|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-763 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1183.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 12 EERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsrTTCRAVLNPLCQVDYRAKLWACNFCYQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 92 NQFPPSYAGISELNQPAELLPQFSSIEYVVLR---GPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLL 244
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 245 GELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYV 324
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 325 KKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGG 404
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 405 TLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVT 483
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 484 QYQHSSGQRRIRVTTIARNWADAqTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD 563
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 564 DPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSIL 643
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 644 ADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVN 723
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 38202214 724 PSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 763
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-764 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 950.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsRTTCRAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 89 YQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKV--PLTQATRGPQVQQPPPSnRFLQPVQKIDMNLTDLLGE 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFASS-RFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 247 LQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKK 326
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 327 GTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTL 406
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 407 EIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGG-RGAIQFVTQY 485
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 486 QHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDP 565
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 566 SSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILAD 645
Cdd:COG5047 560 SSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 646 RILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPS 725
Cdd:COG5047 640 VILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPS 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 38202214 726 QTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 764
Cdd:COG5047 720 DITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
126-388 |
2.69e-164 |
|
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238755 [Multi-domain] Cd Length: 267 Bit Score: 474.94 E-value: 2.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 126 QMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 205
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 206 LSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPN 281
Cdd:cd01478 81 LGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 282 TGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMK 361
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 38202214 362 CCPNLTGGYMVMGDSFNTSLFKQTFQR 388
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
126-390 |
3.52e-93 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 290.69 E-value: 3.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 200
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 201 QEMLglskvpltqatrgpqvqqPPPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFp 280
Cdd:pfam04811 74 QDMF------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 281 nTGARIMMFIGGPATQGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEM 360
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 38202214 361 KCCPNLTGGYMVMGDSFN----TSLFKQTFQRVF 390
Cdd:pfam04811 208 GQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-763 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1183.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 12 EERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsrTTCRAVLNPLCQVDYRAKLWACNFCYQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 92 NQFPPSYAGISELNQPAELLPQFSSIEYVVLR---GPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLL 244
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 245 GELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYV 324
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 325 KKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGG 404
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 405 TLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVT 483
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 484 QYQHSSGQRRIRVTTIARNWADAqTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD 563
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 564 DPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSIL 643
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 644 ADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVN 723
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 38202214 724 PSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 763
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-764 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 950.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsRTTCRAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 89 YQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKV--PLTQATRGPQVQQPPPSnRFLQPVQKIDMNLTDLLGE 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFASS-RFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 247 LQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKK 326
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 327 GTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTL 406
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 407 EIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGG-RGAIQFVTQY 485
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 486 QHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDP 565
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 566 SSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILAD 645
Cdd:COG5047 560 SSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 646 RILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPS 725
Cdd:COG5047 640 VILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPS 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 38202214 726 QTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 764
Cdd:COG5047 720 DITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
126-388 |
2.69e-164 |
|
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238755 [Multi-domain] Cd Length: 267 Bit Score: 474.94 E-value: 2.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 126 QMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 205
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 206 LSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPN 281
Cdd:cd01478 81 LGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 282 TGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMK 361
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 38202214 362 CCPNLTGGYMVMGDSFNTSLFKQTFQR 388
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
126-390 |
3.52e-93 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 290.69 E-value: 3.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 200
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 201 QEMLglskvpltqatrgpqvqqPPPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFp 280
Cdd:pfam04811 74 QDMF------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 281 nTGARIMMFIGGPATQGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEM 360
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 38202214 361 KCCPNLTGGYMVMGDSFN----TSLFKQTFQRVF 390
Cdd:pfam04811 208 GQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
610-730 |
2.60e-84 |
|
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.
Pssm-ID: 200443 [Multi-domain] Cd Length: 121 Bit Score: 262.69 E-value: 2.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 610 QDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPV 689
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 38202214 690 DDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNN 730
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
126-388 |
5.87e-82 |
|
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface. Some members of this family possess a partial MIDAS motif that is a characteristic feature of most vWA domain proteins.
Pssm-ID: 238745 [Multi-domain] Cd Length: 239 Bit Score: 261.03 E-value: 5.87e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGI-SKSYVFRGTKDLsakq 199
Cdd:cd01468 1 PQPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 200 lqemlglskvpltqatrgpqvqQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPqGKRPLRSSGVALSIAVGLLECTF 279
Cdd:cd01468 77 ----------------------FLPLPDRFLVPLSECKKVIHDLLEQLPPMFWPVP-THRPERCLGPALQAAFLLLKGTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 280 pnTGARIMMFIGGPATQGPGMVVGDELKTPIRSWhdidkDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLE 359
Cdd:cd01468 134 --AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|...
gi 38202214 360 MKCCPNLTGGYMVMGDSFN----TSLFKQTFQR 388
Cdd:cd01468 207 LKQLAKSTGGQVYLYDSFQapndGSKFKQDLQR 239
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
518-617 |
1.24e-33 |
|
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is composed of five alpha helices.
