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Conserved domains on  [gi|18422356|ref|NP_568626|]
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Sec23/Sec24 protein transport family protein [Arabidopsis thaliana]

Protein Classification

protein transport protein SEC23( domain architecture ID 11476436)

protein transport protein SEC23 is one of the five subunits of coat protein complex II (COPII), which promotes the formation of transport vesicles from the endoplasmic reticulum

PubMed:  18534853

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
1-794 0e+00

transport protein sec23; Provisional


:

Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 1344.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356    1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPF 80
Cdd:PLN00162   1 MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   81 CFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSgsntttptaaaswsngfnqgvrsmpsnssfsslasstvgg 160
Cdd:PLN00162  81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGG---------------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  161 gggviSELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQ 240
Cdd:PLN00162 121 -----APSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  241 IQQFLGLGYSKQFHHGKM--------SAIRKQSFLLPLVECEFNLTSAFEEIIPLV-DVKPGHRPHRSTGAAISTALGLL 311
Cdd:PLN00162 196 ILEQLGLGGKKRRPAGGGiagardglSSSGVNRFLLPASECEFTLNSALEELQKDPwPVPPGHRPARCTGAALSVAAGLL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:PLN00162 276 GACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQV 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:PLN00162 356 GVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSD 435
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQP-GSAFFIQFITRYRYGNGAMRKRVTTVARRWVAG-KSPEISS 549
Cdd:PLN00162 436 TEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPpGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGsSSEELVA 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  550 SFDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:PLN00162 516 GFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNN 595
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  630 SPDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKD 709
Cdd:PLN00162 596 SPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQ 675
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  710 PSHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHT-GGSDIVLTDDMSLQDFLEDLQ 788
Cdd:PLN00162 676 PEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQ 755

                 ....*.
gi 18422356  789 SLAVKG 794
Cdd:PLN00162 756 RLAVQS 761
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
1-794 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 1344.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356    1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPF 80
Cdd:PLN00162   1 MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   81 CFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSgsntttptaaaswsngfnqgvrsmpsnssfsslasstvgg 160
Cdd:PLN00162  81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGG---------------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  161 gggviSELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQ 240
Cdd:PLN00162 121 -----APSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  241 IQQFLGLGYSKQFHHGKM--------SAIRKQSFLLPLVECEFNLTSAFEEIIPLV-DVKPGHRPHRSTGAAISTALGLL 311
Cdd:PLN00162 196 ILEQLGLGGKKRRPAGGGiagardglSSSGVNRFLLPASECEFTLNSALEELQKDPwPVPPGHRPARCTGAALSVAAGLL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:PLN00162 276 GACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQV 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:PLN00162 356 GVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSD 435
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQP-GSAFFIQFITRYRYGNGAMRKRVTTVARRWVAG-KSPEISS 549
Cdd:PLN00162 436 TEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPpGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGsSSEELVA 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  550 SFDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:PLN00162 516 GFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNN 595
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  630 SPDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKD 709
Cdd:PLN00162 596 SPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQ 675
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  710 PSHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHT-GGSDIVLTDDMSLQDFLEDLQ 788
Cdd:PLN00162 676 PEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQ 755

                 ....*.
gi 18422356  789 SLAVKG 794
Cdd:PLN00162 756 RLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
1-794 0e+00

Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 718.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLIC-SRCGAVLNPYARVDYQSRIWSCP 79
Cdd:COG5047   1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  80 FCFHKNLFPRSYSGITETNLPAELFPTYSAVEY-SPLPSRqsgsntttptaaaswsngfnqgvrsmpsnssfsslasstv 158
Cdd:COG5047  81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYtLSKPVI---------------------------------------- 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 159 gggggviseLGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSP 238
Cdd:COG5047 121 ---------LPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 239 DQIQQFLGLgYSKQFHHGKMSAIRKQS------FLLPLVECEFNLTSAFEEIIP-LVDVKPGHRPHRSTGAAISTALGLL 311
Cdd:COG5047 192 ENLQELLAL-SKPTKSGGFESKISGIGqfassrFLLPTQQCEFKLLNILEQLQPdPWPVPAGKRPLRCTGSALNIASSLL 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:COG5047 271 EQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQI 350
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:COG5047 351 GIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISD 430
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQPGSAF-FIQFITRYRYGNGAMRKRVTTVARRWVAGKSPEISSS 550
Cdd:COG5047 431 SEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPKINRS 510
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 551 FDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNS 630
Cdd:COG5047 511 FDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNS 590
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 631 PDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDP 710
Cdd:COG5047 591 PDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQP 670
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 711 SHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHTGGSDIVLTDDMSLQDFLEDLQSL 790
Cdd:COG5047 671 EYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSETILTDDVNLQKFMNHLRKL 750

                ....
gi 18422356 791 AVKG 794
Cdd:COG5047 751 AVSK 754
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
170-419 5.85e-87

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: 276.17  E-value: 5.85e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQIQQFLGLGY 249
Cdd:cd01478   4 PVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 250 SKQ-----FHHGKMSAIRKQS---FLLPLVECEFNLTSAFEEIIPlvD---VKPGHRPHRSTGAAISTALGLLEGCSVTT 318
Cdd:cd01478  84 PAMrpsasQHPGAGNPLPSAAasrFLLPVSQCEFTLTDLLEQLQP--DpwpVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 319 GSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRY 398
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
                       250       260
                ....*....|....*....|.
gi 18422356 399 AVEMSGGFLLLGETFESEQFK 419
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFK 262
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
170-429 3.64e-54

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: 187.07  E-value: 3.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEcskvvvfHGERDLSPDQIQQF 244
Cdd:pfam04811   4 PVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   245 LGLGYSkqfhhgkmsairkqSFLLPLVECEFNLTSAFEEIIPLVDVKpgHRPHRSTGAAISTALGLLEGCsvTTGSRIMV 324
Cdd:pfam04811  77 FLPLPD--------------RFLVPLSECRFVLEDLLEQLPPMFPVT--KRPERCLGPALQAAFLLLKAA--FTGGKIMV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   325 FTSGPATRGPGIIVDSDLSNSirtHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMSG 404
Cdd:pfam04811 139 FQGGLPTVGPGGKLKSRLDES---HHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTG 215
                         250       260
                  ....*....|....*....|....*
gi 18422356   405 GFLLLGETFESEQFKKCLRHIFIRD 429
Cdd:pfam04811 216 GQVYLYPSFQADVDGSKFKQDLQRY 240
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
1-794 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 1344.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356    1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPF 80
Cdd:PLN00162   1 MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   81 CFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSgsntttptaaaswsngfnqgvrsmpsnssfsslasstvgg 160
Cdd:PLN00162  81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGG---------------------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  161 gggviSELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQ 240
Cdd:PLN00162 121 -----APSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  241 IQQFLGLGYSKQFHHGKM--------SAIRKQSFLLPLVECEFNLTSAFEEIIPLV-DVKPGHRPHRSTGAAISTALGLL 311
Cdd:PLN00162 196 ILEQLGLGGKKRRPAGGGiagardglSSSGVNRFLLPASECEFTLNSALEELQKDPwPVPPGHRPARCTGAALSVAAGLL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:PLN00162 276 GACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQV 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:PLN00162 356 GVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSD 435
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQP-GSAFFIQFITRYRYGNGAMRKRVTTVARRWVAG-KSPEISS 549
Cdd:PLN00162 436 TEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPpGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGsSSEELVA 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  550 SFDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:PLN00162 516 GFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNN 595
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  630 SPDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKD 709
Cdd:PLN00162 596 SPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQ 675
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  710 PSHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHT-GGSDIVLTDDMSLQDFLEDLQ 788
Cdd:PLN00162 676 PEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQ 755

                 ....*.
gi 18422356  789 SLAVKG 794
Cdd:PLN00162 756 RLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
1-794 0e+00

Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 718.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLIC-SRCGAVLNPYARVDYQSRIWSCP 79
Cdd:COG5047   1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  80 FCFHKNLFPRSYSGITETNLPAELFPTYSAVEY-SPLPSRqsgsntttptaaaswsngfnqgvrsmpsnssfsslasstv 158
Cdd:COG5047  81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYtLSKPVI---------------------------------------- 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 159 gggggviseLGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSP 238
Cdd:COG5047 121 ---------LPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 239 DQIQQFLGLgYSKQFHHGKMSAIRKQS------FLLPLVECEFNLTSAFEEIIP-LVDVKPGHRPHRSTGAAISTALGLL 311
Cdd:COG5047 192 ENLQELLAL-SKPTKSGGFESKISGIGqfassrFLLPTQQCEFKLLNILEQLQPdPWPVPAGKRPLRCTGSALNIASSLL 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:COG5047 271 EQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQI 350
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:COG5047 351 GIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISD 430
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQPGSAF-FIQFITRYRYGNGAMRKRVTTVARRWVAGKSPEISSS 550
Cdd:COG5047 431 SEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPKINRS 510
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 551 FDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNS 630
Cdd:COG5047 511 FDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNS 590
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 631 PDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDP 710
Cdd:COG5047 591 PDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQP 670
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 711 SHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHTGGSDIVLTDDMSLQDFLEDLQSL 790
Cdd:COG5047 671 EYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSETILTDDVNLQKFMNHLRKL 750

                ....
gi 18422356 791 AVKG 794
Cdd:COG5047 751 AVSK 754
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
170-419 5.85e-87

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: 276.17  E-value: 5.85e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQIQQFLGLGY 249
Cdd:cd01478   4 PVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 250 SKQ-----FHHGKMSAIRKQS---FLLPLVECEFNLTSAFEEIIPlvD---VKPGHRPHRSTGAAISTALGLLEGCSVTT 318
Cdd:cd01478  84 PAMrpsasQHPGAGNPLPSAAasrFLLPVSQCEFTLTDLLEQLQP--DpwpVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 319 GSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRY 398
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
                       250       260
                ....*....|....*....|.
gi 18422356 399 AVEMSGGFLLLGETFESEQFK 419
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFK 262
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
644-764 5.96e-71

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: 228.03  E-value: 5.96e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 644 EGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDPSHETFRNLLEAPE 723
Cdd:cd11287   1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18422356 724 IDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKT 764
Cdd:cd11287  81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
170-429 3.64e-54

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: 187.07  E-value: 3.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEcskvvvfHGERDLSPDQIQQF 244
Cdd:pfam04811   4 PVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   245 LGLGYSkqfhhgkmsairkqSFLLPLVECEFNLTSAFEEIIPLVDVKpgHRPHRSTGAAISTALGLLEGCsvTTGSRIMV 324
Cdd:pfam04811  77 FLPLPD--------------RFLVPLSECRFVLEDLLEQLPPMFPVT--KRPERCLGPALQAAFLLLKAA--FTGGKIMV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   325 FTSGPATRGPGIIVDSDLSNSirtHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMSG 404
Cdd:pfam04811 139 FQGGLPTVGPGGKLKSRLDES---HHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTG 215
                         250       260
                  ....*....|....*....|....*
gi 18422356   405 GFLLLGETFESEQFKKCLRHIFIRD 429
Cdd:pfam04811 216 GQVYLYPSFQADVDGSKFKQDLQRY 240
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
170-428 1.33e-53

