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Conserved domains on  [gi|42562156|ref|NP_173317|]
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Transducin/WD40 repeat-like superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
80-327 1.25e-29

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  80 DG-LIAGGLVDGNIGLWNPissESGEIahVRDLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLANPsKPSHYLK 156
Cdd:COG2319 131 DGkTLASGSADGTVRLWDL---ATGKL--LRTLTGHSGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATG-KLLRTLT 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 157 GTgsymQSEISSLSWN-KGfqHVLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpn 232
Cdd:COG2319 202 GH----TGAVRSVAFSpDG--KLLASGSADGTVRLWDLATGKLLRTLTGhsgSVRS--VAFSPD--GRLLASGSADGT-- 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 233 VKLLDIRyLQSPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVIS 312
Cdd:COG2319 270 VRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS 347

                       250
                ....*....|....*
gi 42562156 313 ASSvDGKIGIYNLEG 327
Cdd:COG2319 348 GSD-DGTVRLWDLAT 361
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 495-716 1.24e-06

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


The actual alignment was detected with superfamily member cd09233:

Pssm-ID: 449359 [Multi-domain]  Cd Length: 314  Bit Score: 51.49  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 495 SDPTFDDAIQRSLIVGDYKEAVaQCFSANKM-ADALVIAHVGGTELWESTRDKYIRMSNAPY--MKVVSAMMNN------ 565
Cdd:cd09233  61 AEQKALNRFRNLLLTGNRKEAL-ELALDNGLwAHALLLASSLGKETWAEVVSRFARSESKLNdpLQTLYQLFSGnspeai 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 566 DLMTYLHTRQP---KSWKETLALICTFAEGDE----WISLCDALASNlmaaGFTLAATLCYICAG--------NVDKTVD 630
Cdd:cd09233 140 TELADNPAEAEwalGNWREHLAIILSNRTSNLdleaLVELGDLLAQR----GLVEAAHICYLLAGvplgpypsSPSSCLL 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 631 IWSMSLEKQSAGKSyAECVQdLMEkTLVLALTTCNKRVS-ASLR--KLFesYAEILASQGLIATAMK----FLKLLESGD 703
Cdd:cd09233 216 GGAVHNKSPRTFAT-PEAIQ-LTE-IYEYALSLGNPQFGlPHLQpyKLI--HAARLAELGLVSEALKyceaIASSLKSLT 290

                       250       260
                ....*....|....*....|.
gi 42562156 704 FSP--------ELSILRDRIS 716
Cdd:cd09233 291 KSPyydpnllaQLQDLSERLS 311
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 719-867 1.61e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.93  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   719 AEPEAANTSASTNTQ------PKISNPYQEKSFTPAP---LSNAQPSRSItFFP-----LNPPRELKNADQYQQPTMDYH 784
Cdd:PRK10263  695 AEAELARQFAQTQQQrysgeqPAGANPFSLDDFEFSPmkaLLDDGPHEPL-FTPivepvQQPQQPVAPQQQYQQPQQPVA 773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   785 SFNRSAGPAYNAPPGPgSYRSIHSQVGPYINSKIPQtvappvRPMTPTHQVAVQPEPVAPPPTVQTADTSNVPAHQKPIV 864
Cdd:PRK10263  774 PQPQYQQPQQPVAPQP-QYQQPQQPVAPQPQYQQPQ------QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLL 846


                  ...
gi 42562156   865 ASL 867
Cdd:PRK10263  847 HPL 849
RMtype1_S_TRD-CR_like super family cl38903
Type I restriction-modification system specificity (S) subunit Target Recognition ...
 328-409 5.56e-03

Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR) and similar domains; The restriction-modification (RM) system S subunit generally consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This superfamily represents a single TRD-CR unit; in addition to type I TRD-CR units, it includes RMtype1_S_TRD-CR_like domains of various putative Helicobacter type II restriction enzymes and methyltransferases, such as Hci611ORFHP and HfeORF12890P, as well as TRD-CR-like sequence-recognition domains of the M subunit of putative type I DNA methyltransferase such as M2.CinURNWORF2828P and M.Mae7806ORF3969P.


