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Conserved domains on  [gi|1242862660|ref|NP_001342308|]
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protein transport protein Sec23B isoform 1 [Mus musculus]

Protein Classification

protein transport protein sec23( domain architecture ID 1004043)

protein transport protein sec23 is a component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER)

CATH:  1.20.120.730
Gene Ontology:  GO:0006886|GO:0008270|GO:0005096
PubMed:  8898360|18534853

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN00162 super family cl33419
transport protein sec23; Provisional
12-765 0e+00

transport protein sec23; Provisional


The actual alignment was detected with superfamily member PLN00162:

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 1242862660  12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAILNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162    7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  92 NQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:PLN00162   85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLL 246
Cdd:PLN00162  165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:PLN00162  245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:PLN00162  325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVT 485
Cdd:PLN00162  405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 486 QYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:PLN00162  485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:PLN00162  564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:PLN00162  644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 1242862660 726 PSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 765
Cdd:PLN00162  724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
 
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 1242862660  12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAILNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162    7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  92 NQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:PLN00162   85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLL 246
Cdd:PLN00162  165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:PLN00162  245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:PLN00162  325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVT 485
Cdd:PLN00162  405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 486 QYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:PLN00162  485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:PLN00162  564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:PLN00162  644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 1242862660 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 1242862660   9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAILNPLCQVDYRAKLWACNFC 88
Cdd:COG5047     4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  89 FQRNQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:COG5047    83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLL 246
Cdd:COG5047   163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:COG5047   240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:COG5047   320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVT 485
Cdd:COG5047   400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 486 QYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:COG5047   480 TYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:COG5047   558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:COG5047   638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 1242862660 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 1242862660 127 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 206
Cdd:cd01478     2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 207 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 284
Cdd:cd01478    82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 285 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 364
Cdd:cd01478   162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
                         250       260
                  ....*....|....*....|....*.
gi 1242862660 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 1242862660 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 201
Cdd:pfam04811   2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 202 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 281
Cdd:pfam04811  75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 282 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 361
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1242862660 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 1242862660  12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAILNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162    7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  92 NQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:PLN00162   85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLIT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLL 246
Cdd:PLN00162  165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:PLN00162  245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:PLN00162  325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVT 485
Cdd:PLN00162  405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 486 QYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:PLN00162  485 RYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:PLN00162  564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:PLN00162  644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 1242862660 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 1242862660   9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAILNPLCQVDYRAKLWACNFC 88
Cdd:COG5047     4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  89 FQRNQFPPAYAGISEVNQPAELMPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLIT 168
Cdd:COG5047    83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 169 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLL 246
Cdd:COG5047   163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 247 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFM 326
Cdd:COG5047   240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 327 KKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGA 406
Cdd:COG5047   320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 407 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVT 485
Cdd:COG5047   400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 486 QYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 565
Cdd:COG5047   480 TYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 566 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 645
Cdd:COG5047   558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 646 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 725
Cdd:COG5047   638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 1242862660 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 1242862660 127 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 206
Cdd:cd01478     2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 207 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 284
Cdd:cd01478    82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 285 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 364
Cdd:cd01478   162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
                         250       260
                  ....*....|....*....|....*.
gi 1242862660 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 1242862660 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 201
Cdd:pfam04811   2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 202 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 281
Cdd:pfam04811  75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 282 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 361
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1242862660 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 1242862660 127 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGI-SKSYVFRGTKDLTAkqi 200
Cdd:cd01468     2 QPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVFL--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 201 qemlgltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRDPWPVtQGKRPLRSTGVALSIAVGLLEGT 280
Cdd:cd01468    79 ------------------------PLPD-RFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGT 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 281 FpnTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWhdiekDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLL 360
Cdd:cd01468   133 F--AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVA 205
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1242862660 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 1242862660 612 QDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPL 691
Cdd:cd11287     1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1242862660 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 1242862660 520 DQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE--DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNN 597
Cdd:pfam04815   1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
                          90       100
                  ....*....|....*....|...
gi 1242862660 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 1242862660 403 AFGATLDVKTSRELKIAGAIGPCVSLNVkgpcvsenelgvGGTsqWKICGLDPSSTLGIYFEvvnqHNAPVPQGGRGAIQ 482
Cdd:pfam08033   1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
                          90       100
                  ....*....|....*....|....
gi 1242862660 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 1242862660   9 QQNEERDGVRFSWNVWP--SSRLEATRmvVPLACLLTPLKE-RPDLPPVQYE----PVLCSRptCKAILNPLCQVDYRAK 81
Cdd:COG5028   145 QSNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQFIEQGR 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660  82 LWACNFCFQRNQFP-----PAYAGI--SEVNQPAELmpQFSTIEYMIQRGAR----SPLIFLYVVDTCLE--EDDL---- 144
Cdd:COG5028   221 KWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPEL--KSGVVDFLAPKEYSlrqpPPPVYVFLIDVSFEaiKNGLvkaa 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 145 -QALKESLQmSLSLLPPDALVGLITFGRMVqvhelscegisksYVFRGTKDLTAKQIQEMLgltksampvqqarPAQPQe 223
Cdd:COG5028   299 iRAILENLD-QIPNFDPRTKIAIICFDSSL-------------HFFKLSPDLDEQMLIVSD-------------LDEPF- 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 224 QPFVSSRFLQPI-HKIDMNLTdLLGELQRDPwpvTQGKRPLRSTGVALSIAVGLLEGtfpnTGARIMLFTGGPPTQGPGM 302
Cdd:COG5028   351 LPFPSGLFVLPLkSCKQIIET-LLDRVPRIF---QDNKSPKNALGPALKAAKSLIGG----TGGKIIVFLSTLPNMGIGK 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 303 VvgdELKTPIRSWHDIEKDNarFMKKATKHYemlanrtATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTS 382
Cdd:COG5028   423 L---QLREDKESSLLSCKDS--FYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT 490
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 383 LFKQTFQriFSKDF--NGDFRMAFGATLDVKTSRELKIAGAIGPcvslnvkgpcVSENELGVGGTSQwkicgLDPSSTLG 460
Cdd:COG5028   491 RPNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGN----------FFNRSSDLCAFST-----MPRDTSLL 553
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 461 IYFEVVNQHNAPvpqggRGAIQFVTQYQHSSTQKRIRVTTIArnwADAQSQLRHIEAAFDQEAAAVLMARLGVFRAESEE 540
Cdd:COG5028   554 VEFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSS 625
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862660 541 GPDVLRWLDRQLIRLCQkfgQYNKE-----DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLT 615
Cdd:COG5028   626 LKEARVLINKSMVDILK---AYKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLK 702
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242862660 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 1242862660  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 1242862660 634 PEPVLLDSSSILADRILLMDTFFqiviylgeTIAQWRkaGYQDMPEYENFKHLLQAPLDDaqeilQARFPMPRYINTEHG 713
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69

                  ....*..
gi 1242862660 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 1242862660 622 QPILY--SYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGEtiaqwrkagyqdmpeyENFKHLLQAPLDDAQEILQ 699
Cdd:cd11280     1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
                          90       100
                  ....*....|....*....|.
gi 1242862660 700 ARFPMPRYINTEHGGSQARFL 720
Cdd:cd11280    65 ERKGKPEIVRIRQGQEPREFW 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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