|
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 ... |
1829-2086 |
9.51e-112 |
|
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: 356.34 E-value: 9.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1829 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRA 1908
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1909 IQSAKELDMKIKTVIRNVHILLKQISGPDGEGNNVPSGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 1988
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1989 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTS 2068
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 982311033 2069 ADSSLLQTNIALQLMEKS 2086
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.06e-103 |
|
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: 330.48 E-value: 6.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 46 SLHPPYFNLAEAARIWATATCGErgpserrPRPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 982311033 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
1.50e-96 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 311.82 E-value: 1.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 47 LHPPYFNLAEAARIWATATCGERGPserrprpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 982311033 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 ... |
2270-2398 |
4.51e-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: 154.57 E-value: 4.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2270 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGSTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2340
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2341 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2398
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1500-1634 |
9.35e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 150.88 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1500 WVAPASYLGDKVSSYGGYLTYQAKSFGLPSDmVLLEKKPDVQLTGQHMSVIYEETNTPRPDR--LHHGRVQVVEGNFRHa 1577
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 1578 SSRAPVSREELMTVLSRLADMRIQGLYFTETQRLTLSEVGLEEASDTGSGRIAYAVE 1634
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1495-1623 |
1.70e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 143.94 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1495 VHSASWVAPASYLGDKVSSYGGYLTYQAKSFGLPSDmvLLEKKPDVQLTGQHMSVIYEETNTPRPDRLHHGRVQVVEGNF 1574
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 1575 RHASSRaPVSREELMTVLSRLADMRIQGLYFTETQRLTLSEVGLEEASD 1623
Cdd:smart00281 80 QYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3140-3291 |
1.75e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 130.62 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3140 GIYFSEeGGHVILAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLGVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3218
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 3219 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVN 3291
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3163-3292 |
3.47e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.44 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3163 KLVFSIRPRSLTGILIHIGSQPGK-HLGVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3240
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 3241 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVNH 3292
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2976-3116 |
7.13e-30 |
|
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: 117.52 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2976 TSHLLFKLPQeLLKPRSQFAVDVQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3053
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982311033 3054 VFGHDGEKGRLVVDGLR-AREGSLPGNSTVSLRGPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3116
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3168-3293 |
6.02e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 113.67 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3168 IRPRSLTGILIHIGSQPGKHLGVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3247
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 982311033 3248 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVNHI 3293
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2993-3118 |
2.74e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.35 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2993 QFAVDVQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3069
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 3070 RAREGSLPGNSTV-SLRGPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3118
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2584-2724 |
3.01e-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: 104.04 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2584 YFEGTGYARVPTQPHAS-IPTFGQTIQTTVDRGLLFFA--ENRDRFISLNIEDGKLMVRYKLNSEPPKERgVGDAINNGR 2660
Cdd:cd00110 3 SFSGSSYVRLPTLPAPRtRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2661 DHSIQIKIGKVQKRMWIN----VDFQNTIIDGEVFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDgervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2603-2724 |
4.95e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.02 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2603 TFGQTIQTTVDRGLLFFAENRDR--FISLNIEDGKLMVRYKLNSEPPKERGVGDAINNGRDHSIQIKIGKVQKRMWINV- 2679
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgdYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 982311033 2680 DFQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2751-2883 |
1.08e-22 |
|
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: 96.72 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2751 SASFSRGGQLSFTNLGSPLTdHLQASFGFQTFQPSGILLSHQTWTST--LQVTLEDGHIELSTRD-SGSPIFKSPQTYMD 2827
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLgSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2828 GLLHYVSVISDNSGLRLLIDDQPL--RNNQRLNRISSSQQSLRLGG-------------SNFEGCISNVFV 2883
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVveSGSPGGSALLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3000-3118 |
3.83e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 94.41 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3000 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3076
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 982311033 3077 PGNS-TVSLRGPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3118
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2776-2885 |
1.96e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 78.15 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2776 SFGFQTFQPSGILLSHQTW--TSTLQVTLEDGHIELSTRDSGSPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQPL 2851
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKggGDYLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 2852 RNNQRL--NRISSSQQSLRLGG-------------SNFEGCISNVFVQR 2885
Cdd:smart00282 83 VSGESPggLTILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1248-1296 |
2.74e-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: 75.08 E-value: 2.74e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1248 CECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYGFPHCKPCSC 1296
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2610-2724 |
4.08e-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: 74.38 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2610 TTVDRGLLFFAEN-RDRFISLNIEDGKLMVRYKLNSEPPKERGVGDAINNGRDHSIQIKIgkVQKRMWINVDFQNTI--- 2685
Cdd:pfam02210 3 TRQPNGLLLYAGGgGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVER--NGNTLTLSVDGQTVVssl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 982311033 2686 IDGEVFDF---STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:pfam02210 81 PPGESLLLnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1820-2323 |
6.93e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE---- 1889
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1890 -KAQV------NSRKAQTLYN------NVNRAIQ----SAKELDMKIKTVIRNVHILLKQISgpdgegnnvpsgEFSREW 1952
Cdd:TIGR04523 368 kQNEIeklkkeNQSYKQEIKNlesqinDLESKIQnqekLNQQKDEQIKKLQQEKELLEKEIE------------RLKETI 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHqgennglansIRDSLNEYEAKLSDLRARLQEAAARAK 2032
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQ----------LKVLSRSINKIKQNLEQKQKELKSKEK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2033 QANGLNQENeralgaiqRQVKEINslqsdftKYLTSADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDKVREL- 2111
Cdd:TIGR04523 497 ELKKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDLEDELn 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2112 SRSAGKTSLVEEAEKhaqslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESALQTVIK 2191
Cdd:TIGR04523 549 KDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEKQELID 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2192 E------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRGIqrgdida 2265
Cdd:TIGR04523 593 QkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI------- 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 2266 mISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGSTQNE-----DFKKALTDADNSVNK 2323
Cdd:TIGR04523 665 -IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNFNK 739
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1247-1289 |
9.78e-15 |
|
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: 70.46 E-value: 9.78e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 1247 PCECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYGFP 1289
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1248-1291 |
2.78e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.18 E-value: 2.78e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1248 CECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYG--FPHC 1291
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1338-1389 |
1.46e-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: 64.30 E-value: 1.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1389
Cdd:pfam00053 1 CDCNPHGSLSD---TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
514-556 |
4.63e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 4.63e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 514 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 556
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1811-2145 |
4.97e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1811 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQL--------LNYRSTISNHGSKIEGLERELTDLNQ 1882
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1883 EFETLQEK-----AQVNSRKAQTLYNNVNRAIQSAKELDMkiktVIRNVHILLKQISGPDGEGNNVP------------- 1944
Cdd:COG4717 214 ELEEAQEEleeleEELEQLENELEAAALEERLKEARLLLL----IAAALLALLGLGGSLLSLILTIAgvlflvlgllall 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1945 SGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQkthqgENNGLANSIRDsLNEYEAKLSDLRARL 2024
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEE-LQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2025 QEAAARAKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTSADSSLLQTNIALQLmEKSQKEYEKLAASLN 2098
Cdd:COG4717 364 QLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELE 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 982311033 2099 EARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNA 2145
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1386-1436 |
5.16e-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: 5.16e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1386 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANPKGCT 1436
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
515-558 |
6.33e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 6.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 515 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 558
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1338-1383 |
6.59e-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: 6.59e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1383
Cdd:cd00055 2 CDCNGHGSLSG---QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
470-517 |
6.75e-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: 62.37 E-value: 6.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 470 CDCNPEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 517
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1387-1435 |
6.88e-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: 62.37 E-value: 6.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1387 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANPKGC 1435
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1338-1384 |
1.87e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.87e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1384
Cdd:smart00180 1 CDCDPGGSASG---TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1668-1714 |
3.64e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1668 PCNCNGH---SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1714
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
469-510 |
3.68e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.68e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 469 RCDCNPEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 510
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| LamG |
smart00282 |
Laminin G domain; |
2417-2552 |
4.38e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.13 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2417 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDRETELQVDQiltesetqEAVMD----RVKFQRIYQFARL--NYTKGAT 2490
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 2491 SSKPEipgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLRFPPYKGCIELDDLNEN 2552
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-472 |
5.85e-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: 5.85e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFPFCLRCDC 472
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
515-562 |
1.12e-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: 1.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 982311033 515 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.32e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 1.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-512 |
1.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 470 CDCNPEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 512
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2372-2550 |
2.21e-10 |
|
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: 61.67 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2372 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDRET 2451
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2452 ELQVDQILTESETQeavmdRVKFQRIYQFARL--NYTKGATSSKPEipgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDF 2529
Cdd:cd00110 70 VLSSKTPLNDGQWH-----SVSVERNGRSVTLsvDGERVVESGSPG-----------GSALLNLDGP---LYLGGLPEDL 130
|
170 180
....*....|....*....|.
gi 982311033 2530 KLPSRLRFPPYKGCIELDDLN 2550
Cdd:cd00110 131 KSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2779-2883 |
4.01e-10 |
|
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: 60.13 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2779 FQTFQPSGILL-SHQTWTSTLQVTLEDGHIELSTRDSGSP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQPL--RN 2853
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVvsSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 982311033 2854 NQRLNRISSSQQSLRLGG-------------SNFEGCISNVFV 2883
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
8.08e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 8.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1387-1435 |
8.91e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 8.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1387 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHldpANPKGC 1435
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1716-1766 |
1.13e-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: 56.21 E-value: 1.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1716 CPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNPQKFGGSC 1766
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1669-1716 |
1.46e-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: 1.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1669 CNCNGH---SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1716
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1715-1767 |
1.09e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 982311033 1715 ACPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNPQKfGGSCQ 1767
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-660 |
1.20e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFaleKSNYFGC 660
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
610-661 |
1.23e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.13 E-value: 1.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 661
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-660 |
1.44e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 660
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1823-2141 |
1.65e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1823 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQtly 1902
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE--- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1903 nNVNRAIQSAKEldmkiktvirNVHILLKQISGPDGEGNNVPSgefSREWAEAQR-MMRELRNRNFGK------HLREAE 1975
Cdd:PRK02224 374 -EAREAVEDRRE----------EIEELEEEIEELRERFGDAPV---DLGNAEDFLeELREERDELREReaeleaTLRTAR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1976 ADKRESQLLLNRIRTWQKTHQGENNGLANSI---RDSLNEYEAKLSDLRA----------RLQEAAARAKQANGLNQENE 2042
Cdd:PRK02224 440 ERVEEAEALLEAGKCPECGQPVEGSPHVETIeedRERVEELEAELEDLEEeveeveerleRAEDLVEAEDRIERLEERRE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2043 RA--LGAIQRQVKE-----INSLQSDFTKYLTSADSsllQTNIALQLMEKSQKEYEKLAAsLNEARQELSDKVRELSRSA 2115
Cdd:PRK02224 520 DLeeLIAERRETIEekrerAEELRERAAELEAEAEE---KREAAAEAEEEAEEAREEVAE-LNSKLAELKERIESLERIR 595
|
330 340
....*....|....*....|....*.
gi 982311033 2116 GKTSLVEEAEKHAQSLQELAKQLEEI 2141
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAEL 621
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1716-1759 |
3.40e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 982311033 1716 CPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNP 1759
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1669-1711 |
5.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 5.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1669 CNCN--GH-SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1711
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1971-2289 |
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 982311033 1971 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQR 2050
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2051 QVKEinsLQSDFTKyLTSADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQS 2130
Cdd:COG4372 109 EAEE---LQEELEE-LQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2131 LQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLN 2210
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 2211 EAKMTQKKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRGIQRGDIDAMISSAKSMVRKANDITDEVLDGLN 2289
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
564-607 |
2.45e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 2.45e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 982311033 564 ACDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNLDKENPNGC 607
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
298-344 |
3.94e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 3.94e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 982311033 298 RCVCNGHA---EVCNANNpeklFRCQCQHHTCGETCDRCCTGYNQRRWQP 344
Cdd:cd00055 1 PCDCNGHGslsGQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
663-706 |
6.30e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 6.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYYFPDLH 706
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1839-2364 |
7.37e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1839 LEQMRHMETQAKDLRNQLLNYRS---TISNHGSKIEGLERELTDLNQEFETLQEK-AQVNSR------KAQTLYNNVNRa 1908
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKiRELEERieelkkEIEELEEKVKE- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1909 iqsAKELDMKIKTVIRNVHILLKQISgpdgEGNNVPSGE--FSREWAEAQRMMRELRNRNfgKHLREAEADKRESQLLLN 1986
Cdd:PRK03918 285 ---LKELKEKAEEYIKLSEFYEEYLD----ELREIEKRLsrLEEEINGIEERIKELEEKE--ERLEELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1987 RIRTWQKTHQgenngLANSIRDSLNEYEAKLSDLR----ARLQEAAARAKqanglnQENERALGAIQRQVKEINSLQSDF 2062
Cdd:PRK03918 356 ELEERHELYE-----EAKAKKEELERLKKRLTGLTpeklEKELEELEKAK------EEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2063 TKYLTSADSS---------LLQTNIALQLMEKSQKEYEKLAASLnearQELSDKVRELSRSAGKTSLVEEAEKHAQSLQE 2133
Cdd:PRK03918 425 KKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRIEKEL----KEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2134 LAKQLEEIKRNASG---DELVRcavdAATAYENI---LNAIKAAedaanraasasesalQTVIKEDLpRKAKTLSSNSDK 2207
Cdd:PRK03918 501 LAEQLKELEEKLKKynlEELEK----KAEEYEKLkekLIKLKGE---------------IKSLKKEL-EKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2208 LLNEAKMTQKKLKqEVSPALSNLQ-QTLNIV--TVQR-EVIATNLTTLRDGLRGIQRgdIDAMISSAKSMVRKANDITDE 2283
Cdd:PRK03918 561 LEKKLDELEEELA-ELLKELEELGfESVEELeeRLKElEPFYNEYLELKDAEKELER--EEKELKKLEEELDKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2284 VLDGLNPIQTDVERIKDTYGSTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIR---ELIQ 2360
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkelEKLE 717
|
....
gi 982311033 2361 QARD 2364
Cdd:PRK03918 718 KALE 721
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2020-2235 |
7.75e-07 |
|
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: 54.05 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2020 LRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQS----------------DFTKYLTSADSSllQTNI---AL 2080
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSAsvaslekqlleltrvnELLKAKFSEDGT--QKKMsslSM 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2081 QLM------EKSQKEY----EKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHAQSLQELAKQLEEIKR-NASGDE 2149
Cdd:pfam15905 160 ELMklrnklEAKMKEVmakqEGMEGKLQVTQKNLEHSKGKVAQLEEK--LVSTEKEKIEEKSETEKLLEYITElSCVSEQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2150 LVRCAVDAATAyENILNAIKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLSN 2229
Cdd:pfam15905 238 VEKYKLDIAQL-EELLKEKNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEE 311
|
....*.