The actual alignment was detected with superfamily member cd17498:

Pssm-ID: 365779 [Multi-domain]  Cd Length: 173  Bit Score: 38.82  E-value: 5.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 328 CSSYGTENQQHFLFHLLDADpltAPKWWKRPAGASFGfggkliSFNKNLPEASEVFLHSLATEKSLVNRISKFEAALENG 407
Cdd:cd17498  84 CSIRMKNGNNSFLYYLLKNN---IKNLINKSSGTVFG------SINKDDIENLEVDIPEDEEQKRIANILSKIDDKIEIN 154


                ..
gi 42562156 408 EK 409
Cdd:cd17498 155 NQ 156
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
80-327 1.25e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  80 DG-LIAGGLVDGNIGLWNPissESGEIahVRDLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLANPsKPSHYLK 156
Cdd:COG2319 131 DGkTLASGSADGTVRLWDL---ATGKL--LRTLTGHSGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATG-KLLRTLT 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 157 GTgsymQSEISSLSWN-KGfqHVLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpn 232
Cdd:COG2319 202 GH----TGAVRSVAFSpDG--KLLASGSADGTVRLWDLATGKLLRTLTGhsgSVRS--VAFSPD--GRLLASGSADGT-- 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 233 VKLLDIRyLQSPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVIS 312
Cdd:COG2319 270 VRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS 347

                       250
                ....*....|....*
gi 42562156 313 ASSvDGKIGIYNLEG 327
Cdd:COG2319 348 GSD-DGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-324 9.86e-29

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 117.05  E-value: 9.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  13 VAIAPESPFIAAGtmagavdlsfssSANLEIFELDFQSNDRELKLVGQCQSSERFNRLAWGSYgsgsdgLIAGGLvDGNI 92
Cdd:cd00200  15 VAFSPDGKLLATG------------SGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY------LASGSS-DKTI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  93 GLWNPISSESgeiahVRDLSKHKGPVRGLEFnvkSPNQ--LASGADDGTVCIWDLANPsKPSHYLKGTGSYmqseISSLS 170
Cdd:cd00200  76 RLWDLETGEC-----VRTLTGHTSYVSSVAF---SPDGriLSSSSRDKTIKVWDVETG-KCLTTLRGHTDW----VNSVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 171 WNkGFQHVLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpnVKLLDIRyLQSPVRT 247
Cdd:cd00200 143 FS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGhtgEVNS--VAFSPD--GEKLLSSSSDGT--IKLWDLS-TGKCLGT 214

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42562156 248 FVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVISASSvDGKIGIYN 324
Cdd:cd00200 215 LRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA-DGTIRIWD 289
PTZ00420 PTZ00420
coronin; Provisional
 79-214 1.90e-08

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 58.04  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   79 SDGLIA-------GGLVdGNIGLWNPISSESgeiahVRDLSKHKGPVRGLEFNVKSPNQLASGADDGTVCIWDLANPSK- 150
Cdd:PTZ00420  37 SSGFVAvpwevegGGLI-GAIRLENQMRKPP-----VIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDEs 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  151 ------PSHYLKGtgsyMQSEISSLSWNKGFQHVLASTSHNGTTVIWDVNNEKIITDLKTTVRCSVLQWD 214
Cdd:PTZ00420 111 vkeikdPQCILKG----HKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWN 176
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 495-716 1.24e-06

