|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-787 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1171.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 12 EERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsrTTCRAVLNPLCQVDYRAKLWACNFCYQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 92 NQFPPSYAGISELNQPAELLPQFSSIEYVVLR---GPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLL 244
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 245 GELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYV 324
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 325 KKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGG 404
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 405 TLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVT 483
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 484 QYQHSSGQRRIRVTTIARNWADAqTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD 563
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 564 DPSSFRFSETFSLYPQrrdfpktsgeilenqekarsaclkFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMI 643
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQ------------------------FMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMI 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 644 QPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSR 723
Cdd:PLN00162 620 QPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKER 699
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530402948 724 FPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 787
Cdd:PLN00162 700 FPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-788 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 936.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsRTTCRAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 89 YQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKV--PLTQATRGPQVQQPPPSnRFLQPVQKIDMNLTDLLGE 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFASS-RFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 247 LQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKK 326
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 327 GTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTL 406
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 407 EIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGG-RGAIQFVTQY 485
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 486 QHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDP 565
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 566 SSFRFSETFSLYPQrrdfpktsgeilenqekarsaclkFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQP 645
Cdd:COG5047 560 SSFRLDPNFTLYPQ------------------------FMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQP 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 646 ILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFP 725
Cdd:COG5047 616 TLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFP 695
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530402948 726 MPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 788
Cdd:COG5047 696 IPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
126-388 |
3.57e-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: 475.32 E-value: 3.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 126 QMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 205
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 206 LSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPN 281
Cdd:cd01478 81 LGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 282 TGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMK 361
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 530402948 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 |
3.15e-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: 291.46 E-value: 3.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 200
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 201 QEMLglskvpltqatrgpqvqqPPPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFp 280
Cdd:pfam04811 74 QDMF------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 281 nTGARIMMFIGGPATQGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEM 360
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 530402948 361 KCCPNLTGGYMVMGDSFN----TSLFKQTFQRVF 390
Cdd:pfam04811 208 GQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-787 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1171.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 12 EERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsrTTCRAVLNPLCQVDYRAKLWACNFCYQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 92 NQFPPSYAGISELNQPAELLPQFSSIEYVVLR---GPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPgsgGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLL 244
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 245 GELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYV 324
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 325 KKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGG 404
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 405 TLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVT 483
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 484 QYQHSSGQRRIRVTTIARNWADAqTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD 563
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 564 DPSSFRFSETFSLYPQrrdfpktsgeilenqekarsaclkFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMI 643
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQ------------------------FMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMI 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 644 QPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSR 723
Cdd:PLN00162 620 QPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKER 699
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530402948 724 FPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLKKLAVSS 787
Cdd:PLN00162 700 FPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-788 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 936.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCsRTTCRAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 89 YQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 169 FGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKV--PLTQATRGPQVQQPPPSnRFLQPVQKIDMNLTDLLGE 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPtkSGGFESKISGIGQFASS-RFLLPTQQCEFKLLNILEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 247 LQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKK 326
Cdd:COG5047 242 LQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 327 GTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTL 406
Cdd:COG5047 322 ATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 407 EIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGG-RGAIQFVTQY 485
Cdd:COG5047 402 EVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 486 QHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDP 565
Cdd:COG5047 482 QHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 566 SSFRFSETFSLYPQrrdfpktsgeilenqekarsaclkFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQP 645
Cdd:COG5047 560 SSFRLDPNFTLYPQ------------------------FMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQP 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 646 ILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFP 725
Cdd:COG5047 616 TLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFP 695
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530402948 726 MPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 788
Cdd:COG5047 696 IPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
126-388 |
3.57e-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: 475.32 E-value: 3.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 126 QMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLG 205
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 206 LSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPN 281
Cdd:cd01478 81 LGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 282 TGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMK 361
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 530402948 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 |
3.15e-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: 291.46 E-value: 3.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGisksyvfRGTKDLSAKQL 200
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 201 QEMLglskvpltqatrgpqvqqPPPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFp 280
Cdd:pfam04811 74 QDMF------------------LPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 281 nTGARIMMFIGGPATQGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEM 360
Cdd:pfam04811 132 -TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATL 207
|
250 260 270
....*....|....*....|....*....|....
gi 530402948 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 ... |
634-754 |
2.66e-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: 263.47 E-value: 2.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 634 QDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPV 713
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 530402948 714 DDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNN 754
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
126-388 |
5.17e-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: 261.80 E-value: 5.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 126 QMPLIFLYVVDTCME---DEDLQALKESMQMSLSLLP--PTALVGLITFGRMVQVHELGCEGI-SKSYVFRGTKDLsakq 199
Cdd:cd01468 1 PQPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 200 lqemlglskvpltqatrgpqvqQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPqGKRPLRSSGVALSIAVGLLECTF 279
Cdd:cd01468 77 ----------------------FLPLPDRFLVPLSECKKVIHDLLEQLPPMFWPVP-THRPERCLGPALQAAFLLLKGTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 280 pnTGARIMMFIGGPATQGPGMVVGDELKTPIRSWhdidkDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLE 359
Cdd:cd01468 134 --AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|...