gi 982311033 2230 LQQTLN 2235
Cdd:pfam15905 312 LKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
663-701 |
1.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.66e-06
10 20 30
....*....|....*....|....*....|....*....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYY 701
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
3.78e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 3.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 356 CNCHGHAS---DCYydsdverqqaslntqgiyAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSlsdTCD------------------PETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
663-701 |
8.53e-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: 8.53e-06
10 20 30
....*....|....*....|....*....|....*....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYY 701
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1806-2361 |
1.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1806 SCVMTLLNDLATmgeqLRLVKSQLQGLSASaglLEQMRH-----METQAKDLRNqllNYRSTISNHGSKIEGLERELTDL 1880
Cdd:TIGR00606 262 SKIMKLDNEIKA----LKSRKKQMEKDNSE---LELKMEkvfqgTDEQLNDLYH---NHQRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1881 NQEFETL-QEKAQVNSRKAQT------------LYNNVNRAIQSAKELDM-----KIKTVIRNVHILLKQISGPDGEGNN 1942
Cdd:TIGR00606 332 NKERRLLnQEKTELLVEQGRLqlqadrhqehirARDSLIQSLATRLELDGfergpFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1943 VPSGEFSREWAEAQRMMRELRNRNFGK----HLREAEADKRESQlLLNRIRTWQKTHQGENN------GLANSIRD-SLN 2011
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLgrtiELKKEILEKKQEE-LKFVIKELQQLEGSSDRileldqELRKAERElSKA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2012 EYEAKLSDLRARL----QEAAARAKQANGLNQENE----------------RALGAIQRQVKEINSLQSD---------- 2061
Cdd:TIGR00606 491 EKNSLTETLKKEVkslqNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIRKIKSRHSDeltsllgyfp 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2062 FTKYLTSADSSLL-QTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEE 2140
Cdd:TIGR00606 571 NKKQLEDWLHSKSkEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEK 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2141 IKRNasgdelvRCAVDAATA-YENILNAIKAAEDA---ANRAASASESALQTVIKeDLprKAKTLSSNSDKLLNEAKMTQ 2216
Cdd:TIGR00606 651 SSKQ-------RAMLAGATAvYSQFITQLTDENQSccpVCQRVFQTEAELQEFIS-DL--QSKLRLAPDKLKSTESELKK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2217 KKLKQEVSPALSNLQQtlNIVtvqrEVIATNLTTLRDGLRGIQRgdidamissakSMVRKANDITDE--VLDGLNP---- 2290
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQ--SII----DLKEKEIPELRNKLQKVNR-----------DIQRLKNDIEEQetLLGTIMPeees 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2291 ---IQTDVERIkdtygstqnEDFKKALTDADNSVNKLTNKLP--DLWRKIESINQQLLP----LGNISDNMDRIRELIQQ 2361
Cdd:TIGR00606 784 akvCLTDVTIM---------ERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEkqheLDTVVSKIELNRKLIQD 854
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1840-2158 |
1.25e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.37 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1840 EQM-RHMETQAKDLRNQLlnyrstisnhgskieglERELTDLN-QEFETLQEKAQVNSRKAQTLYNN-VNRAIQSAKELD 1916
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARLQAELHTEaVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1917 MKIKTVIRNVHillkqisgpdgegNNVPSGEFSREW------------------------AEAQRMMRELRNRNFGkhlr 1972
Cdd:NF041483 138 ERRQTVESHVN-------------ENVAWAEQLRARtesqarrlldesraeaeqalaaarAEAERLAEEARQRLGS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1973 EAEADKRESQLLLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARlQEAAARAKQANGLNQENERAL 2045
Cdd:NF041483 201 EAESARAEAEAILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QAR-RQAAELSRAAEQRMQEAEEAL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2046 GAIQRQV-KEINSLQSDFTKYLTSADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSR---SA 2115
Cdd:NF041483 275 REARAEAeKVVAEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEKlvaEA 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 982311033 2116 GKTSLVEEAEKHAQSLQELAKQLEEIKRNASGD--ELVRCAVDAA 2158
Cdd:NF041483 351 AEKARTVAAEDTAAQLAKAARTAEEVLTKASEDakATTRAAAEEA 395
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
2.78e-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: 43.88 E-value: 2.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 355 ACNCHGHAS---DCYYDSdverqqaslntqgiyaggGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGT------------------GQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
565-607 |
1.01e-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: 42.34 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 982311033 565 CDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNLDkENPNGC 607
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2419-2545 |
1.21e-04 |
|
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: 44.33 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2419 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDRETELQVdqilteseTQEAVMD----RVKFQRIYQFARLnytkgatsskp 2494
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTL----------- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2495 EIPGVYDMDGRNSNTLLNLDpENVVFYVGGYPPDFKLPSRLRFPPYKGCIE 2545
Cdd:pfam02210 70 SVDGQTVVSSLPPGESLLLN-LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
565-607 |
1.24e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 982311033 565 CDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNldkENPNGC 607
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
1.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 356 CNCH--GHASD-CYYDSdverqqaslntqgiyaggGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPDT------------------GQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2074-2238 |
2.85e-04 |
|
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: 43.85 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2074 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHAQslqELAKQLEEIKRNAS--GDELV 2151
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQG---EVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2152 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2226
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 982311033 2227 LSNLQQTLNIVT 2238
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-344 |
4.62e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 299 CVCN--GHA-EVCNANNpeklFRCQCQHHTCGETCDRCCTGYNQRRWQP 344
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1947-2169 |
1.54e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1947 EFSREWAEA----QRMMRELRNRNFGKHLREAEAdkresqlllnrirtWQKTHQGennglansIRDSLNEYEAKLSDLRA 2022
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDLESVEA--------------LLKKHEA--------LEAELAAHEERVEALNE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2023 rlqeaaarakQANGLNQENERALGAIQRQVKEINSLQSDFTKyLTSADSSLLQTniALQLMEKSQkEYEKLAASLNEARQ 2102
Cdd:cd00176 62 ----------LGEQLIEEGHPDAEEIQERLEELNQRWEELRE-LAEERRQRLEE--ALDLQQFFR-DADDLEQWLEEKEA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2103 ELSDkvRELSRSAGKtslVEEA-EKHAQSLQELAKQLEEIKR-NASGDELV-RCAVDAATAYENILNAIK 2169
Cdd:cd00176 128 ALAS--EDLGKDLES---VEELlKKHKELEEELEAHEPRLKSlNELAEELLeEGHPDADEEIEEKLEELN 192
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1953-2146 |
2.03e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQRMMRElrnrnfgkhlrEAEADKRESQLLLNRIRTWQktHQGENNglANSIRDslnEYEAKLSDLRA-------RLQ 2025
Cdd:NF041483 600 AEAERIRRE-----------AAEETERLRTEAAERIRTLQ--AQAEQE--AERLRT---EAAADASAARAegenvavRLR 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2026 -EAAARAKQANGLNQEN------------ER-------ALGAIQrqvKEINSLQSDFTKYLTSADSSllqtniALQLMEK 2085
Cdd:NF041483 662 sEAAAEAERLKSEAQESadrvraeaaaaaERvgteaaeALAAAQ---EEAARRRREAEETLGSARAE------ADQERER 732
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 2086 SQKEYEKLAAS----LNEARQELSDKVRELSRSAgkTSLVEEAEKHAQS-------LQELAKQleEIK--RNAS 2146
Cdd:NF041483 733 AREQSEELLASarkrVEEAQAEAQRLVEEADRRA--TELVSAAEQTAQQvrdsvagLQEQAEE--EIAglRSAA 802
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
299-337 |
3.14e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 982311033 299 CVCNGHAEV---CNANNpeklFRCQCQHHTCGETCDRCCTGY 337
Cdd:pfam00053 1 CDCNPHGSLsdtCDPET----GQCLCKPGVTGRHCDRCKPGY 38
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2073-2169 |
3.67e-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: 40.26 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2073 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHAQSLQELAKQLEEIKRNAS 2146
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 982311033 2147 GDELvrcavdaATAYENILNAIK 2169
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2019-2110 |
4.11e-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: 40.26 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2019 DLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKY---LTSADSSLLQTNIAlQLMEKSQKEYEKLAA 2095
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaatLSEAAREKKEKELQ-KKVQEFQRKQQKLQQ 83
|
90
....*....|....*
gi 982311033 2096 SLNEARQELSDKVRE 2110
Cdd:smart00935 84 DLQKRQQEELQKILD 98
|
|
| |
|
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 ... |
1829-2086 |
9.51e-112 |
|
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: 356.34 E-value: 9.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1829 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRA 1908
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1909 IQSAKELDMKIKTVIRNVHILLKQISGPDGEGNNVPSGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 1988
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1989 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTS 2068
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 982311033 2069 ADSSLLQTNIALQLMEKS 2086
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.06e-103 |
|
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: 330.48 E-value: 6.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 46 SLHPPYFNLAEAARIWATATCGErgpserrPRPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 982311033 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
1.50e-96 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 311.82 E-value: 1.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 47 LHPPYFNLAEAARIWATATCGERGPserrprpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 982311033 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 ... |
2270-2398 |
4.51e-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: 154.57 E-value: 4.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2270 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGSTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2340
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2341 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2398
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1500-1634 |
9.35e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 150.88 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1500 WVAPASYLGDKVSSYGGYLTYQAKSFGLPSDmVLLEKKPDVQLTGQHMSVIYEETNTPRPDR--LHHGRVQVVEGNFRHa 1577
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 1578 SSRAPVSREELMTVLSRLADMRIQGLYFTETQRLTLSEVGLEEASDTGSGRIAYAVE 1634
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1495-1623 |
1.70e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 143.94 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1495 VHSASWVAPASYLGDKVSSYGGYLTYQAKSFGLPSDmvLLEKKPDVQLTGQHMSVIYEETNTPRPDRLHHGRVQVVEGNF 1574
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 1575 RHASSRaPVSREELMTVLSRLADMRIQGLYFTETQRLTLSEVGLEEASD 1623
Cdd:smart00281 80 QYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3140-3291 |
1.75e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 130.62 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3140 GIYFSEeGGHVILAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLGVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3218
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 3219 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVN 3291
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3163-3292 |
3.47e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.44 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3163 KLVFSIRPRSLTGILIHIGSQPGK-HLGVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3240
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 3241 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVNH 3292
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2976-3116 |
7.13e-30 |
|
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: 117.52 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2976 TSHLLFKLPQeLLKPRSQFAVDVQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3053
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982311033 3054 VFGHDGEKGRLVVDGLR-AREGSLPGNSTVSLRGPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3116
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3168-3293 |
6.02e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 113.67 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3168 IRPRSLTGILIHIGSQPGKHLGVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3247
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 982311033 3248 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIFVNHI 3293
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2993-3118 |
2.74e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.35 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2993 QFAVDVQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3069
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 3070 RAREGSLPGNSTV-SLRGPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3118
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2584-2724 |
3.01e-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: 104.04 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2584 YFEGTGYARVPTQPHAS-IPTFGQTIQTTVDRGLLFFA--ENRDRFISLNIEDGKLMVRYKLNSEPPKERgVGDAINNGR 2660
Cdd:cd00110 3 SFSGSSYVRLPTLPAPRtRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2661 DHSIQIKIGKVQKRMWIN----VDFQNTIIDGEVFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDgervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2603-2724 |
4.95e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.02 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2603 TFGQTIQTTVDRGLLFFAENRDR--FISLNIEDGKLMVRYKLNSEPPKERGVGDAINNGRDHSIQIKIGKVQKRMWINV- 2679
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgdYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 982311033 2680 DFQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2751-2883 |
1.08e-22 |
|
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: 96.72 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2751 SASFSRGGQLSFTNLGSPLTdHLQASFGFQTFQPSGILLSHQTWTST--LQVTLEDGHIELSTRD-SGSPIFKSPQTYMD 2827
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLgSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2828 GLLHYVSVISDNSGLRLLIDDQPL--RNNQRLNRISSSQQSLRLGG-------------SNFEGCISNVFV 2883
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVveSGSPGGSALLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3000-3118 |
3.83e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 94.41 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3000 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3076
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 982311033 3077 PGNS-TVSLRGPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3118
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3000-3121 |
9.05e-20 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 87.76 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3000 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3075
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 3076 LPGNSTVSLRGPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPLD 3121
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2776-2885 |
1.96e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 78.15 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2776 SFGFQTFQPSGILLSHQTW--TSTLQVTLEDGHIELSTRDSGSPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQPL 2851
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKggGDYLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 2852 RNNQRL--NRISSSQQSLRLGG-------------SNFEGCISNVFVQR 2885
Cdd:smart00282 83 VSGESPggLTILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1248-1296 |
2.74e-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: 75.08 E-value: 2.74e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1248 CECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYGFPHCKPCSC 1296
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2610-2724 |
4.08e-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: 74.38 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2610 TTVDRGLLFFAEN-RDRFISLNIEDGKLMVRYKLNSEPPKERGVGDAINNGRDHSIQIKIgkVQKRMWINVDFQNTI--- 2685
Cdd:pfam02210 3 TRQPNGLLLYAGGgGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVER--NGNTLTLSVDGQTVVssl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 982311033 2686 IDGEVFDF---STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2724
Cdd:pfam02210 81 PPGESLLLnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1820-2323 |
6.93e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE---- 1889
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1890 -KAQV------NSRKAQTLYN------NVNRAIQ----SAKELDMKIKTVIRNVHILLKQISgpdgegnnvpsgEFSREW 1952
Cdd:TIGR04523 368 kQNEIeklkkeNQSYKQEIKNlesqinDLESKIQnqekLNQQKDEQIKKLQQEKELLEKEIE------------RLKETI 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHqgennglansIRDSLNEYEAKLSDLRARLQEAAARAK 2032
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQ----------LKVLSRSINKIKQNLEQKQKELKSKEK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2033 QANGLNQENeralgaiqRQVKEINslqsdftKYLTSADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDKVREL- 2111
Cdd:TIGR04523 497 ELKKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDLEDELn 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2112 SRSAGKTSLVEEAEKhaqslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESALQTVIK 2191
Cdd:TIGR04523 549 KDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEKQELID 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2192 E------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRGIqrgdida 2265
Cdd:TIGR04523 593 QkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI------- 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 2266 mISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGSTQNE-----DFKKALTDADNSVNK 2323
Cdd:TIGR04523 665 -IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNFNK 739
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1247-1289 |
9.78e-15 |
|
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: 70.46 E-value: 9.78e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 1247 PCECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYGFP 1289
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1811-2358 |
1.04e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1811 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEK 1890
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1891 AQVNSRKAQTLYNNVNRA---IQSAKELDMKIKTVIRNVHILLK---QISGPDG---EGNNVPSG-EFSREWAEAQRM-M 1959
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEGyEAAIEAALGGRLqA 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1960 RELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRAR---- 2023
Cdd:TIGR02168 550 VVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvv 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2024 --LQEAAARAKQANGLN------------------QENERALGAIQRQvKEINSLQSDFTKyltsADSSLLQTNIALQLM 2083
Cdd:TIGR02168 629 ddLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERR-REIEELEEKIEE----LEEKIAELEKALAEL 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2084 EKSQKEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHAQSLQELAKQLEEI---------KRNASGDELVRCA 2154
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAE 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2155 VDAATAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ----------- 2221
Cdd:TIGR02168 782 AEIEELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsed 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2222 --EVSPALSNLQQT-------LNIVTVQREVIATNLTTLRDGLRgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQ 2292
Cdd:TIGR02168 854 ieSLAAEIEELEELieeleseLEALLNERASLEEALALLRSELE-----ELSEELRELESKRSELRRELEELREKLAQLE 928
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 2293 TDVERIK---DTYGSTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2358
Cdd:TIGR02168 929 LRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3168-3295 |
1.23e-13 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 70.42 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3168 IRPRSLTGILIHIGSQPGK-HLGVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3240
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 3241 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIFVNHIPV 3295
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1248-1291 |
2.78e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.18 E-value: 2.78e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1248 CECHPAGATSPHCSPEGGQCPCRPNVIGRQCTRCATGHYG--FPHC 1291
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1821-2364 |
1.44e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1821 QLRLVKSQ--LQGLSASAGLLE-QMRHMETQA------KDLRNQLLNYRSTIS-----NHGSKIEGLERELTDLNQEFET 1886
Cdd:TIGR02168 178 ERKLERTRenLDRLEDILNELErQLKSLERQAekaeryKELKAELRELELALLvlrleELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1887 LQEKAQvnsrKAQTLYNNVNRAIQsakELDMKIKTVIRNVHILLKQISGPDGEgnnVPSGEFSREWAEAQRMMRELRNRN 1966
Cdd:TIGR02168 258 LTAELQ----ELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1967 FGKHLREAEADKRESQLLLNRIrtwQKTHQGENNGLANSiRDSLNEYEAKLSDLRARLQEAAARAKQA-NGLNQENERal 2045
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEEL---KEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQLeLQIASLNNE-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2046 gaIQRQVKEINSLQ----------SDFTKYLTSADSSLLQTNIAL--QLMEKSQKEYE-------KLAASLNEARQELSD 2106
Cdd:TIGR02168 402 --IERLEARLERLEdrrerlqqeiEELLKKLEEAELKELQAELEEleEELEELQEELErleealeELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2107 KVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNASGD-----ELVRCAVDAATAYEN----ILNAIkaaedaanr 2177
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIlgvlsELISVDEGYEAAIEAalggRLQAV--------- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2178 AASASESALQTVikeDLPRKAKT-------LSSNSDKLLNEAKMTQKKLKQEVSPALSNLQQTLNIVTV------QREVI 2244
Cdd:TIGR02168 551 VVENLNAAKKAI---AFLKQNELgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllGGVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2245 ATNLTT---LRDGLRGIQR-----GDIdamISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGstQNEDFKKALTD 2316
Cdd:TIGR02168 628 VDDLDNaleLAKKLRPGYRivtldGDL---VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEE--KIAELEKALAE 702
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 982311033 2317 ADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNMDRIRELIQQARD 2364
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQ---ISALRKDLARLEAEVEQLEE 747
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1338-1389 |
1.46e-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: 64.30 E-value: 1.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1389
Cdd:pfam00053 1 CDCNPHGSLSD---TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1817-2268 |
1.53e-12 |
|
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: 74.00 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1817 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSTISNHGSKIEGLERELTDLNQEF-ETLQEKAQVNs 1895
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQFS- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1896 rkaqtlynnvnraiQSAKELDMKIKTVIRNVHILLKQISgPDGEGNNvpsgefsREWAE-------AQRMMRELRNRNFG 1968
Cdd:pfam15921 370 --------------QESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1969 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAARAKQANGL 2037
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2038 NQENERALGAIQRQVKEINS---LQSDFTKYLTSADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2114
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2115 AG-----KTSLVEEAEKHAQSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2170
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2171 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALSNLQQTLNI-------------- 2236
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkv 728
|
490 500 510
....*....|....*....|....*....|...