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 51.49  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 495 SDPTFDDAIQRSLIVGDYKEAVaQCFSANKM-ADALVIAHVGGTELWESTRDKYIRMSNAPY--MKVVSAMMNN------ 565
Cdd:cd09233  61 AEQKALNRFRNLLLTGNRKEAL-ELALDNGLwAHALLLASSLGKETWAEVVSRFARSESKLNdpLQTLYQLFSGnspeai 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 566 DLMTYLHTRQP---KSWKETLALICTFAEGDE----WISLCDALASNlmaaGFTLAATLCYICAG--------NVDKTVD 630
Cdd:cd09233 140 TELADNPAEAEwalGNWREHLAIILSNRTSNLdleaLVELGDLLAQR----GLVEAAHICYLLAGvplgpypsSPSSCLL 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 631 IWSMSLEKQSAGKSyAECVQdLMEkTLVLALTTCNKRVS-ASLR--KLFesYAEILASQGLIATAMK----FLKLLESGD 703
Cdd:cd09233 216 GGAVHNKSPRTFAT-PEAIQ-LTE-IYEYALSLGNPQFGlPHLQpyKLI--HAARLAELGLVSEALKyceaIASSLKSLT 290

                       250       260
                ....*....|....*....|.
gi 42562156 704 FSP--------ELSILRDRIS 716
Cdd:cd09233 291 KSPyydpnllaQLQDLSERLS 311
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 719-867 1.61e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.93  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   719 AEPEAANTSASTNTQ------PKISNPYQEKSFTPAP---LSNAQPSRSItFFP-----LNPPRELKNADQYQQPTMDYH 784
Cdd:PRK10263  695 AEAELARQFAQTQQQrysgeqPAGANPFSLDDFEFSPmkaLLDDGPHEPL-FTPivepvQQPQQPVAPQQQYQQPQQPVA 773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   785 SFNRSAGPAYNAPPGPgSYRSIHSQVGPYINSKIPQtvappvRPMTPTHQVAVQPEPVAPPPTVQTADTSNVPAHQKPIV 864
Cdd:PRK10263  774 PQPQYQQPQQPVAPQP-QYQQPQQPVAPQPQYQQPQ------QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLL 846


                  ...
gi 42562156   865 ASL 867
Cdd:PRK10263  847 HPL 849
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 108-144 2.38e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.30  E-value: 2.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 42562156    108 VRDLSKHKGPVRGLEFNvKSPNQLASGADDGTVCIWD 144
Cdd:smart00320   5 LKTLKGHTGPVTSVAFS-PDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
108-144 1.16e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 42562156   108 VRDLSKHKGPVRGLEFNvKSPNQLASGADDGTVCIWD 144
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFS-PDGKLLASGSDDGTVKVWD 39
RMtype1_S_Aco12261I-TRD1-CR1_like cd17498
Type I restriction-modification system specificity (S) subunit Target Recognition ...
 328-409 5.56e-03

Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) TRD1-CR1; The S.Aco12261I S subunit recognizes 5'... GCANNNNNNTGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.Aco12261I TRD2-CR2 does not belong to this subfamily.


Pssm-ID: 341189 [Multi-domain]  Cd Length: 173  Bit Score: 38.82  E-value: 5.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 328 CSSYGTENQQHFLFHLLDADpltAPKWWKRPAGASFGfggkliSFNKNLPEASEVFLHSLATEKSLVNRISKFEAALENG 407
Cdd:cd17498  84 CSIRMKNGNNSFLYYLLKNN---IKNLINKSSGTVFG------SINKDDIENLEVDIPEDEEQKRIANILSKIDDKIEIN 154


                ..
gi 42562156 408 EK 409
Cdd:cd17498 155 NQ 156
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
80-327 1.25e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  80 DG-LIAGGLVDGNIGLWNPissESGEIahVRDLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLANPsKPSHYLK 156
Cdd:COG2319 131 DGkTLASGSADGTVRLWDL---ATGKL--LRTLTGHSGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATG-KLLRTLT 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 157 GTgsymQSEISSLSWN-KGfqHVLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpn 232
Cdd:COG2319 202 GH----TGAVRSVAFSpDG--KLLASGSADGTVRLWDLATGKLLRTLTGhsgSVRS--VAFSPD--GRLLASGSADGT-- 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 233 VKLLDIRyLQSPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVIS 312
Cdd:COG2319 270 VRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS 347