Pssm-ID: 461441 [Multi-domain] Cd Length: 103 Bit Score: 124.54 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 518 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD--DPSSFRFSETFSLYPQFMFHLRRSSFLQVFNN 595
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 38202214 596 SP-DESSYYRHHFMRQDLTQSLI 617
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
401-504 |
5.97e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 118.79 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 401 GFGGTLEIKTSREIKISGAIGPCVSLNSkgpcvseneigtGGTcqWKICGLSPTTTLAIYFEvvnqHNAPIPQGGRGAIQ 480
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 38202214 481 FVTQYQHSSGQRRIRVTTIARNWA 504
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
9-667 |
1.44e-18 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 90.62 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 9 QQNEERDGVRFSWNVWP--SSRLEATRmvVPVAALFTPLKE-RPDLPPIQYE----PVLCSRttCRAVLNPLCQVDYRAK 81
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQFIEQGR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 82 LWACNFCYQRNQFP-----PSYAGI--SELNQPAELLpqFSSIEYVV-----LRGPQmPLIFLYVVDT---CMEDEDLQA 146
Cdd:COG5028 221 KWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPELK--SGVVDFLApkeysLRQPP-PPVYVFLIDVsfeAIKNGLVKA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 147 LKESMQMSLSLLP---PTALVGLITFGRMVqvhelgcegisksYVFRGTKDLSAKQLqemlglskvpLTQATRGPQVqqP 223
Cdd:COG5028 298 AIRAILENLDQIPnfdPRTKIAIICFDSSL-------------HFFKLSPDLDEQML----------IVSDLDEPFL--P 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 224 PPSNRFLQPVQKIDMNLTDLLGELQRdpwpVPQGKR-PLRSSGVALSIAVGLLEctfpNTGARIMMFIGGPATQGPGMVv 302
Cdd:COG5028 353 FPSGLFVLPLKSCKQIIETLLDRVPR----IFQDNKsPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNMGIGKL- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 303 gdELKTPIRSWHDIDKDnaKYVKKGTKHFealanraATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLF 382
Cdd:COG5028 424 --QLREDKESSLLSCKD--SFYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATRP 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 383 KQTFQrvFTKDM--HGQFKMGFGGTLEIKTSREIKISGAIGPCVSlNSKGPCvsenEIGTggtcqwkicgLSPTTTLAIY 460
Cdd:COG5028 493 NDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN-RSSDLC----AFST----------MPRDTSLLVE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 461 FEVVNQHNAPipqggRGAIQFVTQYQHSSGQRRIRVTTIArnwADAQTQIQNIAASFDQEAAAILMARLAIyraeTEEGP 540
Cdd:COG5028 556 FSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKAS----TKALN 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 541 DVLRWLDRQLIRLCQKFGEYHKDD------PSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQ 614
Cdd:COG5028 624 SSLKEARVLINKSMVDILKAYKKElvksntSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQ 703
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 38202214 615 SLIMIQPILYA----YSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQW 667
Cdd:COG5028 704 LMRNIYPTLYAlhdmPIEAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW 760
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
58-97 |
1.45e-15 |
|
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is found to be zinc binding domain.
Pssm-ID: 461437 [Multi-domain] Cd Length: 38 Bit Score: 70.94 E-value: 1.45e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 38202214 58 PVLCSRttCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPS 97
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
632-718 |
8.52e-14 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 66.95 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 632 PEPVLLDSSSILADRILLMDTFFqiliyhgeTIAQWRksGYQDMPEYENFRHLLQAPVDDAQeilhsRFPMPRYIDTEHG 711
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDDDE-----RFPLPEVIRVPQG 69
|
....*..
gi 38202214 712 GSQARFL 718
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
620-718 |
9.26e-14 |
|
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.
Pssm-ID: 200436 Cd Length: 88 Bit Score: 67.39 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202214 620 QPILYAYSFSG--PPEPVLLDSSSILADRILLMDTFFQILIYHGEtiaqwrksgyqdmpeyENFRHLLQAPVDDAQEILH 697
Cdd:cd11280 1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 38202214 698 SRFPMPRYIDTEHGGSQARFL 718
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| |