gi 982311033 2237 -VTVQREVIAtnlttlrdglrgiQRGDIDAMIS 2268
Cdd:pfam15921 729 aMGMQKQITA-------------KRGQIDALQS 748
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
514-556 |
4.63e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 4.63e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 514 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 556
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1811-2145 |
4.97e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1811 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQL--------LNYRSTISNHGSKIEGLERELTDLNQ 1882
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1883 EFETLQEK-----AQVNSRKAQTLYNNVNRAIQSAKELDMkiktVIRNVHILLKQISGPDGEGNNVP------------- 1944
Cdd:COG4717 214 ELEEAQEEleeleEELEQLENELEAAALEERLKEARLLLL----IAAALLALLGLGGSLLSLILTIAgvlflvlgllall 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1945 SGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQkthqgENNGLANSIRDsLNEYEAKLSDLRARL 2024
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEE-LQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2025 QEAAARAKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTSADSSLLQTNIALQLmEKSQKEYEKLAASLN 2098
Cdd:COG4717 364 QLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELE 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 982311033 2099 EARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNA 2145
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1386-1436 |
5.16e-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: 5.16e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1386 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANPKGCT 1436
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
515-558 |
6.33e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 6.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 515 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 558
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1338-1383 |
6.59e-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: 6.59e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1383
Cdd:cd00055 2 CDCNGHGSLSG---QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
470-517 |
6.75e-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: 62.37 E-value: 6.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 470 CDCNPEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 517
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1387-1435 |
6.88e-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: 62.37 E-value: 6.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1387 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANPKGC 1435
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1338-1384 |
1.87e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.87e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1338 CNCSRRGTSEAamlQCDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1384
Cdd:smart00180 1 CDCDPGGSASG---TCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1668-1714 |
3.64e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.64e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1668 PCNCNGH---SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1714
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
469-510 |
3.68e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.68e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 469 RCDCNPEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 510
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| LamG |
smart00282 |
Laminin G domain; |
2417-2552 |
4.38e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.13 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2417 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDRETELQVDQiltesetqEAVMD----RVKFQRIYQFARL--NYTKGAT 2490
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 2491 SSKPEipgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLRFPPYKGCIELDDLNEN 2552
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1820-2167 |
4.88e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1899
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1900 TLYNNVNRAIQSAKELDMKIKTVIRNVHILLKQISGpdgegnnvpsGEFSREWAEAQRMMRELRNRNFGKHLREAEAD-K 1978
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEE----------LEEELEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1979 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEinsl 2058
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA---- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2059 qsdftkyLTSADSSLLQtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQL 2138
Cdd:COG1196 444 -------LEEAAEEEAE---LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350
....*....|....*....|....*....|...
gi 982311033 2139 EEIKRNA----SGDELVRCAVDAATAYENILNA 2167
Cdd:COG1196 514 LLLAGLRglagAVAVLIGVEAAYEAALEAALAA 546
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-472 |
5.85e-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: 5.85e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFPFCLRCDC 472
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1813-2369 |
6.57e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1813 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSTISNHGSKIE---GLERELTDLNQEFETLQ- 1888
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKd 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1889 --EKAQVNSRKAQTLYNNVNRAIQSAKELDMKIKTVIRNvhillKQIsgpDGEGNNVPSGEFSREWAEAQRMMRELRN-- 1964
Cdd:TIGR04523 233 niEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE-----KQK---ELEQNNKKIKELEKQLNQLKSEISDLNNqk 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1965 -----RNFGKHLREAEADKRESQlllNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRA----RLQEAAARAKQAN 2035
Cdd:TIGR04523 305 eqdwnKELKSELKNQEKKLEEIQ---NQIS--------QNNKIISQLNEQISQLKKELTNSESenseKQRELEEKQNEIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2036 GLNQENERALGAIQRQVKEINSLQSDFTKYltSADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQELSDKVRElsr 2113
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSEIKDLTNQ--- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2114 sagKTSLVEEAEKHAQSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASESALQTVIKE- 2192
Cdd:TIGR04523 449 ---DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKEKELKKLNEEk 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2193 --------DLPRKAKTLSSNSDKLlnEAKMTQKKLKqevspaLSNLQQTLNivtvqreVIATNLTtlRDGLRGIQRGdID 2264
Cdd:TIGR04523 506 keleekvkDLTKKISSLKEKIEKL--ESEKKEKESK------ISDLEDELN-------KDDFELK--KENLEKEIDE-KN 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2265 AMISSAK---SMVRKANDITDEVLDGLNPIQTDVERIKDTYGSTQNEdFKKALTDADNSVNKLTNKLPDLWRKIESINQQ 2341
Cdd:TIGR04523 568 KEIEELKqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS-LEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
570 580 590
....*....|....*....|....*....|..
gi 982311033 2342 llpLGNISDNMDRIR----ELIQQARDAASKV 2369
Cdd:TIGR04523 647 ---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
515-562 |
1.12e-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: 1.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 982311033 515 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1820-2336 |
1.30e-10 |
|
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: 67.76 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSTISNHGSKIEGLERELTDLNQEFETL-QEKAQVNSRK 1897
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLdQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1898 -AQTLYNNVNRAIQSAKELDMKIKTviRNVHILLKQIsgPDGEGNNVPSGEFSREWAEAQRMMRELRNRNfgKHLREAEA 1976
Cdd:TIGR00606 532 tTRTQMEMLTKDKMDKDEQIRKIKS--RHSDELTSLL--GYFPNKKQLEDWLHSKSKEINQTRDRLAKLN--KELASLEQ 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1977 DKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAARAKQANG-----------LNQENER 2043
Cdd:TIGR00606 606 NK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDENQS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2044 ALGAIQRQVK---EINSLQSDFTKYLTSADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT-S 2119
Cdd:TIGR00606 679 CCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqK 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2120 LVEEAEKHAQSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAK 2199
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2200 TLSSNSDKLLNEAKMTQkKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTlrdglRGIQRGDIDAMISSAKSMVRKAND 2279
Cdd:TIGR00606 833 EKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR-----RQQFEEQLVELSTEVQSLIREIKD 906
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2280 ITDEVLDGLNPIQTDVERiKDTYGSTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2336
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.32e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 1.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-512 |
1.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 470 CDCNPEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 512
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2372-2550 |
2.21e-10 |
|
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: 61.67 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2372 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDRET 2451
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2452 ELQVDQILTESETQeavmdRVKFQRIYQFARL--NYTKGATSSKPEipgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDF 2529
Cdd:cd00110 70 VLSSKTPLNDGQWH-----SVSVERNGRSVTLsvDGERVVESGSPG-----------GSALLNLDGP---LYLGGLPEDL 130
|
170 180
....*....|....*....|.
gi 982311033 2530 KLPSRLRFPPYKGCIELDDLN 2550
Cdd:cd00110 131 KSPGLPVSPGFVGCIRDLKVN 151
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1835-2364 |
2.36e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 66.74 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1835 SAGLLEQMRHMETQAKDLRNQL-----------LNYRSTisnhGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLY 1902
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLdeeeaarqklqLEKVTT----EAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1903 NNVNRAIQSAKELDmKIKT----VIRNVHILLKQISGP-----------DGEgnnvpSGEFSREWAEAQRMMRELRnrnf 1967
Cdd:pfam01576 166 SNLAEEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1968 gkhlreAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARL-QEAAARAKQanglnQENERA 2044
Cdd:pfam01576 236 ------AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDLeSERAARNKA-----EKQRRD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2045 LGaiqrqvKEINSLQsdftkylTSADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2124
Cdd:pfam01576 297 LG------EELEALK-------TELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2125 EKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2194
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2195 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALSNLQQT---LNIVTVQREVIATNLTTLRDGLRGIQrgdidamis 2268
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2269 saksmvrkanditdEVLDGLNPIQTDVERIKDTYGStQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2348
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTLQA-QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 982311033 2349 SDNMDRIRELIQQARD 2364
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1812-2143 |
2.59e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1812 LNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSTIsnHGSKIEGLERELTDLNQEFETLQEKA 1891
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1892 QVNSRKAQTLYNNVNRAIQSAKELDMKIKTVirnvhillkqisgPDGEGNNVPS--GEFSREWAEAQRMMRELRNRnfgk 1969
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDL-------------GEEEQLRVKEkiGELEAEIASLERSIAEKERE---- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1970 hLREAEADKRESQLLLNRIR---TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALG 2046
Cdd:TIGR02169 317 -LEDAEERLAKLEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2047 AIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQKEyekLAASLNEARQELSDKVRELSRSAGKTSLVE-EAE 2125
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQLAADLSKYEqELY 472
|
330
....*....|....*...
gi 982311033 2126 KHAQSLQELAKQLEEIKR 2143
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQR 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1818-2358 |
3.08e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1818 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQefETLQEKAQVNSRK 1897
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLND--KLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1898 AQTlyNNVNRAIQSAKELDMKIKTVIRNvhiLLKQISGPDGEGNNVpSGEFSREWAEAQRMMRELRNRNFGKHLREAEAD 1977
Cdd:TIGR04523 103 SDL--SKINSEIKNDKEQKNKLEVELNK---LEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1978 KRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINS 2057
Cdd:TIGR04523 177 LLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2058 LQSDF----TKYLTSADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktSLVE 2122
Cdd:TIGR04523 244 KTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----ELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2123 EAEKHAQSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKAAEDAANRAASA-------SESALQTVIKEDLP 2195
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLKKELTNSESENSEkqreleeKQNEIEKLKKENQS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2196 RKA--KTLSSNSDKLLNEAKmTQKKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRgiqrgDIDAMISSAKSM 2273
Cdd:TIGR04523 382 YKQeiKNLESQINDLESKIQ-NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-----DLTNQDSVKELI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2274 VRKANDITDEvldglnpIQTDVERIKDTYGSTQN--EDFKKALTDADNSVNKLTNKLPDLWRKIESINQQllplgnISDN 2351
Cdd:TIGR04523 456 IKNLDNTRES-------LETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK------ISSL 522
|
....*..
gi 982311033 2352 MDRIREL 2358
Cdd:TIGR04523 523 KEKIEKL 529
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2779-2883 |
4.01e-10 |
|
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: 60.13 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2779 FQTFQPSGILL-SHQTWTSTLQVTLEDGHIELSTRDSGSP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQPL--RN 2853
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVvsSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 982311033 2854 NQRLNRISSSQQSLRLGG-------------SNFEGCISNVFV 2883
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
8.08e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 8.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 982311033 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAVGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1387-1435 |
8.91e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 8.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 1387 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHldpANPKGC 1435
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1716-1766 |
1.13e-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: 56.21 E-value: 1.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1716 CPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNPQKFGGSC 1766
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1669-1716 |
1.46e-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: 1.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1669 CNCNGH---SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1716
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1953-2169 |
2.03e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.50 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2026
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2027 AAARAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLTSADSS-----LLQTNIAlQLMEKSQKEYEKLAA 2095
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSARYTPNhpdviALRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2096 SLNEARQELSDKVRELSRSagktslVEEAEKHAQSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2169
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1950-2371 |
2.23e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1950 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAA 2029
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2030 RAKQANGLNQENERALGAIQRQVKEInslqsdftkyltsadssllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2109
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQL--------------------SLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2110 ELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2173
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2174 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALSNLQQTLNIVTVQRE-------V 2243
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQEiaallaeA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2244 IATNLTTLRDGLRGIQRgdidamissAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGSTQNEDFKKALTDADNSVNK 2323
Cdd:COG4717 380 GVEDEEELRAALEQAEE---------YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 982311033 2324 LTNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2371
Cdd:COG4717 451 LREEL----AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2608-2724 |
5.80e-09 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 56.94 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2608 IQTTVDRGLLFFAENRDR--FISLNIEDGKLMVRYKLNSEPPKERGvGDAINNGRDHSIQIKigKVQKRMWINVDfQNTI 2685
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTErdFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVELE--RNGRSGTLSVD-GEAR 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 982311033 2686 IDGEV-------FDFST-YYLGGIPIAI--RERFNISTPaFRGCMKNLK 2724
Cdd:pfam00054 77 PTGESplgattdLDVDGpLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1819-2262 |
7.54e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1819 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSTISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrka 1898
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1899 qtlynnVNRAIQSAKELDMKIKTVIRNVHILLKQIsgpdgegnnvpsgefsREWAEAQRMMRELRNRNFGKHLREAEADK 1978
Cdd:COG4717 127 ------LLPLYQELEALEAELAELPERLEELEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1979 RESQLLLNRIRTWQKTHQgennglanSIRDSLNEYEAKLSDLRARLQEAAARAKQAnglnqENERALGAIQRQVKEINSL 2058
Cdd:COG4717 185 QLSLATEEELQDLAEELE--------ELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2059 --------------QSDFTKYLTSADSSLLQTNIALQLMEKSQKEYEKLAASLNE-----ARQELSD-KVRELSRSAG-- 2116
Cdd:COG4717 252 lliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEElqalpALEELEEeELEELLAALGlp 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2117 ---KTSLVEEAEKHAQSLQELAKQLEEIKRNASGDE--------LVRCAVDAATAYENILNAIKAAEdaanraasaSESA 2185
Cdd:COG4717 332 pdlSPEELLELLDRIEELQELLREAEELEEELQLEEleqeiaalLAEAGVEDEEELRAALEQAEEYQ---------ELKE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 2186 LQTVIKEDLPRKAKTLSSNSDKLlneakmTQKKLKQEvspaLSNLQQTLNIVTVQREVIATNLTTLRDGLRGIQRGD 2262
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEAL------DEEELEEE----LEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1840-2142 |
8.01e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.92 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1840 EQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLYNNVNRAIQSA 1912
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1913 KELDMKIKTvirnvhiLLKQISGPDGEGNNVPSGEFSREwaEAQRMMRELRNRnfgkHLREA---EADKR---ESQLLLN 1986
Cdd:COG1340 81 DELNEKLNE-------LREELDELRKELAELNKAGGSID--KLRKEIERLEWR----QQTEVlspEEEKElveKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1987 RIRTWQKTHQGEnnglaNSIRDSLNEYEA---KLSDLRARLQEAAARAKQANGLNQEnerALGAIQRQVKEINSLQSDFT 2063
Cdd:COG1340 148 ELEKAKKALEKN-----EKLKELRAELKElrkEAEEIHKKIKELAEEAQELHEEMIE---LYKEADELRKEADELHKEIV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2064 KYLTSADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHA-QSLQELAKQ----L 2138
Cdd:COG1340 220 EAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAeEIFEKLKKGekltT 284
|
....