                       250
                ....*....|....*
gi 42562156 313 ASSvDGKIGIYNLEG 327
Cdd:COG2319 348 GSD-DGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-324 9.86e-29

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 117.05  E-value: 9.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  13 VAIAPESPFIAAGtmagavdlsfssSANLEIFELDFQSNDRELKLVGQCQSSERFNRLAWGSYgsgsdgLIAGGLvDGNI 92
Cdd:cd00200  15 VAFSPDGKLLATG------------SGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY------LASGSS-DKTI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  93 GLWNPISSESgeiahVRDLSKHKGPVRGLEFnvkSPNQ--LASGADDGTVCIWDLANPsKPSHYLKGTGSYmqseISSLS 170
Cdd:cd00200  76 RLWDLETGEC-----VRTLTGHTSYVSSVAF---SPDGriLSSSSRDKTIKVWDVETG-KCLTTLRGHTDW----VNSVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 171 WNkGFQHVLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpnVKLLDIRyLQSPVRT 247
Cdd:cd00200 143 FS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGhtgEVNS--VAFSPD--GEKLLSSSSDGT--IKLWDLS-TGKCLGT 214

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42562156 248 FVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVISASSvDGKIGIYN 324
Cdd:cd00200 215 LRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA-DGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
80-327 4.28e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 118.09  E-value: 4.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  80 DG-LIAGGLVDGNIGLWNPissESGEIAHVrdLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLANPsKPSHYLK 156
Cdd:COG2319 173 DGkLLASGSDDGTVRLWDL---ATGKLLRT--LTGHTGAVRSVAF---SPDgkLLASGSADGTVRLWDLATG-KLLRTLT 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 157 GTGSYmqseISSLSWNKGFQHvLASTSHNGTTVIWDVNNEKIITDLKT---TVRCsvLQWDPDhfNQILVASDEDSSpnV 233
Cdd:COG2319 244 GHSGS----VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGhsgGVNS--VAFSPD--GKLLASGSDDGT--V 312

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 234 KLLDIRyLQSPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKMPGVISA 313
Cdd:COG2319 313 RLWDLA-TGKLLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390

                       250
                ....*....|....
gi 42562156 314 SSvDGKIGIYNLEG 327
Cdd:COG2319 391 SA-DGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 107-326 8.10e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 105.49  E-value: 8.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 107 HVRDLSKHKGPVRGLEFNVKSP-----------------------------------------NQLASGADDGTVCIWDL 145
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKllatgsgdgtikvwdletgellrtlkghtgpvrdvaasadgTYLASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 146 ANPsKPSHYLKGtgsyMQSEISSLSWNKGfQHVLASTSHNGTTVIWDVNNEKIITDLKtTVRCSVLQWDPDHFNQILVAS 225
Cdd:cd00200  81 ETG-ECVRTLTG----HTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSPDGTFVASS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 226 DEDSSpnVKLLDIRYLqSPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYP 305
Cdd:cd00200 154 SQDGT--IKLWDLRTG-KCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260
                ....*....|....*....|.
gi 42562156 306 KmPGVISASSVDGKIGIYNLE 326
Cdd:cd00200 230 D-GYLLASGSEDGTIRVWDLR 249
WD40 COG2319
WD40 repeat [General function prediction only];
69-327 7.42e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 99.22  E-value: 7.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  69 RLAWGSYGSGSDGLIAGGLVDGNIGLWNPISSesgeiAHVRDLSKHKGPVRGLEFNVkSPNQLASGADDGTVCIWDLANP 148
Cdd:COG2319  37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAG-----ALLATLLGHTAAVLSVAFSP-DGRLLASASADGTVRLWDLATG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 149 SKPSHYLKGTGSymqseISSLSWNKGfQHVLASTSHNGTTVIWDVNNEKIITDLK---TTVRCsvLQWDPDhfNQILVAS 225
Cdd:COG2319 111 LLLRTLTGHTGA-----VRSVAFSPD-GKTLASGSADGTVRLWDLATGKLLRTLTghsGAVTS--VAFSPD--GKLLASG 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 226 DEDSSpnVKLLDIRYLQsPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYP 305
Cdd:COG2319 181 SDDGT--VRLWDLATGK-LLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP 256

