd:TIGR02169 166 AEFDRKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRRE-----------------REKAERyQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1997 HLREAEADKRESQLLLNRIrtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGA 2074
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL---------------ASLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2075 iqrqvKEINSLQSDFTKylTTADSSLLQTNIAL--QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE- 2150
Cdd:TIGR02169 287 -----EEQLRVKEKIGE--LEAEIASLERSIAEkeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2151 -----------------AEKHARSLQELAK----------QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDA 2201
Cdd:TIGR02169 360 aelkeeledlraeleevDKEFAETRDELKDyrekleklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2202 ANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------N 2274
Cdd:TIGR02169 436 INELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraV 512
|
410
....*....|.
gi 2217316812 2275 LTTLRDGLHGI 2285
Cdd:TIGR02169 513 EEVLKASIQGV 523
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1866-2397 |
1.46e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.79 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1866 LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK 1945
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1946 IKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNR---IRTWQKTH 2022
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLAlalLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2023 QGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINslQSDFTKYLTTadssllq 2102
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDV------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2103 tnialqlmeKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcav 2182
Cdd:COG0840 232 ---------DSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2183 DAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL-- 2257
Cdd:COG0840 292 ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELge 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2258 --QQTLNIVTVQKEVID-TNLTTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDI 2307
Cdd:COG0840 359 ssQEIGEIVDVIDDIAEqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2308 TDEVLDGlnpIQTDVERIKDTygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELI 2386
Cdd:COG0840 437 MEEGSEE---VEEGVELVEEA---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAA 500
|
570
....*....|.
gi 2217316812 2387 QQARDAASKVA 2397
Cdd:COG0840 501 QENAASVEEVA 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1865-2396 |
2.06e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1865 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1944
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1945 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2024
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2025 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2088
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2089 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2161
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2162 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2223
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2224 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2296
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2297 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2364
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 2217316812 2365 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2396
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2071-2357 |
2.37e-05 |
|
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: 48.95 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2071 ALGAIQRQVKEINSLQSDFTKYLTtadSSLLQTNIALQLMEKSQKEYEklaaSLNEARQELSDKVRELSRSAGK------ 2144
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQ---EYLSPENAHKIQIEILEKELS----SLAQETEELQKKATQTLAKAQQvnaese 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2145 ------TSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIK 2218
Cdd:pfam06008 79 rtlghaKELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2219 EDLpRKAKtlssnsdKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvqkeviDTNlttlrDGLHgiqrgDIDAMISSAK 2298
Cdd:pfam06008 148 AEL-KAAQ-------DLLSRIQTWFQSPQEENKALANALRDSLA---------EYE-----AKLS-----DLRELLREAA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 2299 SMVRKANDITDEVLDGLNPIQTDVERIkdtygRTQNEDFKKALTDADNSV---NKLTNKLPD 2357
Cdd:pfam06008 201 AKTRDANRLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1847-2384 |
2.39e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1916
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1995
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1996 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2067
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2068 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2138
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2139 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2217
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2218 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2295
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2296 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2375
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 2217316812 2376 SDNMDRIRE 2384
Cdd:PRK02224 697 RERREALEN 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1849-2179 |
2.45e-05 |
|
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: 50.50 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1849 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1920
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1921 NSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDgegnnvpsgdfsrEWAEAQRMMRELRNRNFGKH 1997
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKD-------------KVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1998 LREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAAQA-KQANGLNQENERALG 2073
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERlRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2074 AIQRQVKEINSLQSDF---------------------TKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLneaRQELS 2132
Cdd:pfam15921 661 EVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM---QKQIT 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316812 2133 DKVRELSRSAGKTSLVEEA------EKH------ARSLQELAKQLEEIKRNASGDELVR 2179
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAmtnankEKHflkeekNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1980-2196 |
3.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1980 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2053
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2054 AAAQAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAA 2122
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217316812 2123 SLNEARQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2196
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1817-2085 |
3.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1817 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1896
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1897 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDGEGNNVPSg 1973
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIADAEDEIER- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1974 dfSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEY----EAKLSDLRA 2049
Cdd:PRK02224 611 --LREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYleqvEEKLDELRE 674
|
250 260 270
....*....|....*....|....*....|....*.