gi 982311033 2139 EEIK 2142
Cdd:COG1340 285 EELK 288
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1715-1767 |
1.09e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 982311033 1715 ACPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNPQKfGGSCQ 1767
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1788-2235 |
1.17e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1788 INQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRNQLLNYRS 1861
Cdd:TIGR00618 286 INRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIRDAHEVAT 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1862 TISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRAI-QSAKELDMKIKTVIRNVHILLKQISGPDGE- 1939
Cdd:TIGR00618 366 SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAa 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1940 -GNNVPSGEFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANSIRdslnE 2012
Cdd:TIGR00618 446 aITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGSCI----H 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2013 YEAKLSDL------RARLQEAAARAKQANGLNQENERALGAIQRQVK----EINSLQSDFTKyLTSADSSLLQT-NIALQ 2081
Cdd:TIGR00618 513 PNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAslkeQMQEIQQSFSI-LTQCDNRSKEDiPNLQN 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2082 LMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNASGDE----LVRCAVDA 2157
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehALSIRVLP 671
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2158 ATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALSNLQQTLN 2235
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-660 |
1.20e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFaleKSNYFGC 660
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
610-661 |
1.23e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.13 E-value: 1.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 661
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
610-660 |
1.44e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 610 CQCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 660
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1823-2141 |
1.65e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1823 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQtly 1902
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE--- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1903 nNVNRAIQSAKEldmkiktvirNVHILLKQISGPDGEGNNVPSgefSREWAEAQR-MMRELRNRNFGK------HLREAE 1975
Cdd:PRK02224 374 -EAREAVEDRRE----------EIEELEEEIEELRERFGDAPV---DLGNAEDFLeELREERDELREReaeleaTLRTAR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1976 ADKRESQLLLNRIRTWQKTHQGENNGLANSI---RDSLNEYEAKLSDLRA----------RLQEAAARAKQANGLNQENE 2042
Cdd:PRK02224 440 ERVEEAEALLEAGKCPECGQPVEGSPHVETIeedRERVEELEAELEDLEEeveeveerleRAEDLVEAEDRIERLEERRE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2043 RA--LGAIQRQVKE-----INSLQSDFTKYLTSADSsllQTNIALQLMEKSQKEYEKLAAsLNEARQELSDKVRELSRSA 2115
Cdd:PRK02224 520 DLeeLIAERRETIEekrerAEELRERAAELEAEAEE---KREAAAEAEEEAEEAREEVAE-LNSKLAELKERIESLERIR 595
|
330 340
....*....|....*....|....*.
gi 982311033 2116 GKTSLVEEAEKHAQSLQELAKQLEEI 2141
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAEL 621
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1716-1759 |
3.40e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 982311033 1716 CPCPHTNRFATGCVVNGGdvRCSCKAGYIGTQCERCAPGYFGNP 1759
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1822-2150 |
3.76e-08 |
|
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: 59.75 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1822 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQefeTLQEKaqv 1893
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEK--- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1894 nsrkaqtlynnvNRAIQSAKELDMKIKTvirNVHILLKQISGPDGEGNNVPSGE-----FSREWAEAQRMMRELRNR--N 1966
Cdd:pfam15921 509 ------------ERAIEATNAEITKLRS---RVDLKLQELQHLKNEGDHLRNVQteceaLKLQMAEKDKVIEILRQQieN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1967 F----GKHLREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAA-RAKQANGLN 2038
Cdd:pfam15921 574 MtqlvGQHGRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSeRLRAVKDIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2039 QENERALGAIQRQVKEINSLQSDF---------------------TKYLTSADSSLLQTNIALQLMEKSQKEYEKLAASL 2097
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982311033 2098 neaRQELSDKVRELSRSAGKTSLVEEA------EKH--AQSLQELAKQLEEI--KRNASGDEL 2150
Cdd:pfam15921 733 ---QKQITAKRGQIDALQSKIQFLEEAmtnankEKHflKEEKNKLSQELSTVatEKNKMAGEL 792
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1958-2150 |
4.04e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1958 MMRELRNRnFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGL------ANSIRDSLNEYEAKLSDLRARLQEAAARA 2031
Cdd:COG1340 9 SLEELEEK-IEELREEIEELKEKRDELNEELKELAEKRDELNAQVkelreeAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2032 KQ-------ANGLNQENERALGAIQRQVKEINSLQSDF-TKYLTSAD-------SSLLQTNI-ALQLMEKSQKEYEKLAA 2095
Cdd:COG1340 88 NElreeldeLRKELAELNKAGGSIDKLRKEIERLEWRQqTEVLSPEEekelvekIKELEKELeKAKKALEKNEKLKELRA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2096 SLNEARQELSDKVRELsrsagkTSLVEEAEKHAQSLQELAKQLEEIKRNAsgDEL 2150
Cdd:COG1340 168 ELKELRKEAEEIHKKI------KELAEEAQELHEEMIELYKEADELRKEA--DEL 214
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1669-1711 |
5.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 5.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 982311033 1669 CNCN--GH-SNRCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1711
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1930-2143 |
5.73e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1930 LKQISGPDgegnnvpsgEFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2007
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2008 DSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTSADSSLLQTNIA-LQLMEKS 2086
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2087 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHAQSLQELAKQLEEIKR 2143
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRleeeINGIEERIKELEEKEERLEELKKKLKELEK 352
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1869-2164 |
6.25e-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: 58.93 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1869 KIEGLERELTDLNQEFETLQekaqvnsrkaqtlyNNVNRAIQSAKELDMKIKTVIRNVHILLKQISGPDGEGNNVPS--G 1946
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIE--------------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1947 EFSREWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLQ 2025
Cdd:TIGR02169 748 SLEQEIENVKSELKELEAR-----IEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2026 EAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALqlmeksqKEYEKLAASLNEARQELS 2105
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2106 DKVRELSRSAGKTSL-VEEAEKHAQSLQE----LAKQLEEIKRN-ASGDELVRCAVDAATAYENI 2164
Cdd:TIGR02169 896 AQLRELERKIEELEAqIEKKRKRLSELKAkleaLEEELSEIEDPkGEDEEIPEEELSLEDVQAEL 960
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1838-2334 |
1.05e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1838 LLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLYNNvnraiQSAKELD 1916
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1917 MKIKtvirnvhillkqisgpdgegnnvpsgefsrewaEAQRMMRELRnrnfgKHLREAEADKREsqllLNRIRtWQKTHQ 1996
Cdd:PRK03918 259 EKIR---------------------------------ELEERIEELK-----KEIEELEEKVKE----LKELK-EKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1997 GENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKY------LTSAD 2070
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeakakKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2071 SslLQTNIALQLMEKSQKEYEKLA-----------------ASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH- 2127
Cdd:PRK03918 376 R--LKKRLTGLTPEKLEKELEELEkakeeieeeiskitariGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKEl 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2128 -----------AQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPR 2196
Cdd:PRK03918 454 leeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2197 KAK---TLSSNSDKLLNEAKMTQKKLKQEvsPALSNLQQTLN--IVTVQREviatnLTTLRDGLRGIQRGDIDAMissaK 2271
Cdd:PRK03918 523 KAEeyeKLKEKLIKLKGEIKSLKKELEKL--EELKKKLAELEkkLDELEEE-----LAELLKELEELGFESVEEL----E 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2272 SMVRKANDITDEVLDgLNPIQTDVERIKDTYGSTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2334
Cdd:PRK03918 592 ERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1820-2143 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLSASAGLLEQMrhmETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQ---EFETLQEKAQvNSR 1896
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEEL---EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAE-EYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1897 KAQTLYNNVNRAIQSAKELDMKIKTVIRNVHILLKQISGPDGEGNNVpSGEFS---------REWAEAQRM-------MR 1960
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-KKKLKelekrleelEERHELYEEakakkeeLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1961 ELRNRNFG-------KHLREAEADKRESQLLLNRIRTwqktHQGENNGLANSIRDSLNE--------------------- 2012
Cdd:PRK03918 376 RLKKRLTGltpekleKELEELEKAKEEIEEEISKITA----RIGELKKEIKELKKAIEElkkakgkcpvcgrelteehrk 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2013 -----YEAKLSDLRARLQEAAARakqanglnqenERALGAIQRQVKEINSLQSDFTKYLTSAD------SSLLQTNiaLQ 2081
Cdd:PRK03918 452 elleeYTAELKRIEKELKEIEEK-----------ERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LE 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 2082 LMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKhaqSLQELAKQLEEIKR 2143
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK---KLDELEEELAELLK 577
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1971-2289 |
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 982311033 1971 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQR 2050
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2051 QVKEinsLQSDFTKyLTSADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQS 2130
Cdd:COG4372 109 EAEE---LQEELEE-LQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2131 LQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLN 2210
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 2211 EAKMTQKKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRGIQRGDIDAMISSAKSMVRKANDITDEVLDGLN 2289
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
564-607 |
2.45e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 2.45e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 982311033 564 ACDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNLDKENPNGC 607
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
298-344 |
3.94e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 3.94e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 982311033 298 RCVCNGHA---EVCNANNpeklFRCQCQHHTCGETCDRCCTGYNQRRWQP 344
Cdd:cd00055 1 PCDCNGHGslsGQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
2982-3120 |
4.42e-07 |
|
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: 52.00 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2982 KLPQELLkPRSQFAVDV-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3055
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 3056 GHDGEKGRLVVDGLRAREGSLPGNSTVSLRGPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3120
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2009-2148 |
6.25e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 53.46 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2009 SLNEYEAKLSDLRARLQEAAARAKQANGLNQEN----ERA---LGAIQRQVKEINS-LQSDFTKYLTSADSSLLQTNIAL 2080
Cdd:pfam12795 79 SLEELEQRLLQTSAQLQELQNQLAQLNSQLIELqtrpERAqqqLSEARQRLQQIRNrLNGPAPPGEPLSEAQRWALQAEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2081 QLMEKSQKEYEKLAASLNeARQELSDKVRELsrsagKTSLVEEAEKHAQSLQEL------------AKQLEEIKRNASGD 2148
Cdd:pfam12795 159 AALKAQIDMLEQELLSNN-NRQDLLKARRDL-----LTLRIQRLEQQLQALQELlnekrlqeaeqaVAQTEQLAEEAAGD 232
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
663-706 |
6.30e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 6.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYYFPDLH 706
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1820-2156 |
7.15e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLSASA--GLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRK 1897
Cdd:COG4372 16 FGLRPKTGILIAALSEQlrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1898 AQTLYNNVNRAIQSAKELDMKIKTVIRNVHILLKQisgpdgegnnvpsgefsrewaeAQRMMRELRNRNFGKHLREAEAD 1977
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQ----------------------RKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1978 KRESQL--LLNRIRTWQKTHQGENNGLANSIRDSLneyeakLSDLRARLQEAAARAKQANGLNQENERALGAIQRQV--- 2052
Cdd:COG4372 154 ELEEQLesLQEELAALEQELQALSEAEAEQALDEL------LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKdsl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2053 --KEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQS 2130
Cdd:COG4372 228 eaKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
330 340
....*....|....*....|....*.
gi 982311033 2131 LQELAKQLEEIKRNASGDELVRCAVD 2156
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALA 333
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1839-2364 |
7.37e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1839 LEQMRHMETQAKDLRNQLLNYRS---TISNHGSKIEGLERELTDLNQEFETLQEK-AQVNSR------KAQTLYNNVNRa 1908
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKiRELEERieelkkEIEELEEKVKE- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1909 iqsAKELDMKIKTVIRNVHILLKQISgpdgEGNNVPSGE--FSREWAEAQRMMRELRNRNfgKHLREAEADKRESQLLLN 1986
Cdd:PRK03918 285 ---LKELKEKAEEYIKLSEFYEEYLD----ELREIEKRLsrLEEEINGIEERIKELEEKE--ERLEELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1987 RIRTWQKTHQgenngLANSIRDSLNEYEAKLSDLR----ARLQEAAARAKqanglnQENERALGAIQRQVKEINSLQSDF 2062
Cdd:PRK03918 356 ELEERHELYE-----EAKAKKEELERLKKRLTGLTpeklEKELEELEKAK------EEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2063 TKYLTSADSS---------LLQTNIALQLMEKSQKEYEKLAASLnearQELSDKVRELSRSAGKTSLVEEAEKHAQSLQE 2133
Cdd:PRK03918 425 KKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRIEKEL----KEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2134 LAKQLEEIKRNASG---DELVRcavdAATAYENI---LNAIKAAedaanraasasesalQTVIKEDLpRKAKTLSSNSDK 2207
Cdd:PRK03918 501 LAEQLKELEEKLKKynlEELEK----KAEEYEKLkekLIKLKGE---------------IKSLKKEL-EKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2208 LLNEAKMTQKKLKqEVSPALSNLQ-QTLNIV--TVQR-EVIATNLTTLRDGLRGIQRgdIDAMISSAKSMVRKANDITDE 2283
Cdd:PRK03918 561 LEKKLDELEEELA-ELLKELEELGfESVEELeeRLKElEPFYNEYLELKDAEKELER--EEKELKKLEEELDKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2284 VLDGLNPIQTDVERIKDTYGSTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIR---ELIQ 2360
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkelEKLE 717
|
....
gi 982311033 2361 QARD 2364
Cdd:PRK03918 718 KALE 721
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2020-2235 |
7.75e-07 |
|
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: 54.05 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2020 LRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQS----------------DFTKYLTSADSSllQTNI---AL 2080
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSAsvaslekqlleltrvnELLKAKFSEDGT--QKKMsslSM 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2081 QLM------EKSQKEY----EKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHAQSLQELAKQLEEIKR-NASGDE 2149
Cdd:pfam15905 160 ELMklrnklEAKMKEVmakqEGMEGKLQVTQKNLEHSKGKVAQLEEK--LVSTEKEKIEEKSETEKLLEYITElSCVSEQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2150 LVRCAVDAATAyENILNAIKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLSN 2229
Cdd:pfam15905 238 VEKYKLDIAQL-EELLKEKNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEE 311
|
....*.
gi 982311033 2230 LQQTLN 2235
Cdd:pfam15905 312 LKEKLT 317
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1947-2152 |
9.84e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1947 EFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2013
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2014 EAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQK----- 2088
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982311033 2089 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHAQSLQELAKQLEEIKRNASGD---ELVR 2152
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1820-2142 |
1.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE---KAQVNSR 1896
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1897 ------KAQTL--Y----NNVNRAIQSAKELDMKIKTVIRNVHILLKQISgpdgegnnvpsgEFSREWAEAQRMmRELRN 1964
Cdd:PRK03918 444 elteehRKELLeeYtaelKRIEKELKEIEEKERKLRKELRELEKVLKKES------------ELIKLKELAEQL-KELEE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1965 RNFGKHLREAEADKRESQLLLNRIRTWQkthqGENNGLANSIRdSLNEYEAKLSDLRARLQEAaaRAKQANGLNQENERA 2044
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIKLK----GEIKSLKKELE-KLEELKKKLAELEKKLDEL--EEELAELLKELEELG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2045 LGAIQRQVKEINSLQSDFTKYLTSADS-----------SLLQTNI--ALQLMEKSQKEYEKLAASLNEARQ--------E 2103
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAekelereekelKKLEEELdkAFEELAETEKRLEELRKELEELEKkyseeeyeE 663
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2104 LSDKVRELSRS-AGKTSLVEEAEKHAQS-------------------------------LQELAKQLEEIK 2142
Cdd:PRK03918 664 LREEYLELSRElAGLRAELEELEKRREEikktleklkeeleerekakkeleklekalerVEELREKVKKYK 734
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1843-2234 |
1.30e-06 |
|
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: 54.46 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1843 RHMETQAKDlRNQLLN---YRSTISNHGSKIEGLERELTDLNQEFetlqekAQVNSrkAQTLYNnVNRAIQSAKELDMKI 1919
Cdd:pfam12128 126 RFMKNAGIQ-RTNLLNtreYRSIIQNDRTLLGRERVELRSLARQF------ALCDS--ESPLRH-IDKIAKAMHSKEGKF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1920 KTVIRNVHILLKQisgpdgEGNNVPSGEFSRewaeaQRMMRELRNRNfgkHLREAEADKRESQLLLNRIRTWQKTH---Q 1996
Cdd:pfam12128 196 RDVKSMIVAILED------DGVVPPKSRLNR-----QQVEHWIRDIQ---AIAGIMKIRPEFTKLQQEFNTLESAElrlS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1997 GENNGLANSIRDS----------LNEYEAKLSDLRARLQEAAARakqangLNQENERALGAIQRQVKEINSLQSDFTKYL 2066
Cdd:pfam12128 262 HLHFGYKSDETLIasrqeerqetSAELNQLLRTLDDQWKEKRDE------LNGELSAADAAVAKDRSELEALEDQHGAFL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2067 T------SADSSLL-QTNIALQLMEKSQKEYEKLAASLNEARQEL-----SDKVRELSR--------SAGKTSLVEEAEK 2126
Cdd:pfam12128 336 DadietaAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRrskikEQNNRDIAGikdklakiREARDRQLAVAED 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2127 HAQSL-QELAKQLEEIKRNASGDEL--------VRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVikEDLP-- 2195
Cdd:pfam12128 416 DLQALeSELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQLENFDERIERAREEQEAANAEV--ERLQse 493
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 982311033 2196 -RKAKTLSSNSDKLLNEAKMTQKKLKQevspALSNLQQTL 2234
Cdd:pfam12128 494 lRQARKRRDQASEALRQASRRLEERQS----ALDELELQL 529
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1814-2138 |
1.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1814 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE 1889
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1890 KAQVNSRkaQTLYNNVNRAIQSAKEldmkiktvirnvhillkqisgpdgegnnvpsgefsrewaeaqrmmRELRnRNFGK 1969
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVE---------------------------------------------RELR-ENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1970 HLREAEADK-RESQLLLNRIRTWQKTHQGENNGLANSIrDSLNEYEAKLSDLRA----RLQEAAARAKQAN------GLN 2038
Cdd:COG4913 774 RIDALRARLnRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEdglpEYEERFKELLNENsiefvaDLL 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2039 QENERALGAIQRQVKEIN-SL-QSDFtkyltSADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAG 2116
Cdd:COG4913 853 SKLRRAIREIKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGAS 911
|
330 340
....*....|....*....|..
