|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-765 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1151.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAILNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 92 NQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLL 246
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVT 485
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 486 QYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1242862617 726 PSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 765
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-766 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 955.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAILNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 89 FQRNQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLL 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:COG5047 240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:COG5047 320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVT 485
Cdd:COG5047 400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 486 QYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:COG5047 480 TYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1242862617 726 PSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 766
Cdd:COG5047 718 PSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
127-390 |
1.51e-173 |
|
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: 498.82 E-value: 1.51e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 127 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 206
Cdd:cd01478 2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 207 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 284
Cdd:cd01478 82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 285 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 364
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|....*.
gi 1242862617 365 CPNLTGGHMVMGDSFNTSLFKQTFQR 390
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
127-392 |
1.41e-90 |
|
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: 284.14 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 201
Cdd:pfam04811 2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 202 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 281
Cdd:pfam04811 75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 282 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 361
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|....*
gi 1242862617 362 MKCCPNLTGGHMVMGDSFN----TSLFKQTFQRIF 392
Cdd:pfam04811 207 LGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-765 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1151.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAILNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 92 NQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLL 246
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVT 485
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 486 QYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1242862617 726 PSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 765
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-766 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 955.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAILNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 89 FQRNQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLL 246
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:COG5047 240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:COG5047 320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVT 485
Cdd:COG5047 400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 486 QYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:COG5047 480 TYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1242862617 726 PSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 766
Cdd:COG5047 718 PSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
127-390 |
1.51e-173 |
|
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: 498.82 E-value: 1.51e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 127 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 206
Cdd:cd01478 2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 207 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 284
Cdd:cd01478 82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 285 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 364
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|....*.
gi 1242862617 365 CPNLTGGHMVMGDSFNTSLFKQTFQR 390
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
127-392 |
1.41e-90 |
|
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: 284.14 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 201
Cdd:pfam04811 2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 202 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 281
Cdd:pfam04811 75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 282 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 361
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|....*
gi 1242862617 362 MKCCPNLTGGHMVMGDSFN----TSLFKQTFQRIF 392
Cdd:pfam04811 207 LGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
127-390 |
6.41e-87 |
|
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: 274.12 E-value: 6.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGI-SKSYVFRGTKDLTAkqi 200
Cdd:cd01468 2 QPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVFL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 201 qemlgltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRDPWPVtQGKRPLRSTGVALSIAVGLLEGT 280
Cdd:cd01468 79 ------------------------PLPD-RFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 281 FpnTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWhdiekDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLL 360
Cdd:cd01468 133 F--AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVA 205
|
250 260 270
....*....|....*....|....*....|....
gi 1242862617 361 EMKCCPNLTGGHMVMGDSFN----TSLFKQTFQR 390
Cdd:cd01468 206 TLKQLAKSTGGQVYLYDSFQapndGSKFKQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
612-732 |
3.49e-82 |
|
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: 257.30 E-value: 3.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 612 QDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPL 691
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1242862617 692 DDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNN 732
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
520-619 |
5.51e-32 |
|
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: 119.53 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 520 DQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE--DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNN 597
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 1242862617 598 SP-DESSYYRHHFARQDLTQSLI 619
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
403-506 |
3.69e-28 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 108.01 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 403 AFGATLDVKTSRELKIAGAIGPCVSLNVkgpcvsenelgvGGTsqWKICGLDPSSTLGIYFEvvnqHNAPVPQGGRGAIQ 482
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 1242862617 483 FVTQYQHSSTQKRIRVTTIARNWA 506
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
9-664 |
2.28e-16 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 83.69 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 9 QQNEERDGVRFSWNVWP--SSRLEATRmvVPLACLLTPLKE-RPDLPPVQYE----PVLCSRptCKAILNPLCQVDYRAK 81
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQFIEQGR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 82 LWACNFCFQRNQFP-----PAYAGI--SEVNQPAELmpQFSTIEYMIQRGAR----SPLIFLYVVDTCLE--EDDL---- 144
Cdd:COG5028 221 KWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPEL--KSGVVDFLAPKEYSlrqpPPPVYVFLIDVSFEaiKNGLvkaa 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 145 -QALKESLQmSLSLLPPDALVGLITFGRMVqvhelscegisksYVFRGTKDLTAKQIQEMLgltksampvqqarPAQPQe 223
Cdd:COG5028 299 iRAILENLD-QIPNFDPRTKIAIICFDSSL-------------HFFKLSPDLDEQMLIVSD-------------LDEPF- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 224 QPFVSSRFLQPI-HKIDMNLTdLLGELQRDPwpvTQGKRPLRSTGVALSIAVGLLEGtfpnTGARIMLFTGGPPTQGPGM 302
Cdd:COG5028 351 LPFPSGLFVLPLkSCKQIIET-LLDRVPRIF---QDNKSPKNALGPALKAAKSLIGG----TGGKIIVFLSTLPNMGIGK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 303 VvgdELKTPIRSWHDIEKDNarFMKKATKHYemlanrtATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTS 382
Cdd:COG5028 423 L---QLREDKESSLLSCKDS--FYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 383 LFKQTFQriFSKDF--NGDFRMAFGATLDVKTSRELKIAGAIGPcvslnvkgpcVSENELGVGGTSQwkicgLDPSSTLG 460
Cdd:COG5028 491 RPNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGN----------FFNRSSDLCAFST-----MPRDTSLL 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 461 IYFEVVNQHNAPvpqggRGAIQFVTQYQHSSTQKRIRVTTIArnwADAQSQLRHIEAAFDQEAAAVLMARLGVFRAESEE 540
Cdd:COG5028 554 VEFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSS 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 541 GPDVLRWLDRQLIRLCQkfgQYNKE-----DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLT 615
Cdd:COG5028 626 LKEARVLINKSMVDILK---AYKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLK 702
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242862617 616 QSLIMIQPILysYSFHGP--------------PEPVLLDSSSILADRILLMDTFFQIVIYLGE 664
Cdd:COG5028 703 QLMRNIYPTL--YALHDMpieaglpdegllvlPSPINATSSLLESGGLYLIDTGQKIFLWFGK 763
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
58-97 |
2.27e-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: 70.17 E-value: 2.27e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1242862617 58 PVLCSRptCKAILNPLCQVDYRAKLWACNFCFQRNQFPPA 97
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
634-720 |
3.49e-15 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 70.80 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 634 PEPVLLDSSSILADRILLMDTFFqiviylgeTIAQWRkaGYQDMPEYENFKHLLQAPLDDaqeilQARFPMPRYINTEHG 713
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 1242862617 714 GSQARFL 720
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
622-720 |
2.78e-10 |
|
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: 57.38 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862617 622 QPILY--SYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGEtiaqwrkagyqdmpeyENFKHLLQAPLDDAQEILQ 699
Cdd:cd11280 1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 1242862617 700 ARFPMPRYINTEHGGSQARFL 720
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| |