gi 2217316812 2050 RlqeaaaqakqanglNQENERALGAIQRQVKEINSL 2085
Cdd:PRK02224 675 E--------------RDDLQAEIGAVENELEELEEL 696
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1982-2311 |
3.91e-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: 49.67 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1982 AQRMmRELRNRnfgkhLREAEADkresqLLLNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQA 2061
Cdd:TIGR02168 212 AERY-KELKAE-----LRELELA-----LLVLRLE--------ELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2062 NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA-----LQLMEKSQKEYEKLAASLNEARQELSDK 2134
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2135 VrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQ 2214
Cdd:TIGR02168 353 L---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2215 TVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQrgdidAMI 2294
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQ-----ARL 491
|
330
....*....|....*..
gi 2217316812 2295 SSAKSMVRKANDITDEV 2311
Cdd:TIGR02168 492 DSLERLQENLEGFSEGV 508
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2101-2265 |
4.23e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.55 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2101 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2178
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2179 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2253
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 2217316812 2254 LNNLQQTLNIVT 2265
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1998-2316 |
4.81e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1998 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQR 2077
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEEL----------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2078 QVKEINSLQSDFTKY------LTTADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEA 2151
Cdd:COG4372 99 AQEELESLQEEAEELqeeleeLQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2152 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSN 2231
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2232 SDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEV 2311
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
....*
gi 2217316812 2312 LDGLN 2316
Cdd:COG4372 336 LAELA 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1817-1947 |
4.89e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1817 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1896
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 1897 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1947
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2446-2572 |
5.55e-05 |
|
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: 45.10 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2446 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2521
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 2522 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2572
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1834-2147 |
5.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1834 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1912
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1913 TLQEKaqvnsrkaqtlnnnVNRATQSAKELDVKIKNVIRNvhillkqisgtdgegnnvpsgdfsrewaeAQRMMRE---- 1988
Cdd:COG4942 87 ELEKE--------------IAELRAELEAQKEELAELLRA-----------------------------LYRLGRQppla 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1989 --LRNRNFGKHLREAEADKRESQLLLNRIRTWQKThqgennglansiRDSLNEYEAKLSDLRARLqeaaaqakqanglnq 2066
Cdd:COG4942 124 llLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------LAELAALRAELEAERAEL--------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2067 enERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2146
Cdd:COG4942 177 --EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 2217316812 2147 L 2147
Cdd:COG4942 255 L 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 5.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316812 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1878-2399 |
6.90e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1878 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIK------- 1947
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKtaesdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1948 ----------------------------NVIRNVHILLKQI-------SGTDGEGNNVPSG--------DFSREWAEAQR 1984
Cdd:PRK01156 267 meleknnyykeleerhmkiindpvyknrNYINDYFKYKNDIenkkqilSNIDAEINKYHAIikklsvlqKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1985 MMRELRN-------------------RNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLS 2045
Cdd:PRK01156 347 RYDDLNNqilelegyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2046 DLRARLQEAAAQAKQ----ANGLNQENERALGAIQRQVKEINSLQSDFTKylttaDSSLLQTNIalqlmeksqKEYEKLA 2121
Cdd:PRK01156 427 SLNQRIRALRENLDElsrnMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE-----KKSRLEEKI---------REIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2122 ASLNEARQELsdkVRELSRSAGKTslVEEAEKHARSLQELAKQLEEIKrnasgDELVRCAvDAATAYENILNAIKAAEDA 2201
Cdd:PRK01156 493 KDIDEKIVDL---KKRKEYLESEE--INKSINEYNKIESARADLEDIK-----IKINELK-DKHDKYEEIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2202 ANRAASASESALQTVI-----------KEDLPRKAKTLSSNSDKLLNE----AKMTQKKLKqEVSPALNNLQQTLNIVTV 2266
Cdd:PRK01156 562 DLDSKRTSWLNALAVIslidietnrsrSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIR-EIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2267 QKEVIDTNLTTLRDglHGIQRGDIDAMISSAKSMVRKANDITDEvldgLNPIQTDVERIKDTYGRtqnedfKKALTDADN 2346
Cdd:PRK01156 641 NKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRAR------LESTIEILR 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2217316812 2347 S-VNKLTNKLPDLWRKIESINQQLLPLGNIsdnmDRIREliqqardAASKVAVP 2399
Cdd:PRK01156 709 TrINELSDRINDINETLESMKKIKKAIGDL----KRLRE-------AFDKSGVP 751
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1842-2187 |
1.05e-04 |
|
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: 48.28 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1842 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1908
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1909 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE------------------------------LDVKiknvIRNVH 1954
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsflnkktkqlqdlteekstlageirdlkdmLDVK----ERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1955 ILLKQISgtdgegnnvpsgDFSREWAEAQRMMRELRNRNFGKH------------LREAEADK------------RESQL 2010
Cdd:pfam10174 398 VLQKKIE------------NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttLEEALSEKeriierlkeqreREDRE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2011 LLNRIRTWQKthqgENNGL---ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVKEINSLQS 2087
Cdd:pfam10174 466 RLEELESLKK----ENKDLkekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2088 DFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL-VEEAEK 2153
Cdd:pfam10174 539 QLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRqMKEQNK 618
|
410 420 430
....*....|....*....|....*....|....