gi 982311033 2117 KTSLvEEAEKHAQSLQELAKQL 2138
Cdd:COG4913 912 LFDE-ELSEARFAALKRLIERL 932
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
663-701 |
1.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.66e-06
10 20 30
....*....|....*....|....*....|....*....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYY 701
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1820-2150 |
2.10e-06 |
|
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: 54.03 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRL----VKSQLQGlsASAGLLEQMRHMETQAKDLRNQLlnyrstisnhGSKIEGLERELTDLNQEfeTLQE-KAQVN 1894
Cdd:pfam01576 200 EKGRQelekAKRKLEG--ESTDLQEQIAELQAQIAELRAQL----------AKKEEELQAALARLEEE--TAQKnNALKK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1895 SRKAQTLYNNVNRAIQSAKELDMKIKTVIRNVhillkqisgpdGEGNNVPSGEF--SREWAEAQRMMRELRNRNFG--KH 1970
Cdd:pfam01576 266 IRELEAQISELQEDLESERAARNKAEKQRRDL-----------GEELEALKTELedTLDTTAAQQELRSKREQEVTelKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1971 LREAEADKRESQLLLNRIR--------------------TWQKTHQG---ENNGLANSIRdSLN----EYEAKLSDLRAR 2023
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKhtqaleelteqleqakrnkaNLEKAKQAlesENAELQAELR-TLQqakqDSEHKRKKLEGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2024 LQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSD-------FTKYLTSADSSLLQTNIALQ--------------- 2081
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegknikLSKDVSSLESQLQDTQELLQeetrqklnlstrlrq 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2082 -------LMEKSQKEYEK---LAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQS-LQELAKQLEEikRNASGDEL 2150
Cdd:pfam01576 494 ledernsLQEQLEEEEEAkrnVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQReLEALTQQLEE--KAAAYDKL 571
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1953-2225 |
2.36e-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: 53.49 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRA------ 2022
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAelaaym 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2023 --RLQEAAARAKQANGLNQENERALGAIQRQVKEIN-SLQ--SDFTKYLTSADSSLlqtnialqlmeKSQKEYEKlaASL 2097
Cdd:pfam05701 271 esKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2098 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHAQS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2169
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 2170 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2225
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1840-2072 |
2.45e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1840 EQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQE---KAQVNSRKAQTLYNNVNRAIQ----SA 1912
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaEAEAEIEERREELGERARALYrsggSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1913 KELDM-----KIKTVIRNVHiLLKQISGPDgegnnvpsgefsrewaeaQRMMRELRNRnfgkhLREAEADKRESQLLLNR 1987
Cdd:COG3883 103 SYLDVllgseSFSDFLDRLS-ALSKIADAD------------------ADLLEELKAD-----KAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1988 IRTWQKthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT 2067
Cdd:COG3883 159 LEALKA----ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*
gi 982311033 2068 SADSS 2072
Cdd:COG3883 235 AAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1807-2120 |
2.54e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1807 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFE 1885
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1886 TLQ---EKAQVNSRKAQTLYNNVNRAIQSAKELDmkiktvirNVHILLKQisgpdgegnnvpsgefsREWAEAQRMMREL 1962
Cdd:COG4942 87 ELEkeiAELRAELEAQKEELAELLRALYRLGRQP--------PLALLLSP-----------------EDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1963 RnrnfgkhlreaeadkresqlllnrirtwqkthqgennGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENE 2042
Cdd:COG4942 142 K-------------------------------------YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2043 RALGAIQRQVKEINSLqsdftkyLTSADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL 2120
Cdd:COG4942 185 EERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1974-2185 |
2.85e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1974 AEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVK 2053
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2054 E------INSLQSDFTKYLTSADS--------SLLQT-----NIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrs 2114
Cdd:COG3883 90 EraralyRSGGSVSYLDVLLGSESfsdfldrlSALSKiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELE-- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2115 agktSLVEEAEKHAQSLQELAKQLEEIKRNASgDELVRCAVDAATAYENILNAIKAAEDAANRAASASESA 2185
Cdd:COG3883 168 ----AAKAELEAQQAEQEALLAQLSAEEAAAE-AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1904-2370 |
3.57e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 52.72 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1904 NVNRAIQSAKELDMKIKTVIRNVHILLKQISGPDGEGNNVPSGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL 1983
Cdd:COG0840 44 ALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1984 LLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFT 2063
Cdd:COG0840 124 LAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2064 KYLTSADSSLLQT-------NIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHAQSLQELAK 2136
Cdd:COG0840 204 RSITRPLRELLEVleriaegDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2137 QLEEIKRNASgdelvrcavDAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQ 2216
Cdd:COG0840 282 GAEEQAASLE---------ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2217 KKLKQEVSPALSNLQQtLN--------IVTVQREvIA--TNLTTL-------RDGLRGiqRG------------------ 2261
Cdd:COG0840 340 EEIRESVEETAETIEE-LGessqeigeIVDVIDD-IAeqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaea 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2262 --DIDAMISSAKSMVRKANDITDEVldglnpiqtdVERIKDtyGSTQNEDFKKALTDADNSVNKLTNKLpdlwRKI-ESI 2338
Cdd:COG0840 416 tkEIEELIEEIQSETEEAVEAMEEG----------SEEVEE--GVELVEEAGEALEEIVEAVEEVSDLI----QEIaAAS 479
|
490 500 510
....*....|....*....|....*....|..
gi 982311033 2339 NQQLLPLGNISDNMDRIRELIQQARDAASKVA 2370
Cdd:COG0840 480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVA 511
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
3.78e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 3.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 356 CNCHGHAS---DCYydsdverqqaslntqgiyAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSlsdTCD------------------PETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2009-2310 |
3.88e-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: 52.65 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2009 SLNEYEAKLS-------DLR-ARLQEAAARAKQangLNQENERALGAIQRQVKEIN-SLQSDFTKYLTSADSSLLQTNIA 2079
Cdd:COG5185 247 DLAQTSDKLEklveqntDLRlEKLGENAESSKR---LNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2080 LQLMEKSQKEYE-----------KLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNASGD 2148
Cdd:COG5185 324 EQELEESKRETEtgiqnltaeieQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2149 ELVrcavdaatAYENILNAIKAAEDAANRAASASESALQTVikEDLPRKAKTLSSNSDKLLNEAK-MTQKKLKQEVSPAL 2227
Cdd:COG5185 404 AQE--------ILATLEDTLKAADRQIEELQRQIEQATSSN--EEVSKLLNELISELNKVMREADeESQSRLEEAYDEIN 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2228 SNLQQTLNIVTVQREVIATNLTTLRDGLRGiQRGDIDAMISSAKSMVRK-ANDITD-EVLDGLNPIQTDVERIKDTYGST 2305
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTLKATLEK-LRAKLERQLEGVRSKLDQvAESLKDfMRARGYAHILALENLIPASELIQ 552
|
....*
gi 982311033 2306 QNEDF 2310
Cdd:COG5185 553 ASNAK 557
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1790-2058 |
4.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1790 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSTISNHGSK 1869
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1870 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRAIQSAKELDMKIKTV------IRNVHILLKQISgpdgegNNV 1943
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkeriesLERIRTLLAAIA------DAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1944 PSGEFSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDlraR 2023
Cdd:PRK02224 606 DEIERLREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYLEQVEE---K 668
|
250 260 270
....*....|....*....|....*....|....*
gi 982311033 2024 LQEaaARAKQANGLNQeneraLGAIQRQVKEINSL 2058
Cdd:PRK02224 669 LDE--LREERDDLQAE-----IGAVENELEELEEL 696
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1868-2111 |
4.24e-06 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 51.47 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1868 SKIEGLERELTDLNQEFETLQEK-----AQVNSRKA-QTLYNNVNR---AIQSAKELDMKIKTVIRNVHILLKQISGPDG 1938
Cdd:pfam13949 38 EILDEAEKLLDEEESEDEQLRAKygtrwTRPPSSELtATLRAEIRKyreILEQASESDSQVRSKFREHEEDLELLSGPDE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1939 EGNN-VPSGEFSREWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYE--- 2014
Cdd:pfam13949 118 DLEAfLPSSRRAKNSPSVEEQVAKLREL-----LNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQEeql 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2015 -----AKLSDLRARLQEAAARakqanglnQENeralgaIQRQVKEINSlqsDFTKYLTSADSSLLQTNIALQLMEKSQKE 2089
Cdd:pfam13949 193 feeelEKYDPLQNRLEQNLHK--------QEE------LLKEITEANN---EFLQDKRVDSEKQRQREEALQKLENAYDK 255
|
250 260
....*....|....*....|....*
gi 982311033 2090 YEKLAASLNEARQ---ELSDKVREL 2111
Cdd:pfam13949 256 YKELVSNLQEGLKfynDLTEILEKL 280
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1815-2248 |
5.82e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1815 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLN----- 1881
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1882 --QEFETLQEKAQVNSRKAQTLYNNVN--RAIQSAKE--LDMKIKTVIRnvhiLLKQISGPDGEGNNVpsgefsrewaea 1955
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsfLNKKTKQLQD----LTEEKSTLAGEIRDL------------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1956 qRMMRELRNRNFG------KHLREAEADKrESQL--LLNRIRTWQKTHQGENNGLAnSIRDSLNEYE--------AKLSD 2019
Cdd:pfam10174 386 -KDMLDVKERKINvlqkkiENLQEQLRDK-DKQLagLKERVKSLQTDSSNTDTALT-TLEEALSEKEriierlkeQRERE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2020 LRARLQEAAARAKQanglNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLME----KSQKEYEKLAA 2095
Cdd:pfam10174 463 DRERLEELESLKKE----NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiaveQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2096 SLNEARQ---------ELSDKVRELSRSAgkTSLVEEAEKhAQS----LQELAKQLEEIK--RNASGDELVRCAVDAATA 2160
Cdd:pfam10174 539 QLKKAHNaeeavrtnpEINDRIRLLEQEV--ARYKEESGK-AQAeverLLGILREVENEKndKDKKIAELESLTLRQMKE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2161 yENILNAIKAAEDAANRAASASEsaLQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALSNLQQTLNivtvQ 2240
Cdd:pfam10174 616 -QNKKVANIKHGQQEMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRQEL-DATKARLSSTQQSLA----E 687
|
....*...
gi 982311033 2241 REVIATNL 2248
Cdd:pfam10174 688 KDGHLTNL 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1838-2265 |
7.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1838 LLEQMRHMETQAKDLRNQLLNYRstisnhgsKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRAIQSAKELDM 1917
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTR--------RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1918 KIKTVIRNVHILLK--QISGPDGEGNnvpsgefsrewAEAQRMMRELRNRnfgkHLREaeadKRESQLLLNRIRTWQKTH 1995
Cdd:TIGR00618 578 CDNRSKEDIPNLQNitVRLQDLTEKL-----------SEAEDMLACEQHA----LLRK----LQPEQDLQDVRLHLQQCS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1996 QGENNGLAnsirdSLNEYEAKLSDLRARLQEAAARAKQANgLNQENERALGAIQRQVKEinslqsdftkyLTSADSSLLQ 2075
Cdd:TIGR00618 639 QELALKLT-----ALHALQLTLTQERVREHALSIRVLPKE-LLASRQLALQKMQSEKEQ-----------LTYWKEMLAQ 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2076 TNIALQLMEKSQKEYEKLaaslneaRQELsdkvrELSRSAGKTSLVEEAEKHAQSLQELAKQ-------LEEIKRNASGD 2148
Cdd:TIGR00618 702 CQTLLRELETHIEEYDRE-------FNEI-----ENASSSLGSDLAAREDALNQSLKELMHQartvlkaRTEAHFNNNEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2149 ELVRCAVDA--ATAYENILNAIKaAEDAANRAASASESALQTVIKEDLprKAKTLS--------SNSDKLLNEAKMTQKK 2218
Cdd:TIGR00618 770 VTAALQTGAelSHLAAEIQFFNR-LREEDTHLLKTLEAEIGQEIPSDE--DILNLQcetlvqeeEQFLSRLEEKSATLGE 846
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 982311033 2219 LKQEVSPALSNLQQTLNIVTVQREviatnLTTLRD---GLRGIQrGDIDA 2265
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAK-----IIQLSDklnGINQIK-IQFDG 890
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
663-701 |
8.53e-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: 8.53e-06
10 20 30
....*....|....*....|....*....|....*....
gi 982311033 663 CQCDVGGALSSVCSGPSGVCQCREHVVGKACQRPENNYY 701
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2004-2147 |
9.55e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2004 NSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSS----------- 2072
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2073 LLQTNIA------LQLMEK---SQKEYEKLAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKHAQSL-QELAKQ 2137
Cdd:COG1579 100 SLKRRISdledeiLELMERieeLEEELAELEAELAELEAELEEKKAELDEELAELeaeleELEAEREELAAKIpPELLAL 179
|
170
....*....|
gi 982311033 2138 LEEIKRNASG 2147
Cdd:COG1579 180 YERIRKRKNG 189
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2012-2149 |
1.06e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.44 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2012 EYEAKLSDLRARLQEAAARAKQAngLNQENE----RALGAIQRQVKEINSLQSDFTKYLTSADSslLQTNIAlQLMEK-S 2086
Cdd:COG1842 55 RLERQLEELEAEAEKWEEKARLA--LEKGREdlarEALERKAELEAQAEALEAQLAQLEEQVEK--LKEALR-QLESKlE 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 2087 QKEYEKLAASLNEARQELSDKVRELSRSAGKTSL----------VEEAEKHAQSLQELA------KQLEEIKRNASGDE 2149
Cdd:COG1842 130 ELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDAtsalermeekIEEMEARAEAAAELAagdsldDELAELEADSEVED 208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1820-2143 |
1.09e-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: 51.60 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1820 EQLRLVKSQLQGLS-ASAGLLEQMRHMETQAKDLRNQLLNYRSTISNhgskiegLERELTDLNQEFETLQEKAQVnsrka 1898
Cdd:TIGR02168 761 AEIEELEERLEEAEeELAEAEAEIEELEAQIEQLKEELKALREALDE-------LRAELTLLNEEAANLRERLES----- 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1899 qtLYNNVNRAIQSAKELDMKIKTvirnvhiLLKQISgpdgegnnvpsgEFSREWAEAQRMMRELRnrnfgKHLREAEADK 1978
Cdd:TIGR02168 829 --LERRIAATERRLEDLEEQIEE-------LSEDIE------------SLAAEIEELEELIEELE-----SELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1979 RESQLLLNRIRTwqkthqgenngLANSIRDSLNEYEAKLSDLRARLQEAAARAKQangLNQENERALGAIQRQVKEINSL 2058
Cdd:TIGR02168 883 ASLEEALALLRS-----------ELEELSEELRELESKRSELRRELEELREKLAQ---LELRLEGLEVRIDNLQERLSEE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2059 QSDftkyltsadssllqtnialqLMEKSQKEYEKLAASLNEARQELSDKVRELSRsAGKTSL--VEEAEKHAQSLQELAK 2136
Cdd:TIGR02168 949 YSL--------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKE-LGPVNLaaIEEYEELKERYDFLTA 1007
|
....*..
gi 982311033 2137 QLEEIKR 2143
Cdd:TIGR02168 1008 QKEDLTE 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1952-2146 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1952 WAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQKTHQGennglansIRDSLNEYEAKLSDLRARLQEaAARA 2031
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELAR--------LEAELERLEARLDALREELDE-LEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2032 KQANGLNQEN--ERALGAIQRQVKEINSLQSDFTKYLTSADSSLlqtnialqlmEKSQKEYEKLAASLNEARQELSDKVR 2109
Cdd:COG4913 332 IRGNGGDRLEqlEREIERLERELEERERRRARLEALLAALGLPL----------PASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|....*..