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: 185.53  E-value: 1.33e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEC-SKVVVFHGERDLspdqiqq 243
Cdd:cd01468   4 PVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDV------- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 244 FLGlgyskqfhhgkmsaiRKQSFLLPLVECEFNLTSAFEEIIPLVDVKPGHRPHRSTGAAISTALGLLEGCsvTTGSRIM 323
Cdd:cd01468  77 FLP---------------LPDRFLVPLSECKKVIHDLLEQLPPMFWPVPTHRPERCLGPALQAAFLLLKGT--FAGGRII 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 324 VFTSGPATRGPGIIVDSDLSNSIRTHRDiitghVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMS 403
Cdd:cd01468 140 VFQGGLPTVGPGKLKSREDKEPIRSHDE-----AQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKST 214
                       250       260
                ....*....|....*....|....*
gi 18422356 404 GGFLLLGETFESEQFKKCLRHIFIR 428
Cdd:cd01468 215 GGQVYLYDSFQAPNDGSKFKQDLQR 239
Sec23_helical pfam04815
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ...
552-651 1.07e-25

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: 101.81  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   552 DQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYI--QEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:pfam04815   1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCasSSSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
                          90       100
                  ....*....|....*....|...
gi 18422356   630 SP-DETGFFRLMLNREGVVNSII 651
Cdd:pfam04815  81 SPsDERAYARHLLLSLPVEELLL 103
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
12-701 1.45e-19

Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 94.09  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  12 LRWSWNSWPTTKSDCESLVVPLSIMYTPLMH-FSELPTIPYD----PLICSRCGAVLNPYARVDYQSRIWSCPFCFHKNL 86
Cdd:COG5028 153 VRSTMYAIPETNDLLKKSKIPFGLVIRPFLElYPEEDPVPLVedgsIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKND 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356  87 FPRSYSGitetnlpaelfPTYSAVEYSPLPSRQSGSNTTTPTAAASwsngfnqgvrsmpsnssfsslasstvggGGGVIS 166
Cdd:COG5028 233 VPEGFDN-----------PSGPNDPRSDRYSRPELKSGVVDFLAPK----------------------------EYSLRQ 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 167 ELGPAFVFVVDASMVEDELRAVRS------DVLFVIEQLPENCLVALITFDSMVRVYDLgfsecskvvvfhgerdlSPDQ 240
Cdd:COG5028 274 PPPPVYVFLIDVSFEAIKNGLVKAairailENLDQIPNFDPRTKIAIICFDSSLHFFKL-----------------SPDL 336
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 241 IQQFLGLGYSKQFHHGKMSairkQSFLLPLVEC---EFNLTSAFEEIipLVDVkpgHRPHRSTGAAISTALGLLEGCsvt 317
Cdd:COG5028 337 DEQMLIVSDLDEPFLPFPS----GLFVLPLKSCkqiIETLLDRVPRI--FQDN---KSPKNALGPALKAAKSLIGGT--- 404
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 318 tGSRIMVFTSGPATRGPGiivdsdlsnSIRTHRDIITGHVSYYDkscGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELR 397
Cdd:COG5028 405 -GGKIIVFLSTLPNMGIG---------KLQLREDKESSLLSCKD---SFYKEFAIECSKVGISVDLFLTSEDYIDVATLS 471
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 398 YAVEMSGGFLLLGETFESEQFKKCLRhiFIRDADGNLSMyfDVSLEVV----TTKDMRICGALGPVVSlRQKNDIVsete 473
Cdd:COG5028 472 HLCRYTGGQTYFYPNFSATRPNDATK--LANDLVSHLSM--EIGYEAVmrvrCSTGLRVSSFYGNFFN-RSSDLCA---- 542
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 474 igeggtymwkTSTVTNKTCVSFFFHVSNEQNrkpqpGSAFFIQFITRYRYGNGAMRKRVTTVARRwVAGKSPEISSSFDQ 553
Cdd:COG5028 543 ----------FSTMPRDTSLLVEFSIDEKLM-----TSDVYFQVALLYTLNDGERRIRVVNLSLP-TSSSIREVYASADQ 606
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 554 ETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQED--PSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNSP 631
Cdd:COG5028 607 LAIACILAKKASTKALNSSLKEARVLINKSMVDILKAYKKELVKSntSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPS 686
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18422356 632 DETGFFRLMLNREGVVNSIIMIQPTLlrYSF------DGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQW 701
Cdd:COG5028 687 DIRISALNRLTSLPLKQLMRNIYPTL--YALhdmpieAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW 760
Sec23_BS pfam08033
Sec23/Sec24 beta-sandwich domain;
438-540 8.50e-18