gi 2217316812 2154 HARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2187
Cdd:pfam10174 619 KVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1868-2099 |
1.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1868 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQsakeldvKIK 1947
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1948 NVIRNVhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFGKHLREAEADKRESQLLLNRIRTWQK 2020
Cdd:COG3883 90 ERARAL-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316812 2021 THQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS 2099
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1841-2165 |
1.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1841 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1916
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1917 KAQVNSRkaQTLNNNVNRATQSAKELDVKiknvirnvHILLKQISGTDGEGNnvpsgdfsREWAEAQRMMRELRNR--NF 1994
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVERELR--------ENLEERIDALRARLN--------RAEEELERAMRAFNREwpAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1995 GKHLREAEADKRESQLLLNRIrtwqkthqgENNGLAnsirdslnEYEAKLSDLRARLQEAAAQakqanGLNQENERALGA 2074
Cdd:COG4913 804 TADLDADLESLPEYLALLDRL---------EEDGLP--------EYEERFKELLNENSIEFVA-----DLLSKLRRAIRE 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2075 IQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAE 2152
Cdd:COG4913 862 IKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSE 919
|
330
....*....|...
gi 2217316812 2153 KHARSLQELAKQL 2165
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1892-2402 |
2.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1892 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvHILLKQISGTDGEGNNVP 1971
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-----RDSLIQSLATRLELDGFE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1972 SGDFS-REWAEAQRMMRELRN---RNFGKHLREAEADKRESQLLLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 2047
Cdd:TIGR00606 384 RGPFSeRQIKNFHTLVIERQEdeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2048 RARLqeaaaqakqanglnQENERALGAIQRQVKeinsLQSDFTKYLttADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2127
Cdd:TIGR00606 457 KFVI--------------KELQQLEGSSDRILE----LDQELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2128 RQELSDKVRELSRSagKTSLvEEAEKHARSLQELAKQLEEIKRNASgDELVRCA---------VDAATAYENILNAIKAA 2198
Cdd:TIGR00606 517 LRKLDQEMEQLNHH--TTTR-TQMEMLTKDKMDKDEQIRKIKSRHS-DELTSLLgyfpnkkqlEDWLHSKSKEINQTRDR 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2199 EDAANRAASASESaLQTVIKEDLPRKAKTLSSNSDKLLN-------EAKMtqKKLKQEVSPAlnnlQQTLNIVTVQKEVI 2271
Cdd:TIGR00606 593 LAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDvcgsqdeESDL--ERLKEEIEKS----SKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2272 DTNLTTLRDGLHG----IQR-----GDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEdfkkalt 2342
Cdd:TIGR00606 666 SQFITQLTDENQSccpvCQRvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI------- 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217316812 2343 dadnsVNKLTNKLPDLWRKIESINQQLLPL-GNISDN---MDRIRELIQQARDAASKVAVPMRF 2402
Cdd:TIGR00606 739 -----IDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQetlLGTIMPEEESAKVCLTDVTIMERF 797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1847-2140 |
3.29e-04 |
|
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: 46.59 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1847 EQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA 1918
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1919 QVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQI----SGTDGEGNnvpsgdfSREWAEAQRMMRELRNRNF 1994
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleSELEALLN-------ERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1995 GKHLREAEADKRESQLLLNRIRTwqkthqgennglansirdSLNEYEAKLSDLRARLQEAAAQakqangLNQENERALGA 2074
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELRE------------------KLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 2075 IQRQVKEINSLQS---DFTKYLTTADSSLLQTNI-ALQLMEKSQKEYEKLAA---SLNEARQELSDKVRELSR 2140
Cdd:TIGR02168 956 AEALENKIEDDEEearRRLKRLENKIKELGPVNLaAIEEYEELKERYDFLTAqkeDLTEAKETLEEAIEEIDR 1028
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.32e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316812 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.51e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2217316812 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1873-2146 |
3.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1873 ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRN 1952
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1953 VhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFgkhLREAEADKREsqlllnrirtwqkthqge 2025
Cdd:COG3883 95 L-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADL---LEELKADKAE------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2026 nnglansirdsLNEYEAKLSDLRARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2105
Cdd:COG3883 145 -----------LEAKKAELEAKLAELEA----------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2217316812 2106 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2146
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1896-2173 |
6.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1896 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK----ELDVK-IKNVIRNVHILLKQISGTdgegnnv 1970
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1971 pSGDFS---REWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDL 2047
Cdd:COG4913 684 -SDDLAaleEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2048 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTTADSSLLQTNIAlqLMEKSQKEYEKLAAS-LNE 2126
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE--SLPEYLALLDRLEEDgLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217316812 2127 ARQELSDKVRELSRsAGKTSLVEEAEKHARSLQElakQLEEIkrNAS 2173
Cdd:COG4913 832 YEERFKELLNENSI-EFVADLLSKLRRAIREIKE---RIDPL--NDS 872
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1703-1795 |
7.06e-04 |
|
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: 42.39 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1703 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1771
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 2217316812 1772 -GTQCERCAPGYFGNPQkfGGSCQP 1795
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
7.15e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217316812 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
7.23e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 7.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217316812 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2062-2262 |