gi 982311033 2110 ELSRSAgkTSLVEEAEKHAQSLQELAKQLEEIKRNAS 2146
Cdd:COG4913 402 ALEEAL--AEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1806-2361 |
1.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1806 SCVMTLLNDLATmgeqLRLVKSQLQGLSASaglLEQMRH-----METQAKDLRNqllNYRSTISNHGSKIEGLERELTDL 1880
Cdd:TIGR00606 262 SKIMKLDNEIKA----LKSRKKQMEKDNSE---LELKMEkvfqgTDEQLNDLYH---NHQRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1881 NQEFETL-QEKAQVNSRKAQT------------LYNNVNRAIQSAKELDM-----KIKTVIRNVHILLKQISGPDGEGNN 1942
Cdd:TIGR00606 332 NKERRLLnQEKTELLVEQGRLqlqadrhqehirARDSLIQSLATRLELDGfergpFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1943 VPSGEFSREWAEAQRMMRELRNRNFGK----HLREAEADKRESQlLLNRIRTWQKTHQGENN------GLANSIRD-SLN 2011
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLgrtiELKKEILEKKQEE-LKFVIKELQQLEGSSDRileldqELRKAERElSKA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2012 EYEAKLSDLRARL----QEAAARAKQANGLNQENE----------------RALGAIQRQVKEINSLQSD---------- 2061
Cdd:TIGR00606 491 EKNSLTETLKKEVkslqNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIRKIKSRHSDeltsllgyfp 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2062 FTKYLTSADSSLL-QTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLEE 2140
Cdd:TIGR00606 571 NKKQLEDWLHSKSkEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEK 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2141 IKRNasgdelvRCAVDAATA-YENILNAIKAAEDA---ANRAASASESALQTVIKeDLprKAKTLSSNSDKLLNEAKMTQ 2216
Cdd:TIGR00606 651 SSKQ-------RAMLAGATAvYSQFITQLTDENQSccpVCQRVFQTEAELQEFIS-DL--QSKLRLAPDKLKSTESELKK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2217 KKLKQEVSPALSNLQQtlNIVtvqrEVIATNLTTLRDGLRGIQRgdidamissakSMVRKANDITDE--VLDGLNP---- 2290
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQ--SII----DLKEKEIPELRNKLQKVNR-----------DIQRLKNDIEEQetLLGTIMPeees 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2291 ---IQTDVERIkdtygstqnEDFKKALTDADNSVNKLTNKLP--DLWRKIESINQQLLP----LGNISDNMDRIRELIQQ 2361
Cdd:TIGR00606 784 akvCLTDVTIM---------ERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEkqheLDTVVSKIELNRKLIQD 854
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2014-2165 |
1.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2014 EAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSL-QSDFTKY-LTSADSSLLQTNIALQLMEKSQKEYE 2091
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaEYSWDEIdVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 2092 KLAASLNEARQELSDKVRELSRSAGKtslVEEAEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENIL 2165
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGE---IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1840-2158 |
1.25e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.37 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1840 EQM-RHMETQAKDLRNQLlnyrstisnhgskieglERELTDLN-QEFETLQEKAQVNSRKAQTLYNN-VNRAIQSAKELD 1916
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARLQAELHTEaVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1917 MKIKTVIRNVHillkqisgpdgegNNVPSGEFSREW------------------------AEAQRMMRELRNRNFGkhlr 1972
Cdd:NF041483 138 ERRQTVESHVN-------------ENVAWAEQLRARtesqarrlldesraeaeqalaaarAEAERLAEEARQRLGS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1973 EAEADKRESQLLLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARlQEAAARAKQANGLNQENERAL 2045
Cdd:NF041483 201 EAESARAEAEAILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QAR-RQAAELSRAAEQRMQEAEEAL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2046 GAIQRQV-KEINSLQSDFTKYLTSADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSR---SA 2115
Cdd:NF041483 275 REARAEAeKVVAEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEKlvaEA 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 982311033 2116 GKTSLVEEAEKHAQSLQELAKQLEEIKRNASGD--ELVRCAVDAA 2158
Cdd:NF041483 351 AEKARTVAAEDTAAQLAKAARTAEEVLTKASEDakATTRAAAEEA 395
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2044-2330 |
1.32e-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: 49.72 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2044 ALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQK----EYEKLAASLNEARQELSDKVRELSRSAGK-T 2118
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSslaqETEELQKKATQTLAKAQQVNAESERTLGHaK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2119 SLVEEAEKHAQSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLpRKA 2198
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAEL-KAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2199 KtlssnsdKLLNEAKMTQKKLKQEVSPALSNLQQTLNivtvQREviaTNLTTLRDGLRgiqrgdidamisSAKSMVRKAN 2278
Cdd:pfam06008 154 Q-------DLLSRIQTWFQSPQEENKALANALRDSLA----EYE---AKLSDLRELLR------------EAAAKTRDAN 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2279 DITDEVLDGLNPIQTDVERIkdtygSTQNEDFKKALTDADNSV---NKLTNKLPD 2330
Cdd:pfam06008 208 RLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1852-2334 |
1.50e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1852 LRNQLLNYRSTISNHGSKIEGLE---RELTDLNQEFETLQEKaqvnsrkaQTLYNNVNRAIQSAKELDMKIKTVIRNVHI 1928
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHaiiKKLSVLQKDYNDYIKK--------KSRYDDLNNQILELEGYEMDYNSYLKSIES 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1929 LLKQIsgpdgegnnvpsgefsREWAEAQRMMRELRNRNFGKHLREAEAdkresqllLNRIRtwqkthqgennglaNSIRD 2008
Cdd:PRK01156 375 LKKKI----------------EEYSKNIERMSAFISEILKIQEIDPDA--------IKKEL--------------NEINV 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2009 SLNEYEAKLSDLRAR-------LQEAAARAKQANG----------LNQENERALgaIQRQVKEINSLQSDFTKylTSADS 2071
Cdd:PRK01156 417 KLQDISSKVSSLNQRiralrenLDELSRNMEMLNGqsvcpvcgttLGEEKSNHI--INHYNEKKSRLEEKIRE--IEIEV 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2072 SLLQTNIALQLMEKSQKEYEKLAASLNEARQeLSDKVRELSRSAGKTSLVEEAEKHAQSLQELAKQLE-EIKRNASGDEL 2150
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINKSINEYNK-IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWL 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2151 VRCAVDAATAYENI----------LNAIKAAEDAANRAASASESALQTVIKEdLPRKAKTLsSNSDKLLNEAKMTQKKLK 2220
Cdd:PRK01156 572 NALAVISLIDIETNrsrsneikkqLNDLESRLQEIEIGFPDDKSYIDKSIRE-IENEANNL-NNKYNEIQENKILIEKLR 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2221 QEV------SPALSNLQQTLNIVTVQREVIATNLTTLRDGLRgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTD 2294
Cdd:PRK01156 650 GKIdnykkqIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-----DAKANRARLESTIEILRTRINELSDRINDINET 724
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 982311033 2295 VERIKdtygstqneDFKKALTDADNSVNKLT-NKLPDLWRK 2334
Cdd:PRK01156 725 LESMK---------KIKKAIGDLKRLREAFDkSGVPAMIRK 756
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1814-2401 |
1.54e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1814 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKA-- 1891
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1892 ------------QVNSRKA----------------QTLYNNVNRAIQSAKELDMKIKTVIRNVHILLKQ-ISGPD---GE 1939
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPElllQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1940 GNNVPSGEFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 1990
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1991 -----------------------WQKTHQGENN--GL--------ANSIRDSLNEYEAKLSDLRARLQEAAARAK----- 2032
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVkldlkridVPEWAASEEELRERLDKAEEALQSAREKQAaaeeq 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2033 --QANG----LNQENERALGA-------IQRQVKEINSLQSDFTKYLTS----ADSSLLQTNIALQLMEKSQKEY-EKLA 2094
Cdd:pfam12128 627 lvQANGelekASREETFARTAlknarldLRRLFDEKQSEKDKKNKALAErkdsANERLNSLEAQLKQLDKKHQAWlEEQK 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2095 ASLNEARQELSDKVREL--SRSAGKTSLVEEAEKHAQSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2166
Cdd:pfam12128 707 EQKREARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2167 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALSNLQQTLNIVTVQREVIAT 2246
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2247 NLTTLRDGLRGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVER--------IKDTYGSTQNEDFKKaLTDAD 2318
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKyvehfknvIADHSGSGLAETWES-LREED 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2319 NSVNKLTNKLPDLWRKIESINQQLLPL-----------GNISDNM---------DRIRELIQQARDAASKVAVPMRFNGK 2378
Cdd:pfam12128 940 HYQNDKGIRLLDYRKLVPYLEQWFDVRvpqsimvlreqVSILGVDltefydvlaDFDRRIASFSRELQREVGEEAFFEGV 1019
|
730 740
....*....|....*....|...
gi 982311033 2379 SGVEVRLPNDLEDLKGYTSLSLF 2401
Cdd:pfam12128 1020 SESAVRIRSKVSELEYWPELRVF 1042
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1950-2242 |
2.55e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1950 REWAEAQRMMRELRNR--NFGKHLREAEAdkRESQLL---------LNRIRTWQKtHQGEnnglansirdsLNEYEAKLS 2018
Cdd:COG3096 292 RELFGARRQLAEEQYRlvEMARELEELSA--RESDLEqdyqaasdhLNLVQTALR-QQEK-----------IERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2019 DLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQ----------K 2088
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARalcglpdltpE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2089 EYEKLAASLNEARQELSDKVRELSRsagKTSLVEEA-EKHAQSLQELAKQLEEIKRNASGD---ELVRCAVDAATAYENi 2164
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQ---KLSVADAArRQFEKAYELVCKIAGEVERSQAWQtarELLRRYRSQQALAQR- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2165 LNAIKAAEDAANRAASASESAlQTVIKEDLPRKAKTLSSNSD--KLLNEAKMTQKKLKQEVSPA---LSNLQQTLNIVTV 2239
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEEleELLAELEAQLEELEEQAAEAveqRSELRQQLEQLRA 592
|
...
gi 982311033 2240 QRE 2242
Cdd:COG3096 593 RIK 595
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1837-2068 |
2.64e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1837 GLLEQMRHMETQAKDLRNQLLNYRSTIS-----------NHGSKIEGLERELTDLNQEFETLQEKaqvnsrkaQTLYNNV 1905
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEyleseeinksiNEYNKIESARADLEDIKIKINELKDK--------HDKYEEI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1906 NRAIQSAKELDMKIKTVIRNVhiLLKQISGPDGEGNNVPSGEFSREWAEAQRMMRELRN--------------------R 1965
Cdd:PRK01156 552 KNRYKSLKLEDLDSKRTSWLN--ALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIgfpddksyidksireieneaN 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1966 NFGKHLREAEADKRESQLLLNRIRTWQKTHQGennglANSIRDSLNEYEAKLSDLRARLQEAAARAKQANgLNQENERAL 2045
Cdd:PRK01156 630 NLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAK-ANRARLEST 703
|
250 260
....*....|....*....|....
gi 982311033 2046 GAIQRQ-VKEINSLQSDFTKYLTS 2068
Cdd:PRK01156 704 IEILRTrINELSDRINDINETLES 727
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
2.78e-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: 43.88 E-value: 2.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 355 ACNCHGHAS---DCYYDSdverqqaslntqgiyaggGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGT------------------GQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1869-2144 |
2.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1869 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLyNNVNRAIQSAKELDMKIKTV------IRNVHILLKQISGPDGEgnn 1942
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEIDVasaereIAELEAELERLDASSDD--- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1943 vpSGEFSREWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDLRA 2022
Cdd:COG4913 687 --LAALEEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2023 RLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTSADSSLLQTNIAlqlmekSQKEYEKLAASLneARQ 2102
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE------SLPEYLALLDRL--EED 827
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 982311033 2103 ELSDKVRELSRsagktsLVEEAEKHAQS--LQELAKQLEEIKRN 2144
Cdd:COG4913 828 GLPEYEERFKE------LLNENSIEFVAdlLSKLRRAIREIKER 865
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2014-2371 |
3.14e-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: 50.06 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2014 EAKLSDLRARLQEAA------ARAKQA-NGLN--QEN-----------ERALGAIQRQVK----------EINSLQSDFT 2063
Cdd:TIGR02168 151 EAKPEERRAIFEEAAgiskykERRKETeRKLErtRENldrledilnelERQLKSLERQAEkaerykelkaELRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2064 KY-LTSADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELS---DKVRELSRSagktslVEEAEKHAQSLQELAKQLE 2139
Cdd:TIGR02168 231 VLrLEELREELEELQEEL---KEAEEELEELTAELQELEEKLEelrLEVSELEEE------IEELQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2140 EIKR--NASGDELVRCAVDAATAYENILNaiKAAEDAANRAASASESALQTVIKEDLPRKAKTLSsnsdKLLNEAKMTQK 2217
Cdd:TIGR02168 302 QQKQilRERLANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELEELE----AELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2218 KLKQEVSPALSNLQQTLNivtvQREVIATNLTTLRDGLRGIQ--RGDIDAMISSA-KSMVRKANDITDEVLDGLNPIQTD 2294
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLEL----QIASLNNEIERLEARLERLEdrRERLQQEIEELlKKLEEAELKELQAELEELEEELEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2295 VErikdtygsTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL----GNISDNMDRIRELIQQARDAASKVA 2370
Cdd:TIGR02168 452 LQ--------EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlqENLEGFSEGVKALLKNQSGLSGILG 523
|
.
gi 982311033 2371 V 2371
Cdd:TIGR02168 524 V 524
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2006-2231 |
7.20e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.95 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2006 IRDSLNEYEAKLSDLRARLQEAAARAKQAnglnqENERAlgAIQRQVKEINSlQSDFTK-YLTSADSSLLQTNIALQLME 2084
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKA-----EAEVA--ALNRRIQLLEE-ELERTEeRLAEALEKLEEAEKAADESE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2085 --------KSQKEYEKLA---ASLNEARQELSDKVRELSRSAGKTSLV----EEAEKHAQSLQELAKQLEEIKRN----- 2144
Cdd:pfam00261 78 rgrkvlenRALKDEEKMEileAQLKEAKEIAEEADRKYEEVARKLVVVegdlERAEERAELAESKIVELEEELKVvgnnl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2145 ----ASGDElvrcAVDAATAYEnilNAIKAaedaanraasasesaLQTVIK------EDLPRKAKTLSSNSDKL---LNE 2211
Cdd:pfam00261 158 ksleASEEK----ASEREDKYE---EQIRF---------------LTEKLKeaetraEFAERSVQKLEKEVDRLedeLEA 215
|
250 260
....*....|....*....|
gi 982311033 2212 AKMTQKKLKQEVSPALSNLQ 2231
Cdd:pfam00261 216 EKEKYKAISEELDQTLAELN 235
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
565-607 |
1.01e-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: 42.34 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 982311033 565 CDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNLDkENPNGC 607
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2419-2545 |
1.21e-04 |
|
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: 44.33 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2419 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDRETELQVdqilteseTQEAVMD----RVKFQRIYQFARLnytkgatsskp 2494
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTL----------- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2495 EIPGVYDMDGRNSNTLLNLDpENVVFYVGGYPPDFKLPSRLRFPPYKGCIE 2545
Cdd:pfam02210 70 SVDGQTVVSSLPPGESLLLN-LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
565-607 |
1.24e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 982311033 565 CDPAGTI----DSNLGSCPCKLHVEGPTCSICKPLYWNldkENPNGC 607
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1969-2364 |
1.44e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1969 KHLREAEADKRESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLrARLQEAAARAKQANGLNQENErALGAI 2048
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQ-LLKQLRARIEELRAQEAVL-EETQERINRARKAAPLAAHIK-AVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2049 QRQVKEINS-LQSDFTKYltsadSSLLQTNIALQLMEKSQKEYEKLAASL----NEARQELSDKVRELSRSAGKTSLVEE 2123
Cdd:TIGR00618 306 EQQAQRIHTeLQSKMRSR-----AKLLMKRAAHVKQQSSIEEQRRLLQTLhsqeIHIRDAHEVATSIREISCQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2124 AEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILN----AIKAAEDAANRAASASESALQTVIKEDLPRKAk 2199
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKI- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2200 tlssnsdkLLNEAKMTQKKLKQEvspaLSNLQQTLNIVTVQREVIATNLTTLRDGLRGIQrgdidamissaKSMVRKAND 2279
Cdd:TIGR00618 460 --------HLQESAQSLKEREQQ----LQTKEQIHLQETRKKAVVLARLLELQEEPCPLC-----------GSCIHPNPA 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2280 ITDevLDGLNPIQTDVERIKDTYGSTQnedfkKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLG----NISDNMDRI 2355
Cdd:TIGR00618 517 RQD--IDNPGPLTRRMQRGEQTYAQLE-----TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnRSKEDIPNL 589
|
....*....