                       250       260
                ....*....|....*....|...
gi 42562156 306 KmpG-VISASSVDGKIGIYNLEG 327
Cdd:COG2319 257 D--GrLLASGSADGTVRLWDLAT 277
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-333 2.29e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 2.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 164 SEISSLSWNKGFQHvLASTSHNGTTVIWDVNNEKIITDLK------TTVRCSvlqwdpDHFNQILVASDeDSSpnVKLLD 237
Cdd:cd00200  10 GGVTCVAFSPDGKL-LATGSGDGTIKVWDLETGELLRTLKghtgpvRDVAAS------ADGTYLASGSS-DKT--IRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 238 IRyLQSPVRTFVGHQRGVIAMEWCPSDSLyLLTCGKDNRTICWNTKTGKIVAELPTGQNWNFDVHWYPKmPGVISASSVD 317
Cdd:cd00200  80 LE-TGECVRTLTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPD-GTFVASSSQD 156

                       170
                ....*....|....*.
gi 42562156 318 GKIGIYNLEGCSSYGT 333
Cdd:cd00200 157 GTIKLWDLRTGKCVAT 172
WD40 COG2319
WD40 repeat [General function prediction only];
13-239 1.91e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 1.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  13 VAIAPESPFIAAGTMAGAVDLsFSSSANLEIFELDFQSNdrelklvgqcqsseRFNRLAWGSYGSgsdgLIAGGLVDGNI 92
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRL-WDLATGKLLRTLTGHSG--------------SVRSVAFSPDGR----LLASGSADGTV 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  93 GLWNPissESGEIahVRDLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLANPsKPSHYLKGTGsymqSEISSLS 170
Cdd:COG2319 271 RLWDL---ATGEL--LRTLTGHSGGVNSVAF---SPDgkLLASGSDDGTVRLWDLATG-KLLRTLTGHT----GAVRSVA 337

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42562156 171 WN-KGfqHVLASTSHNGTTVIWDVNNEKIITDLKT-TVRCSVLQWDPDhfNQILVASDEDSSpnVKLLDIR 239
Cdd:COG2319 338 FSpDG--KTLASGSDDGTVRLWDLATGELLRTLTGhTGAVTSVAFSPD--GRTLASGSADGT--VRLWDLA 402
PTZ00420 PTZ00420
coronin; Provisional
 79-214 1.90e-08

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 58.04  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   79 SDGLIA-------GGLVdGNIGLWNPISSESgeiahVRDLSKHKGPVRGLEFNVKSPNQLASGADDGTVCIWDLANPSK- 150
Cdd:PTZ00420  37 SSGFVAvpwevegGGLI-GAIRLENQMRKPP-----VIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDEs 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  151 ------PSHYLKGtgsyMQSEISSLSWNKGFQHVLASTSHNGTTVIWDVNNEKIITDLKTTVRCSVLQWD 214
Cdd:PTZ00420 111 vkeikdPQCILKG----HKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWN 176
WD40 COG2319
WD40 repeat [General function prediction only];
13-147 8.63e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 8.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  13 VAIAPESPFIAAGTMAGAVDLsfsssanleifeLDFQSNDRELKLVGqcqSSERFNRLAWgsygSGSDGLIAGGLVDGNI 92
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRL------------WDLATGKLLRTLTG---HTGAVRSVAF----SPDGKTLASGSDDGTV 354