1.27e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2062 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2137
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2138 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2194
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316812 2195 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2262
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.41e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217316812 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1838-2130 |
1.58e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1838 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1913
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1914 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRN 1991
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQ-------LRAQL-------------------AELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1992 RNFGKHLREAEADKRESQLllnrirtwqkthqgeNNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEnera 2071
Cdd:COG3206 285 RYTPNHPDVIALRAQIAAL---------------RAQLQQEAQRILASLEAELEALQAREAS----------LQAQ---- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316812 2072 LGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLAASLNEARQE 2130
Cdd:COG3206 336 LAQLEARLAELPELEAELRR---------LEREV-----EVARELYESLLQRLEEARLA 380
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1890-2377 |
1.79e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1890 ISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE 1966
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEEL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1967 GNNVPSG--DFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNRIR----------- 2016
Cdd:PTZ00440 604 INEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNTSKneyeklefmks 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2017 ------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQR 2077
Cdd:PTZ00440 684 dnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2078 QVKEINSLQSDFTKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EA 2151
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHT 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2152 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV--------- 2216
Cdd:PTZ00440 829 EKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkid 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2217 IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHG 2284
Cdd:PTZ00440 909 LKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDK 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2285 IQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFK 2338
Cdd:PTZ00440 989 EKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIK 1068
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2217316812 2339 KALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2377
Cdd:PTZ00440 1069 KYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2063-2342 |
2.09e-03 |
|
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: 43.79 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2063 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2130
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2131 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2208
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2209 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2288
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217316812 2289 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2342
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1825-2004 |
2.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1825 AEECDDCDSCVMTLlnDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHG--------S 1895
Cdd:COG4913 268 RERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1896 KIEGLERELTDLNQEFETLQEKAQV--------------NSRKAQ----TLNNNVNRATQSAKELDVKIKNVIRNVHILL 1957
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAlglplpasaeefaaLRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217316812 1958 KQISGTDGEGNNVPsgdfsrewAEAQRMMRELRnrnfgKHLREAEAD 2004
Cdd:COG4913 426 AEIASLERRKSNIP--------ARLLALRDALA-----EALGLDEAE 459
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1674-1797 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1674 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1749
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217316812 1750 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1797
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3195-3253 |
2.73e-03 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 40.38 E-value: 2.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 3195 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSV 3253
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSV 58
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1841-2434 |
2.78e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1841 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA-- 1918
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1919 ------------QVNSRKA----------------QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE---- 1966
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllql 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1967 GNNVPSGDFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 2017
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2018 -----------------------WQKTHQGENN--GLANSI-RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERA 2071
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVKLDLkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2072 LGAIQRQVKEINSLQSDFTKYLTTADSSLLQ-----TNIALQLME-------KSQKEYEKLAASLN-------------- 2125
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdekQSEKDKKNKalaerkdSANERLNSLEAQLKqldkkhqawleeqk 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2126 ----EARQELSDKVREL--SRSAGKTSLVEEAEKHARSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2193
Cdd:pfam12128 707 eqkrEARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2194 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT 2273
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2274 NLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERikdtygrtQNEDFKKALTDADNSvnkltn 2353
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK--------YVEHFKNVIADHSGS------ 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2354 klpDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVrLPNDLEDLkgYTSLSLFLQRPN 2433
Cdd:pfam12128 927 ---GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVDLTEF--YDVLADFDRRIA 1000
|
.