gi 982311033 2356 RELIQQARD 2364
Cdd:TIGR00618 590 QNITVRLQD 598
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
1.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 356 CNCH--GHASD-CYYDSdverqqaslntqgiyaggGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPDT------------------GQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1850-2350 |
1.64e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.90 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1850 KDLRNQLLNYRSTISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLYNNVNRAIQSAKELDMKIKTVIRNV 1926
Cdd:PTZ00440 511 KEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1927 HILLKQISGPDGEGNNVPSG--EFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNR 1987
Cdd:PTZ00440 591 DEIDNIIQQIEELINEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNT 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1988 IR-----------------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQ---- 2033
Cdd:PTZ00440 671 SKneyeklefmksdnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKlevy 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2034 ANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMeKSQKEYEKLAASLNEARQELSDKvrelsr 2113
Cdd:PTZ00440 751 KHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDI-NILKENKKNNQDLLNSYNILIQK------ 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2114 sagktsLVEEAEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQ 2187
Cdd:PTZ00440 824 ------LEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQ 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2188 TV---------IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPALSN-----LQQTLNIVTVQREVIAT 2246
Cdd:PTZ00440 898 LVehllnnkidLKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTKINnlkmqIEKTLEYYDKSKENING 977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2247 NLTTLRDGLRGIQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDT 2301
Cdd:PTZ00440 978 NDGTHLEKLDKEKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTK 1057
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2302 YGS-TQNEDFKKALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2350
Cdd:PTZ00440 1058 LSSfHFNIDIKKYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1838-2355 |
1.89e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.52 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1838 LLEQMRhMETQAKDLRNQLLNYRS-TISNHGS----KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRAIQSA 1912
Cdd:PTZ00440 1050 LLEKMK-TKLSSFHFNIDIKKYKNpKIKEEIKlleeKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKK 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1913 KELDMKIKTVIRNvhiLLKQISgpDGEGNNVPSGEFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQ 1992
Cdd:PTZ00440 1129 KKSLEKIYKQMEK---TLKELE--NMNLEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVK 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1993 KTHQGENNGLA-----NSIRDSLNEYEAKLSDLRAR---LQEAAARAKQANGLNQENERALGAIQRQVKEINSLQS---- 2060
Cdd:PTZ00440 1204 KNMSKERNDHLttfeyNAYYDKATASYENIEELTTEakgLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENalhe 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2061 --DFTKYLTSADSSLLQTNI------ALQLMEKSQKEYEKLaaslNEARQELSDKVRELSRSAGKtslVEEAEKHAQSLQ 2132
Cdd:PTZ00440 1284 ikNMYEFLISIDSEKILKEIlnstkkAEEFSNDAKKELEKT----DNLIKQVEAKIEQAKEHKNK---IYGSLEDKQIDD 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2133 ELAKqLEEIKRNASG--DELVRCAVDAATAYENILNAIKaaedaanraasaseSALQTVIKEDLPRKAKTLSSNSDKLLN 2210
Cdd:PTZ00440 1357 EIKK-IEQIKEEISNkrKEINKYLSNIKSNKEKCDLHVR--------------NASRGKDKIDFLNKHEAIEPSNSKEVN 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2211 EAKMTQ--KKLKQEVSPALSNLQQtlniVTVQREVI---ATNLTTLrdglrgIQRGDIDAMISSAKSMVRKANDITDEVL 2285
Cdd:PTZ00440 1422 IIKITDniNKCKQYSNEAMETENK----ADENNDSIikyEKEITNI------LNNSSILGKKTKLEKKKKEATNIMDDIN 1491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2286 DGLNPIQTDVERIKDTYGS-TQNEDFKKALTDADNSVNKLTNKLPDLwrKIESINQQLLPLGNISDNMDRI 2355
Cdd:PTZ00440 1492 GEHSIIKTKLTKSSEKLNQlNEQPNIKREGDVLNNDKSTIAYETIQY--NLGRVKHNLLNILNIKDEIETI 1560
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1855-2119 |
2.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1855 QLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKaqvnsrkaqtlYNNVNRAIQSAKEldmKIKTvirnvhiLLKQIs 1934
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEE-----------YNELQAELEALQA---EIDK-------LQAEI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1935 gpdgegnnvpsgefsrewAEAQRMMRELRNRnFGKHLREA-EADKRESQL-----------LLNRIRTWQKthqgenngL 2002
Cdd:COG3883 75 ------------------AEAEAEIEERREE-LGERARALyRSGGSVSYLdvllgsesfsdFLDRLSALSK--------I 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2003 ANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQL 2082
Cdd:COG3883 128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250 260 270
....*....|....*....|....*....|....*..
gi 982311033 2083 MEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2119
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3120-3287 |
2.64e-04 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 44.66 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3120 LDTPSSSFGV----SSCLGGP---LEKGIYFSEeggHVILAHSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLGV 3190
Cdd:smart00210 8 FDLPSLSFAIrqvvGPEPGSPayrLGDPALVPQ---PTRDLFPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 3191 YLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVTIKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapA 3268
Cdd:smart00210 85 EVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALSVSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--I 158
|
170
....*....|....*....
gi 982311033 3269 NLTTLRIPVWKSFFGCLRN 3287
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQ 177
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2020-2132 |
2.83e-04 |
|
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: 43.63 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2020 LRARLQEAAARAKQANGLNQ--ENERA-LGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQKEYEKlaas 2096
Cdd:pfam06009 5 AREANETAKEVLEQLAPLSQnlENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ---- 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 982311033 2097 LNEARQELSDKVRELSRsagktsLVEEAEKHAQSLQ 2132
Cdd:pfam06009 81 LEVNSSSLSDNISRIKE------LIAQARKAANSIK 110
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2074-2238 |
2.85e-04 |
|
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: 43.85 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2074 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHAQslqELAKQLEEIKRNAS--GDELV 2151
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQG---EVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2152 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2226
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 982311033 2227 LSNLQQTLNIVT 2238
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2013-2270 |
3.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2013 YEAKLSDLRARLQEAAARAKQANGlnQENERALGAIQRQVKEINSLQSDFTKYLTsadssllqtniALQLMEKSQKEYEK 2092
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEEEYAE-----------LQEELEELEEELEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2093 LAASLNEARQELsdkvRELSRSAGKTSLVEEAEKHAQSLQELAKQLEEIKRNAsgDELvrcaVDAATAYENILNAIKAAe 2172
Cdd:COG4717 107 LEAELEELREEL----EKLEKLLQLLPLYQELEALEAELAELPERLEELEERL--EEL----RELEEELEELEAELAEL- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2173 daanraasasESALQTVIKEDLPRKAKTLSSNSDKlLNEAKMTQKKLKQEvspaLSNLQQTLNIVTVQREVIATNLTTLR 2252
Cdd:COG4717 176 ----------QEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEE----LEEAQEELEELEEELEQLENELEAAA 240
|
250
....*....|....*...
gi 982311033 2253 DgLRGIQRGDIDAMISSA 2270
Cdd:COG4717 241 L-EERLKEARLLLLIAAA 257
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1816-2040 |
3.70e-04 |
|
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: 44.92 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1816 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQvn 1894
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1895 srKAQTLYNNVnraiQSAKELDmkiktvirnvhILLKQIsgpdgegnnvpsgefsrewAEAQRMMRELRnrnfgKHLREA 1974
Cdd:COG1579 77 --KYEEQLGNV----RNNKEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 1975 --EADKRESQLllnrirtwqKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEA-AARAKQANGLNQE 2040
Cdd:COG1579 116 meRIEELEEEL---------AELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPE 175
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1943-2226 |
4.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1943 VPSGEFSREWAEAQRMMRELRNRNFGKHLREAEAD---KRESQLLLNRIRTWQKTHQGENNGLANSIRDSlnEYEAKLSD 2019
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAhfaRRQAAIKAEEARKADELKKAEEKKKADEAKKA--EEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2020 LRARLQE----------AAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQKE 2089
Cdd:PTZ00121 1307 AKKKAEEakkadeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2090 YE--KLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAQSLQ---ELAKQLEEIKRnasGDELVRCAVDAATAYEni 2164
Cdd:PTZ00121 1387 AEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAKK---ADEAKKKAEEAKKAEE-- 1461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 2165 lnaIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKmtQKKLKQEVSPA 2226
Cdd:PTZ00121 1462 ---AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKADEAKKA 1518
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-344 |
4.62e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 982311033 299 CVCN--GHA-EVCNANNpeklFRCQCQHHTCGETCDRCCTGYNQRRWQP 344
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
2022-2145 |
5.18e-04 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 43.71 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2022 ARLQEAAARAKQAN--GLNQENERALGAIQrqvKEINSLQSdfTKY-----LTSADSSLLQTNIALQLMEKSQKEYEKLA 2094
Cdd:pfam05335 47 AKAAEAALAGKQQIveQLEQELREAEAVVQ---EESASLQQ--SQAnanaaQRAAQQAQQQLEALTAALKAAQANLENAE 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 982311033 2095 ASLNEARQELsdkvrelsrsAGKTSLVEEAEKHAQSLQE---LAKQ-LEEIKRNA 2145
Cdd:pfam05335 122 QVAAGAQQEL----------AEKTQLLEAAKKRVERLQRqlaEARAdLEKTKKAA 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1881-2111 |
5.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1881 NQEFETLQEKAQVNSRKAQTLYNNVNRAIQSAKELDMKIKTVIRNVHI--LLKQISGPDGEGNNVPSGEFsREWAEAQRM 1958
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLeeLEQEIAALLAEAGVEDEEEL-RAALEQAEE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1959 MRELRNRnfgkhLREAEADKREsqlLLNRIRTWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQAnGL 2037
Cdd:COG4717 397 YQELKEE-----LEELEEQLEE---LLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAELEAELEQL-EE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 2038 NQENERALGAIQRQVKEINSLQSDFTKYltsadssllqtNIALQLMEKSQKEYEKlaaslnEARQELSDKVREL 2111
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAAL-----------KLALELLEEAREEYRE------ERLPPVLERASEY 524
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1950-2115 |
5.91e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1950 REWAEAQRMMRELRNR-----NFGK-HL-REAEADKRESQlllNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRA 2022
Cdd:COG1842 58 RQLEELEAEAEKWEEKarlalEKGReDLaREALERKAELE---AQAEALEAQLA-QLEEQVEKLKEALRQLESKLEELKA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2023 RLQEAAARAKQAnglnqeneRALGAIQRQVKEINSlqsdftkylTSADSsllqtniALQLMEKSQKEYEKLAASLNE--A 2100
Cdd:COG1842 134 KKDTLKARAKAA--------KAQEKVNEALSGIDS---------DDATS-------ALERMEEKIEEMEARAEAAAElaA 189
|
170
....*....|....*
gi 982311033 2101 RQELSDKVRELSRSA 2115
Cdd:COG1842 190 GDSLDDELAELEADS 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1874-2163 |
6.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1874 ERELTDLNQEFETLQE---KAQVNSRKAQTLYNNVNRAIqsakeldmkiktvirNVHILLKQISGPdgegnNVPSGEFSR 1950
Cdd:PRK04863 785 EKRIEQLRAEREELAEryaTLSFDVQKLQRLHQAFSRFI---------------GSHLAVAFEADP-----EAELRQLNR 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1951 EWAEAQRMMRELRNRNfgKHLREAEADKRESQLLLNRirtwqktHQGENNGLAnsiRDSLNEYEAKLSDLRARLQEAAAR 2030
Cdd:PRK04863 845 RRVELERALADHESQE--QQQRSQLEQAKEGLSALNR-------LLPRLNLLA---DETLADRVEEIREQLDEAEEAKRF 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2031 -AKQANGLNQ---------ENERALGAIQRQVKEINSLQSDfTKYLTSADSSLLQTNIAL------QLMEKSQKEYEKLA 2094
Cdd:PRK04863 913 vQQHGNALAQlepivsvlqSDPEQFEQLKQDYQQAQQTQRD-AKQQAFALTEVVQRRAHFsyedaaEMLAKNSDLNEKLR 991
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982311033 2095 ASLNEARQELsDKVRELSRSAGK---------TSLVEEAEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYEN 2163
Cdd:PRK04863 992 QRLEQAEQER-TRAREQLRQAQAqlaqynqvlASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHAR 1068
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1814-2220 |
6.99e-04 |
|
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: 45.55 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1814 DLATMGEQLRLVKSQLQglsasaglleqmrhMETQAKdlrnqlLNYrstisnhGSKIEGLERELTDLNQEFETLQEKAQV 1893
Cdd:pfam01576 462 DVSSLESQLQDTQELLQ--------------EETRQK------LNL-------STRLRQLEDERNSLQEQLEEEEEAKRN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1894 NSRKAQTLynnvnraiqSAKELDMKIKTvirnvhillkqisgpDGEGNNVPSGEFSRewaeaQRMMRELRNRNFGKHLRE 1973
Cdd:pfam01576 515 VERQLSTL---------QAQLSDMKKKL---------------EEDAGTLEALEEGK-----KRLQRELEALTQQLEEKA 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1974 AEADKRESQlllnRIRTWQK-----THQGENNGLANSIR------DSLNEYE----AKLSDLRARlQEAAARAKQ--ANG 2036
Cdd:pfam01576 566 AAYDKLEKT----KNRLQQElddllVDLDHQRQLVSNLEkkqkkfDQMLAEEkaisARYAEERDR-AEAEAREKEtrALS 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2037 LNQENERALGAIQRQVKEINSLQSDFTKYLTSADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSD--------KV 2108
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDD----VGKNVHELERSKRALEQQVEEMKTQLEELEDelqatedaKL 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2109 R-ELSRSAGKTS----LVEEAEKHAQSLQELAKQLEEIKrnASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASE 2183
Cdd:pfam01576 717 RlEVNMQALKAQferdLQARDEQGEEKRRQLVKQVRELE--AELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRE 794
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 982311033 2184 SA------LQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLK 2220
Cdd:pfam01576 795 EAvkqlkkLQAQMK-DLQRELEEARASRDEILAQSKESEKKLK 836
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2024-2169 |
8.15e-04 |
|
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: 42.70 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2024 LQEAAARAKQA-NGLNQENERALGaIQRQVKEINSLQSDFTKYLTSADSslLQTNIALQLMEKSqkeyEKLAASLNEARQ 2102
Cdd:cd13769 3 LSELIQKAQEAiNNLAQQVQKQLG-LQNPEEVVNTLKEQSDNFANNLQE--VSSSLKEEAKKKQ----GEVEEAWNEFKT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982311033 2103 ELSDKVRELSRSagktslvEEAEKHAQSLQ------------ELAKQLEEIKRNAsgdelvrcavdaATAYENILNAIK 2169
Cdd:cd13769 76 KLSETVPELRKS-------LPVEEKAQELQaklqsglqtlvtESQKLAKAISENS------------QKAQEELQKATK 135
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1678-1768 |
1.02e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 42.00 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1678 CQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNRFATGCVVNG----GDVRCSCKAGY-------IG 1745
Cdd:cd13406 18 CPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTqpldsykPG 94
|
90 100
....*....|....*....|...