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42562156  93 GLWNPissESGEIAHVrdLSKHKGPVRGLEFnvkSPN--QLASGADDGTVCIWDLAN 147
Cdd:COG2319 355 RLWDL---ATGELLRT--LTGHTGAVTSVAF---SPDgrTLASGSADGTVRLWDLAT 403
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 495-716 1.24e-06

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 51.49  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 495 SDPTFDDAIQRSLIVGDYKEAVaQCFSANKM-ADALVIAHVGGTELWESTRDKYIRMSNAPY--MKVVSAMMNN------ 565
Cdd:cd09233  61 AEQKALNRFRNLLLTGNRKEAL-ELALDNGLwAHALLLASSLGKETWAEVVSRFARSESKLNdpLQTLYQLFSGnspeai 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 566 DLMTYLHTRQP---KSWKETLALICTFAEGDE----WISLCDALASNlmaaGFTLAATLCYICAG--------NVDKTVD 630
Cdd:cd09233 140 TELADNPAEAEwalGNWREHLAIILSNRTSNLdleaLVELGDLLAQR----GLVEAAHICYLLAGvplgpypsSPSSCLL 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 631 IWSMSLEKQSAGKSyAECVQdLMEkTLVLALTTCNKRVS-ASLR--KLFesYAEILASQGLIATAMK----FLKLLESGD 703
Cdd:cd09233 216 GGAVHNKSPRTFAT-PEAIQ-LTE-IYEYALSLGNPQFGlPHLQpyKLI--HAARLAELGLVSEALKyceaIASSLKSLT 290

                       250       260
                ....*....|....*....|.
gi 42562156 704 FSP--------ELSILRDRIS 716
Cdd:cd09233 291 KSPyydpnllaQLQDLSERLS 311
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 115-342 4.76e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  115 KGPVRGLEFNVKSPNQLASGADDGTVCIWDLANPSkpshyLKGTGSYMQSEISSLSWNKGFQHVLASTSHNGTTVIWDVN 194
Cdd:PLN00181 532 RSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQ-----LVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSIN 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  195 NEKIITDLKTTVRCSVLQWDPDHFNQILVASdedSSPNVKLLDIRYLQSPVRTFVGHQRGVIAMEWCpsDSLYLLTCGKD 274
Cdd:PLN00181 607 QGVSIGTIKTKANICCVQFPSESGRSLAFGS---ADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFV--DSSTLVSSSTD 681

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42562156  275 NRTICWN-TKTGKIVAELPtgqnwnfdVHWYpkmpgvISASSVDGKIGIYNLEGCSSYGTENQQHFLFH 342
Cdd:PLN00181 682 NTLKLWDlSMSISGINETP--------LHSF------MGHTNVKNFVGLSVSDGYIATGSETNEVFVYH 736
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 719-867 1.61e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.93  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   719 AEPEAANTSASTNTQ------PKISNPYQEKSFTPAP---LSNAQPSRSItFFP-----LNPPRELKNADQYQQPTMDYH 784
Cdd:PRK10263  695 AEAELARQFAQTQQQrysgeqPAGANPFSLDDFEFSPmkaLLDDGPHEPL-FTPivepvQQPQQPVAPQQQYQQPQQPVA 773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   785 SFNRSAGPAYNAPPGPgSYRSIHSQVGPYINSKIPQtvappvRPMTPTHQVAVQPEPVAPPPTVQTADTSNVPAHQKPIV 864
Cdd:PRK10263  774 PQPQYQQPQQPVAPQP-QYQQPQQPVAPQPQYQQPQ------QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLL 846