gi 530402948 360 MKCCPNLTGGYMVMGDSFN----TSLFKQTFQR 388
Cdd:cd01468 207 LKQLAKSTGGQVYLYDSFQapndGSKFKQDLQR 239
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
401-504 |
5.01e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 119.18 E-value: 5.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 401 GFGGTLEIKTSREIKISGAIGPCVSLNSkgpcvseneigtGGTcqWKICGLSPTTTLAIYFEvvnqHNAPIPQGGRGAIQ 480
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 530402948 481 FVTQYQHSSGQRRIRVTTIARNWA 504
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
518-641 |
7.16e-29 |
|
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: 111.06 E-value: 7.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 518 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD--DPSSFRFSETFSLYPQrrdfpktsgeilenqe 595
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPL---------------- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530402948 596 karsaclkFMFHLRRSSFLQVFNNSP-DESSYYRHHFMRQDLTQSLI 641
Cdd:pfam04815 65 --------YMLALLKSPALRGGNSSPsDERAYARHLLLSLPVEELLL 103
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
58-97 |
1.63e-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: 70.55 E-value: 1.63e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530402948 58 PVLCSRttCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPS 97
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
9-691 |
2.82e-15 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 80.22 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 9 QQNEERDGVRFSWNVWP--SSRLEATRmvVPVAALFTPLKE-RPDLPPIQYE----PVLCSRttCRAVLNPLCQVDYRAK 81
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQFIEQGR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 82 LWACNFCYQRNQFP-----PSYAGI--SELNQPAELLpqFSSIEYVV-----LRGPQmPLIFLYVVDT---CMEDEDLQA 146
Cdd:COG5028 221 KWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPELK--SGVVDFLApkeysLRQPP-PPVYVFLIDVsfeAIKNGLVKA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 147 LKESMQMSLSLLP---PTALVGLITFGRMVqvhelgcegisksYVFRGTKDLSAKQLqemlglskvpLTQATRGPQVqqP 223
Cdd:COG5028 298 AIRAILENLDQIPnfdPRTKIAIICFDSSL-------------HFFKLSPDLDEQML----------IVSDLDEPFL--P 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 224 PPSNRFLQPVQKIDMNLTDLLGELQRdpwpVPQGKR-PLRSSGVALSIAVGLLEctfpNTGARIMMFIGGPATQGPGMVv 302
Cdd:COG5028 353 FPSGLFVLPLKSCKQIIETLLDRVPR----IFQDNKsPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNMGIGKL- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 303 gdELKTPIRSWHDIDKDnaKYVKKGTKHFealanraATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLF 382
Cdd:COG5028 424 --QLREDKESSLLSCKD--SFYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATRP 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 383 KQTFQrvFTKDM--HGQFKMGFGGTLEIKTSREIKISGAIGPCVSlNSKGPCvsenEIGTggtcqwkicgLSPTTTLAIY 460
Cdd:COG5028 493 NDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN-RSSDLC----AFST----------MPRDTSLLVE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 461 FEVVNQHNAPipqggRGAIQFVTQYQHSSGQRRIRVTTIArnwADAQTQIQNIAASFDQEAAAILMARLAIyraeTEEGP 540
Cdd:COG5028 556 FSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKAS----TKALN 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 541 DVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQRRDFPktsgeilenqekarsaclKFMFHLRRSSFLQVFNNS 620
Cdd:COG5028 624 SSLKEARVLINKSMVDILKAYKKELVKSNTSTQLPLPANLKLLP------------------LLMLALLKSSAFRSGSTP 685
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530402948 621 PDESSYYRHHFMRQDLTQSLIMIQPILYA----YSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQW 691
Cdd:COG5028 686 SDIRISALNRLTSLPLKQLMRNIYPTLYAlhdmPIEAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW 760
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
656-742 |
8.22e-14 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 66.95 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 656 PEPVLLDSSSILADRILLMDTFFqiliyhgeTIAQWRksGYQDMPEYENFRHLLQAPVDDAQeilhsRFPMPRYIDTEHG 735
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDDDE-----RFPLPEVIRVPQG 69
|
....*..
gi 530402948 736 GSQARFL 742
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
644-742 |
9.57e-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: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402948 644 QPILYAYSFSG--PPEPVLLDSSSILADRILLMDTFFQILIYHGEtiaqwrksgyqdmpeyENFRHLLQAPVDDAQEILH 721
Cdd:cd11280 1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 530402948 722 SRFPMPRYIDTEHGGSQARFL 742
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| |