Sec23/Sec24 beta-sandwich domain;


Pssm-ID: 429794 [Multi-domain]  Cd Length: 86  Bit Score: 78.73  E-value: 8.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   438 FDVSLEVVTTKDMRICGALGPVVSLrqkndivseteiGEGGTymWKTSTVTNKTCVSFFFhvsnEQNRKPQPGSAFFIQF 517
Cdd:pfam08033   2 FNAVLRVRTSKGLKVSGFIGNFVSR------------SSGDT--WKLPSLDPDTSYAFEF----DIDEPLPNGSNAYIQF 63
                          90       100
                  ....*....|....*....|...
gi 18422356   518 ITRYRYGNGAMRKRVTTVARRWV 540
Cdd:pfam08033  64 ALLYTHSSGERRIRVTTVALPVT 86
zf-Sec23_Sec24 pfam04810
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
53-88 3.21e-14

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: 67.09  E-value: 3.21e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 18422356    53 PLICSRCGAVLNPYARVDYQSRIWSCPFCFHKNLFP 88
Cdd:pfam04810   1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVP 36
Gelsolin pfam00626
Gelsolin repeat;
666-752 3.19e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.63  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356   666 PVPVLLDIRSVTPDVILLFDsyfyvvihHGSKIAQWRKleYHKDPSHETFRNLLEAPEIDaaqlvTDRIPMPRIVRCDQH 745
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLD--------NGFTIFLWVG--KGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69

                  ....*..
gi 18422356   746 GSQARFL 752
Cdd:pfam00626  70 KEPARFL 76
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
170-405 5.86e-10

Sec24-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 24 is very similar to Sec23. 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 carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.


Pssm-ID: 238756 [Multi-domain]  Cd Length: 244  Bit Score: 60.36  E-value: 5.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDE---LRAVRSDVLFVIEQLPE---NCLVALITFDSMVRVYDLgfsecskvvvfhgERDLspDQIQQ 243
Cdd:cd01479   4 AVYVFLIDVSYNAIKsglLATACEALLSNLDNLPGddpRTRVGFITFDSTLHFFNL-------------KSSL--EQPQM 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 244 FLglgyskqfhhgkMSAI------RKQSFLLPLVECEFNLTSAFEEIiPLV--DVKPghrPHRSTGAAISTALGLLEGCs 315
Cdd:cd01479  69 MV------------VSDLddpflpLPDGLLVNLKESRQVIEDLLDQI-PEMfqDTKE---TESALGPALQAAFLLLKET- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 316 vttGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIItgHVSYYDKscgFYKKLAKRLCDSSVVLDVFACSLDQVGAAE 395
Cdd:cd01479 132 ---GGKIIVFQSSLPTLGAGKLKSREDPKLLSTDKEKQ--LLQPQTD---FYKKLALECVKSQISVDLFLFSNQYVDVAT 203
                       250
                ....*....|
gi 18422356 396 LRYAVEMSGG 405
Cdd:cd01479 204 LGCLSRLTGG 213
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
657-756 4.25e-04

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: 40.04  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 657 LLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKiaqwrkleyhkdpsheTFRNLLEAPEIDAAQLVTDRIPM 736
Cdd:cd11280   6 RVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRA----------------SSQAELAAAALLAKELDEERKGK 69
                        90       100
                ....*....|....*....|
gi 18422356 737 PRIVRCdQHGSQARFLLAKL 756
Cdd:cd11280  70 PEIVRI-RQGQEPREFWSLF 88
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
172-216 2.93e-03

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 40.47  E-value: 2.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18422356 172 FVFVVDA--SMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRV 216
Cdd:COG2304  94 LVFVIDVsgSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV 140
 
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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