                  ...
gi 42562156   865 ASL 867
Cdd:PRK10263  847 HPL 849
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 108-144 2.38e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 42.30  E-value: 2.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 42562156    108 VRDLSKHKGPVRGLEFNvKSPNQLASGADDGTVCIWD 144
Cdd:smart00320   5 LKTLKGHTGPVTSVAFS-PDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 41-251 6.55e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.00  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   41 LEIFELDFQSND-RELKL-VGQCQSSERFNRLAWGSYGSGSdglIAGGLVDGNIGLWNPISSESgeiahVRDLSKHKGPV 118
Cdd:PLN00181 507 IKIFECESIIKDgRDIHYpVVELASRSKLSGICWNSYIKSQ---VASSNFEGVVQVWDVARSQL-----VTEMKEHEKRV 578

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  119 RGLEFNVKSPNQLASGADDGTVCIWDLaNPSKPSHYLKgtgsyMQSEISSLSWNKGFQHVLASTSHNGTTVIWDVNNEKI 198
Cdd:PLN00181 579 WSIDYSSADPTLLASGSDDGSVKLWSI-NQGVSIGTIK-----TKANICCVQFPSESGRSLAFGSADHKVYYYDLRNPKL 652

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42562156  199 -----ITDLKTTVRCSVLQwdpdhfNQILVASDEDSSpnVKLLDIRYL-----QSPVRTFVGH 251
Cdd:PLN00181 653 plctmIGHSKTVSYVRFVD------SSTLVSSSTDNT--LKLWDLSMSisginETPLHSFMGH 707
WD40 pfam00400
WD domain, G-beta repeat;
108-144 1.16e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 42562156   108 VRDLSKHKGPVRGLEFNvKSPNQLASGADDGTVCIWD 144
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFS-PDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 243-281 2.81e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.22  E-value: 2.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 42562156    243 SPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWN 281
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
243-281 2.82e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 2.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 42562156   243 SPVRTFVGHQRGVIAMEWCPsDSLYLLTCGKDNRTICWN 281
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
RMtype1_S_Aco12261I-TRD1-CR1_like cd17498
Type I restriction-modification system specificity (S) subunit Target Recognition ...
 328-409 5.56e-03

Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to Aminobacterium colombiense DSM 12261 S subunit (S.Aco12261I) TRD1-CR1; The S.Aco12261I S subunit recognizes 5'... GCANNNNNNTGT ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. This subfamily may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases. S.Aco12261I TRD2-CR2 does not belong to this subfamily.


Pssm-ID: 341189 [Multi-domain]  Cd Length: 173  Bit Score: 38.82  E-value: 5.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156 328 CSSYGTENQQHFLFHLLDADpltAPKWWKRPAGASFGfggkliSFNKNLPEASEVFLHSLATEKSLVNRISKFEAALENG 407
Cdd:cd17498  84 CSIRMKNGNNSFLYYLLKNN---IKNLINKSSGTVFG------SINKDDIENLEVDIPEDEEQKRIANILSKIDDKIEIN 154


                ..
gi 42562156 408 EK 409
Cdd:cd17498 155 NQ 156
PTZ00421 PTZ00421
coronin; Provisional
 89-247 6.66e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156   89 DGNIGLWNpISSE---SGEIAHVRDLSKHKGPVRGLEFNVKSPNQLASGADDGTVCIWDLaNPSKPSHYLKGTGSYmqse 165
Cdd:PTZ00421  97 DGTIMGWG-IPEEgltQNISDPIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDV-ERGKAVEVIKCHSDQ---- 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562156  166 ISSLSWN-KGfqHVLASTSHNGTTVIWDVNNEKIITDLKT-----TVRCSvlqWDPDHFNQILVASDEDSSPNVKLLDIR 239
Cdd:PTZ00421 171 ITSLEWNlDG--SLLCTTSKDKKLNIIDPRDGTIVSSVEAhasakSQRCL---WAKRKDLIITLGCSKSQQRQIMLWDTR 245


                 ....*...
gi 42562156  240 YLQSPVRT 247
Cdd:PTZ00421 246 KMASPYST 253
 
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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