gi 2217316812 2434 S 2434
Cdd:pfam12128 1001 S 1001
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1867-2395 |
3.52e-03 |
|
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: 43.50 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1867 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLERELTDLNQEFETLQE--KAQVNSRKaqTLNNNVNRATQSAKELDV 1944
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLELKEKIKNISDKNEyiKKAIDLKK--IIENNNAYIDELAKISPY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1945 KIKNVIRNVHILLKQISGtdgEGNNVPSGDFSREWAEAQRMMRE----------------------------LRNRNFGK 1996
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKS---ELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlkskidkeydkiqnMETATVEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1997 HLREAEADKREsqlLLNRIRTWQKTHQGENNG---------------LANSI------RDSLNEYEAKLSDLRARLqeaA 2055
Cdd:TIGR01612 723 HLSNIENKKNE---LLDIIVEIKKHIHGEINKdlnkiledfknkekeLSNKIndyakeKDELNKYKSKISEIKNHY---N 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2056 AQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT----TADSSLLQTNIALQL----MEKSQKEYEKLAASLNEA 2127
Cdd:TIGR01612 797 DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINemkfMKDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2128 RQELSDKvrELSRSAGK----TSLVEEA----EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAA 2198
Cdd:TIGR01612 877 KAEISDD--KLNDYEKKfndsKSLINEInksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTI 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2199 EDAANRAASASESALQTVI--KEDLPRKAKTLS-----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQt 2260
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLIdkINELDKAFKDASlndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ- 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2261 lNIVTVQKEV------IDTNLTTLRDglhgiqrgDIDAMISSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQN 2334
Cdd:TIGR01612 1034 -KIEDANKNIpnieiaIHTSIYNIID--------EIEKEIGKNIELLNK------EILEEAEINITNFNEIKEKLKHYNF 1098
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 2335 EDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN-MDRIRELIQQARDAASK 2395
Cdd:TIGR01612 1099 DDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENyIDEIKAQINDLEDVADK 1161
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1978-2165 |
3.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1978 EWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS----LNEYEAKLSDLRARLqe 2053
Cdd:COG4913 282 RLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2054 aaaqakqanglnQENERALGAIQRQVKEI----NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQ 2129
Cdd:COG4913 355 ------------EERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217316812 2130 ELSDKVRELSRSAGKTSLVEEAEKHARslQELAKQL 2165
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALR--DALAEAL 453
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2064-2159 |
3.58e-03 |
|
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: 40.55 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2064 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2142
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 2217316812 2143 gktsLVEEAEKHARSLQ 2159
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1974-2179 |
3.89e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1974 DFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2040
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2041 EAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQK----- 2115
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217316812 2116 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHARSLQELAKQLEEIKRNASGD---ELVR 2179
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1843-2125 |
5.20e-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: 41.45 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1843 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1921
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1922 SRKAQTLNNNvnratqsaKELDvkiknvirnvhILLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRnrnfgKHLREA 2001
Cdd:COG1579 79 EEQLGNVRNN--------KEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2002 EaDKREsqlllnrirtwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQrqvKE 2081
Cdd:COG1579 116 M-ERIE------------------------ELEEELAELEAELAELEAEL----------EEKKAELDEELAELE---AE 157
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2217316812 2082 INSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2125
Cdd:COG1579 158 LEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1867-2185 |
5.76e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1867 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1943
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1944 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2010
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2011 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2082
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2083 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2156
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217316812 2157 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2185
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2100-2196 |
6.21e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2100 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2173
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 2217316812 2174 GDELvrcavdaATAYENILNAIK 2196
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1998-2176 |
8.29e-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: 41.67 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 1998 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQE---NERALGA 2074
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRI----------RALEQElaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316812 2075 IQRQV----KEINSLQSDFTKYLTTA--------------DSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2136
Cdd:COG4942 88 LEKEIaelrAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217316812 2137 ELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2176
Cdd:COG4942 168 ELEAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| |