gi 982311033 1746 TQCERCAPGYFGNPQkfGGSCQP 1768
Cdd:cd13406 95 VDCVPCPPGHFSRGD--NQACKP 115
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
2031-2151 |
1.10e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2031 AKQANGLNQENERALGAIQR----QVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD 2106
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESvlpsTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEK 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 982311033 2107 KVRELSRS-----AGKTSLVEEAEKHAQSLQELAKQLEEIKrnasgDELV 2151
Cdd:pfam08614 93 KLREDERRlaaleAERAQLEEKLKDREEELREKRKLNQDLQ-----DELV 137
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1947-2113 |
1.23e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 44.07 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1947 EFSREWAEA-----QRMMREL--RNRN----FGKH-LREAEADKRESQLLLNRIRTWQK----THQGEN-NGLANSIRDS 2009
Cdd:COG3524 150 EDAQAIAEAllaesEELVNQLseRAREdavrFAEEeVERAEERLRDAREALLAFRNRNGildpEATAEAlLQLIATLEGQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2010 LNEYEAKLSDLRARLQEAAARAKQAnglnqenERALGAIQRQVKEINSLqsdftkyLTSAD-----SSLLQTNIALQL-M 2083
Cdd:COG3524 230 LAELEAELAALRSYLSPNSPQVRQL-------RRRIAALEKQIAAERAR-------LTGASggdslASLLAEYERLELeR 295
|
170 180 190
....*....|....*....|....*....|
gi 982311033 2084 EKSQKEYEKLAASLNEARQELSDKVRELSR 2113
Cdd:COG3524 296 EFAEKAYTSALAALEQARIEAARQQRYLAV 325
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1790-1920 |
1.35e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1790 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSTISNHGSK 1869
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 982311033 1870 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLYNNVNRAIQSAKELDMKIK 1920
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1947-2169 |
1.54e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1947 EFSREWAEA----QRMMRELRNRNFGKHLREAEAdkresqlllnrirtWQKTHQGennglansIRDSLNEYEAKLSDLRA 2022
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDLESVEA--------------LLKKHEA--------LEAELAAHEERVEALNE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2023 rlqeaaarakQANGLNQENERALGAIQRQVKEINSLQSDFTKyLTSADSSLLQTniALQLMEKSQkEYEKLAASLNEARQ 2102
Cdd:cd00176 62 ----------LGEQLIEEGHPDAEEIQERLEELNQRWEELRE-LAEERRQRLEE--ALDLQQFFR-DADDLEQWLEEKEA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2103 ELSDkvRELSRSAGKtslVEEA-EKHAQSLQELAKQLEEIKR-NASGDELV-RCAVDAATAYENILNAIK 2169
Cdd:cd00176 128 ALAS--EDLGKDLES---VEELlKKHKELEEELEAHEPRLKSlNELAEELLeEGHPDADEEIEEKLEELN 192
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1825-1914 |
1.67e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1825 VKSQLQGLSASagLLEQMRHMETQAKDLRNQLLNYRSTISNhgSKIEGLERELTDLNQEFETLQEKAQ--VNSRKA---Q 1899
Cdd:COG2825 44 AQKKLEKEFKK--RQAELQKLEKELQALQEKLQKEAATLSE--EERQKKERELQKKQQELQRKQQEAQqdLQKRQQellQ 119
|
90
....*....|....*.
gi 982311033 1900 TLYNNVNRAIQS-AKE 1914
Cdd:COG2825 120 PILEKIQKAIKEvAKE 135
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2027-2222 |
1.83e-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: 43.60 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2027 AAARAKQANGLNQENERALGAIQRQVKEINSLQS---DFTKYLTSADSSLLQTNIALQLMEKS-----------QKEYEK 2092
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKeekALLKQLAALERRIAALARRIRALEQElaaleaelaelEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2093 LAASLNEARQELSDKVRELSRSAGKTSL--------VEEAEKHAQSLQELA----KQLEEIKRNAsgDELVRCAVDAATA 2160
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLalllspedFLDAVRRLQYLKYLAparrEQAEELRADL--AELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982311033 2161 YENILNAIKaaedaanrAASASESALQTVIKEdlprKAKTLSSNSDKLLNEAKMTQKKLKQE 2222
Cdd:COG4942 173 RAELEALLA--------ELEEERAALEALKAE----RQKLLARLEKELAELAAELAELQQEA 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1814-2360 |
2.01e-03 |
|
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: 44.29 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1814 DLATMGEQLRLVKSQLQGLSASA-GLLEQMRHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQ 1892
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKeDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1893 VNSRkaqtlYNNVNRAIQsakeldMKIKTVIRNVHILLKQISGPDGE-------------GNNVPSGEfsrewAEAQRMM 1959
Cdd:TIGR02169 501 ASEE-----RVRGGRAVE------EVLKASIQGVHGTVAQLGSVGERyataievaagnrlNNVVVEDD-----AVAKEAI 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1960 RELRNRNFGkhlreaeadkRESQLLLNRIRTWQKThqgenngLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGL-- 2037
Cdd:TIGR02169 565 ELLKRRKAG----------RATFLPLNKMRDERRD-------LSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVve 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2038 NQENERALGAIQRQVK---EI--------------NSLQSDFTKYLtsadSSLLQTNIALQLMEKS----QKEYEKLAAS 2096
Cdd:TIGR02169 628 DIEAARRLMGKYRMVTlegELfeksgamtggsrapRGGILFSRSEP----AELQRLRERLEGLKRElsslQSELRRIENR 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2097 LNEARQELSDKVRELS-RSAGKTSLVEEAEKHAQSLQELAKQLEEI--KRNASGDELVRCAVD------AATAYENILNA 2167
Cdd:TIGR02169 704 LDELSQELSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLeqEIENVKSELKELEARieeleeDLHKLEEALND 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2168 IKaaedaanraASASESALQTVikEDLPRKAKTLSSNSDKLLNEAKMTQKKL---KQEVSPALSNLQQTLNIVTVQREVI 2244
Cdd:TIGR02169 784 LE---------ARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLtleKEYLEKEIQELQEQRIDLKEQIKSI 852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2245 ATNLTTLRdglrgIQRGDIDAMISSAKSMVRkanDITDEVLDglnpIQTDVERIKDTYGSTQN--EDFKKALTDADNSVN 2322
Cdd:TIGR02169 853 EKEIENLN-----GKKEELEEELEELEAALR---DLESRLGD----LKKERDELEAQLRELERkiEELEAQIEKKRKRLS 920
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 982311033 2323 KLTNKLP----------DLWRKIESINQQLLPLGNISDNMDRIRELIQ 2360
Cdd:TIGR02169 921 ELKAKLEaleeelseieDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1953-2146 |
2.03e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1953 AEAQRMMRElrnrnfgkhlrEAEADKRESQLLLNRIRTWQktHQGENNglANSIRDslnEYEAKLSDLRA-------RLQ 2025
Cdd:NF041483 600 AEAERIRRE-----------AAEETERLRTEAAERIRTLQ--AQAEQE--AERLRT---EAAADASAARAegenvavRLR 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2026 -EAAARAKQANGLNQEN------------ER-------ALGAIQrqvKEINSLQSDFTKYLTSADSSllqtniALQLMEK 2085
Cdd:NF041483 662 sEAAAEAERLKSEAQESadrvraeaaaaaERvgteaaeALAAAQ---EEAARRRREAEETLGSARAE------ADQERER 732
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 2086 SQKEYEKLAAS----LNEARQELSDKVRELSRSAgkTSLVEEAEKHAQS-------LQELAKQleEIK--RNAS 2146
Cdd:NF041483 733 AREQSEELLASarkrVEEAQAEAQRLVEEADRRA--TELVSAAEQTAQQvrdsvagLQEQAEE--EIAglRSAA 802
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1971-2137 |
2.08e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1971 LREAEADKRESQLLLNRIRTWQ---KTHQGENNGLANSIRDSLNEYE-----AKLSDLRARL----QEAAARAKQA-NGL 2037
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTDEGgaiarKEIKDLQKELeklnEEYAAKLKAKiDEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2038 NQENERALGAIQRQVKEINSLqsdftkylTSADSSL--LQTNI--ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR 2113
Cdd:cd22656 207 KALIADDEAKLAAALRLIADL--------TAADTDLdnLLALIgpAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPA 278
|
170 180
....*....|....*....|....
gi 982311033 2114 SAGKTSLVEEAEKHAQSLQELAKQ 2137
Cdd:cd22656 279 AILAKLELEKAIEKWNELAEKADK 302
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1828-2306 |
2.62e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1828 QLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRST-----ISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLy 1902
Cdd:COG5278 31 SLNRLREASEWVEHTYEVLRALEELLSALLDAETGqrgylLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1903 nnvnRAIQSAkeLDMKIKtVIRNVhILLKQISGPDGEGNNVPSGEfsrewaeAQRMMRELRNRNFGKHLREAEADKRESQ 1982
Cdd:COG5278 110 ----DELEAL--IDQWLA-ELEQV-IALRRAGGLEAALALVRSGE-------GKALMDEIRARLLLLALALAALLLAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1983 LL-------------------LNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAARAKQANGLNQENER 2043
Cdd:COG5278 175 LLllllalaallalaellllaLARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2044 ALGAIQRQVKEINSLQSDFTKYLTSADSSLLQTNIALQLMEKSQ--KEYEKLAASLNEARQELSDKVRELSRSAGKTSLV 2121
Cdd:COG5278 255 AALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALAlaELELELLLAAAAAAAAAAAAAAAALAALLALALA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2122 EEAEKHAQSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTL 2201
Cdd:COG5278 335 TALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2202 SSNSDKLLNEAKMTQKKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRDGLRGIQRGDIDAMISSAKSMVRKANDIT 2281
Cdd:COG5278 415 AASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALA 494
|
490 500
....*....|....*....|....*
gi 982311033 2282 DEVLDGLNPIQTDVERIKDTYGSTQ 2306
Cdd:COG5278 495 AAAALSLALALAALLLAAAEAALAA 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1974-2149 |
2.92e-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: 42.83 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1974 AEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEyeakLSDLRARLqeaAARAKQANGLNQENERALGAIQRQVK 2053
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRI---AALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2054 EINSLQ----------------------SDFTKYLTSADSSlLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVREL 2111
Cdd:COG4942 91 EIAELRaeleaqkeelaellralyrlgrQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 982311033 2112 SR-SAGKTSLVEEAEKHAQSLQELAKQLEEIKRNASGDE 2149
Cdd:COG4942 170 EAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
299-337 |
3.14e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 982311033 299 CVCNGHAEV---CNANNpeklFRCQCQHHTCGETCDRCCTGY 337
Cdd:pfam00053 1 CDCNPHGSLsdtCDPET----GQCLCKPGVTGRHCDRCKPGY 38
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2003-2142 |
3.35e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.10 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2003 ANSIRDSLNEyeaKLSDLRARLQEAAARAKQAngLNQENERA---LGAIQRQVKE-----INSLQSDFTKYLTSADSSLL 2074
Cdd:pfam01442 35 TEALRERLQK---DLEEVRAKLEPYLEELQAK--LGQNVEELrqrLEPYTEELRKrlnadAEELQEKLAPYGEELRERLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982311033 2075 QTNIALQlmeksqkeyEKLAASLNEARQELSDKVRELSRS-AGKTSLVEE-AEKHAQSLQE-LAKQLEEIK 2142
Cdd:pfam01442 110 QNVDALR---------ARLAPYAEELRQKLAERLEELKESlAPYAEEVQAqLSQRLQELREkLEPQAEDLR 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1821-2077 |
3.36e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1821 QLRLVKSQLQGLSASAGLLEQmrHMETQAKDLRNQLLNYRSTISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQT 1900
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQ--QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1901 LYNNVNRAIQSAKELDMKIKTVIRNVHILLKqisgpdgeGNNVPSgeFSREWAEAQRMMRELRNR--NFGKHLREAEADK 1978
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKMYEK--------GGVCPT--CTQQISEGPDRITKIKDKlkELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1979 RESQLLLNRIRTWQKTHQGENNGLANsIRDSLNEYEAKLSDLRARLQEAaarakQANGLNQENEraLGAIQRQVKEINSL 2058
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKIST-NKQSLITLVDKAKKVKAAIEEL-----QAEFVDNAEE--LAKLQDELDKIVKT 394
|
250 260
....*....|....*....|.
gi 982311033 2059 QSDFT--KYLTSADSSLLQTN 2077
Cdd:PHA02562 395 KSELVkeKYHRGIVTDLLKDS 415
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2073-2169 |
3.67e-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: 40.26 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2073 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHAQSLQELAKQLEEIKRNAS 2146
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 982311033 2147 GDELvrcavdaATAYENILNAIK 2169
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1647-1784 |
3.68e-03 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 40.75 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1647 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnRCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1722
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982311033 1723 rfatgcvvNGGDVRCSCKAGYiGTQCERCAPGYFGNPQKFGGSCQPCS-CNNNG-QLGSCDPLT 1784
Cdd:cd13416 101 --------PGQGVVQSCGPNQ-DTVCEACPEGTYSDEDSSTDPCLPCTvCEDGEvELRECTPVS 155
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2019-2110 |
4.11e-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: 40.26 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2019 DLRARLQEAAARAKQANGLNQENERALGAIQRQVKEINSLQSDFTKY---LTSADSSLLQTNIAlQLMEKSQKEYEKLAA 2095
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaatLSEAAREKKEKELQ-KKVQEFQRKQQKLQQ 83
|
90
....*....|....*
gi 982311033 2096 SLNEARQELSDKVRE 2110
Cdd:smart00935 84 DLQKRQQEELQKILD 98
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2024-2253 |
5.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2024 LQEAAARAKQANGLNQENEralgaIQRQVKEINSLQsdftkyLTSADSSLLQTNIA-----LQLMEKSQKEYEKLAASLN 2098
Cdd:PRK11281 22 LSSAFARAASNGDLPTEAD-----VQAQLDALNKQK------LLEAEDKLVQQDLEqtlalLDKIDRQKEETEQLKQQLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2099 EARQELSDKVRELSR--SAGKTSLVEEAEKhaQSLQELAKQLEEIKrnasgDELVRCAVDAATAYENILNAikaaedaan 2176
Cdd:PRK11281 91 QAPAKLRQAQAELEAlkDDNDEETRETLST--LSLRQLESRLAQTL-----DQLQNAQNDLAEYNSQLVSL--------- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 982311033 2177 raASASESAlQTVIKEDLPRKAKTlssnsDKLLNEAKMTQKKLKQEVSPALSNLQQTLNIVTVQREVIATNLTTLRD 2253
Cdd:PRK11281 155 --QTQPERA-QAALYANSQRLQQI-----RNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQD 223
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1980-2167 |
5.32e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 1980 ESQLLLNRirtwqKTHQ------GENNGLANSIRDSLNEYeaklSDLRARLQEAAARAKQAnglnqENERALgaIQRQVK 2053
Cdd:COG0497 133 EHQSLLDP-----DAQRelldafAGLEELLEEYREAYRAW----RALKKELEELRADEAER-----ARELDL--LRFQLE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2054 EINS----------LQSDFTK----------------YLTSADSSLLQT-NIALQLMEKSQK---EYEKLAASLNEARQE 2103
Cdd:COG0497 197 ELEAaalqpgeeeeLEEERRRlsnaeklrealqealeALSGGEGGALDLlGQALRALERLAEydpSLAELAERLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2104 LSDKVRELSRSAGKTSL-------VEE--------AEKHAQSLQELAKQLEEIKR-----NASGDELVRCAVDAATAYEN 2163
Cdd:COG0497 277 LEEAASELRRYLDSLEFdperleeVEErlallrrlARKYGVTVEELLAYAEELRAelaelENSDERLEELEAELAEAEAE 356
|
....
gi 982311033 2164 ILNA 2167
Cdd:COG0497 357 LLEA 360
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2019-2217 |
7.91e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2019 DLRARLQEAAARAKQanglnQENERALGaiqRQVKEINSLQSDftkylTSADSSLLQTNIALQLMEKSQK---EYEKLAA 2095
Cdd:PRK07735 6 DLEDLKKEAARRAKE-----EARKRLVA---KHGAEISKLEEE-----NREKEKALPKNDDMTIEEAKRRaaaAAKAKAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2096 SLNEARQELSDKVRELSRSAGKTSLVEEAEKHAqslQELAKQLEEIKRNASGDELVRCAVDAATayenilnAIKAAEDAA 2175
Cdd:PRK07735 73 ALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKA---AALAKQKREGTEEVTEEEKAAAKAKAAA-------AAKAKAAAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 982311033 2176 NRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQK 2217
Cdd:PRK07735 143 AKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQK 184
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2009-2140 |
8.56e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982311033 2009 SLNEYEAKLSDLRARLQEAAARAKQANGL--NQEN--ERALGAI---QRQVKEINSL---QSDFTKYLTSADSSLLQTNI 2078
Cdd:PRK11281 122 SLRQLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTqpERAQAALyanSQRLQQIRNLlkgGKVGGKALRPSQRVLLQAEQ 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982311033 2079 AL--QLMEKSQKEyekLAAslNEARQELSDKVRELsrsagKTSLVEEAEKHAQSLQEL--AKQLEE 2140
Cdd:PRK11281 202 ALlnAQNDLQRKS---LEG--NTQLQDLLQKQRDY-----LTARIQRLEHQLQLLQEAinSKRLTL 257
|
|
| |
