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Conserved domains on  [gi|124301217|ref|NP_112151|]
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VPS10 domain-containing receptor SorCS2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VPS10 smart00602
VPS10 domain;
170-776 0e+00

VPS10 domain;


:

Pssm-ID: 214740 [Multi-domain]  Cd Length: 612  Bit Score: 756.55  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    170 HADMGKVLESSLWRSSDFGTTYTKLTL--QPGVTTVIDNFYICPANKRKIILvssslgdREQSLFLSTDEGATFQKYPVP 247
Cdd:smart00602    1 SLLLGSAEESSVYISEDYGKTWKKIDEieGVIIETVISDFFNSSANKFKTIL-------VKGYIFISSDEGKSFQKFTLP 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    248 FL-VEMLLFHPKEEDKVLAYTKDS---KLYVSSDLGKKWTLLQERVTKDHVFWAVSGVDDDPNLVHVEAQDLSGgyrYYT 323
Cdd:smart00602   74 FPpLPSLLYHPKHPDYVLAYSKDCnykVLYVSKDFGKTWTEIQENVESCEFSWGSMGVYDFPDLVHISVKENSG---ALT 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    324 CLIYNCSAQPHIAPFSGPIDRGSLTVQDEYIFLKATST--NRTKYYVSYRRSDFVLMKLPKY-ALPK--DLQIISTDEQQ 398
Cdd:smart00602  151 ELVSSIDFFQRYDQSTIFLDIVGFLLTDEYLFVAVTDEdtTSRKLYVSNDRSTFAMAKFPKYhALGKqqAYTILDSDEDS 230
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    399 VFVAVQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEenvvIDILEVRGVKGVFLANQK--VDGKVTTVITYNKGRD 476
Cdd:smart00602  231 VFLHVSENNQNDTGNLYISDSRGTKFSLSLENVNRYTGGY----IDFYKVEGLKGIYIANIVskVDKQLQTKITFDKGGD 306
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    477 WDYLRPPSTDMNGKPTNCQPPD---CYLHLHLRWADNPYvSGTVHTKDTAPGLIMGAGNLGSQLVEYKEE-MYITSDCGH 552
Cdd:smart00602  307 WSLLKPPDVDNEGKKFNCDLTSlekCSLHLHLRYSESPY-SGDIASSKSAPGIIIASGNVGDGLASYWEPsTFISSDGGL 385
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    553 TWRQVFEEEHHVLYLDHGGVIAAIKDTSiPLKILKFSVDEGHTWSTHNFTSTSVFVDGLLSEPGDETLVMTVFGHISFR- 631
Cdd:smart00602  386 TWRLVFDGPHLYAYGDHGGIIVAIEYNS-PTNELKYSTDEGKTWKTYTFTSTPVFVKGLLTEPGGSTLVFTLFGFTKERg 464
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    632 SDWELVKVDFRPSFPRQCGEDDYSSWDLTDLQG--DHCIMGQQRSYRKRKSTSWCVKGRSFTS-ALTSRVCKCRDSDFLC 708
Cdd:smart00602  465 SSWSLYTIDFKDIFERQCEEDDYKTWNLDDKRGsrDGCLLGHKTIFKRRKPTSQCLVGKSDYDlSLVSSPCSCTREDFEC 544
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124301217    709 DYGFERSSSSESTankCSA--NFWFNPLspPEDCVLGQTYTS---SLGYRKVVSNVCEGGVDLQQSPVQLQCP 776
Cdd:smart00602  545 DFGFYRLSEGDST---CVPdpNLSGNPL--SDDCKKGKSYTEyvkSLGYRKIPGDKCKGGVKLEAEDIPHPCP 612
PKD_4 super family cl40917
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
809-869 1.45e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


The actual alignment was detected with superfamily member pfam18911:

Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 44.57  E-value: 1.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124301217   809 GDVLTTKYQVDLGDGfkamyvnLTLTGEPIRHHYESPGIYRVSVRAENMAGHDEAVLFVQV 869
Cdd:pfam18911   30 PDGDILSYRWDFGDG-------TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
1-130 1.02e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    1 MAHRGPPSAPKRPGPTAPDRSFQALLPPcwPRSWPLLLLLLVLVAACGAMGRSPQPGrqgPGVQITRLlPAGRTESGDRK 80
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPASPP--PSPAPDLSEMLRPVGSPGPPPAASPPA---AGASPAAV-ASDAASSRQAA 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 124301217   81 DPQARESEPSVPGLGPGSASGPSTDGAPAPGKGRRaRAVPVAGAASASRA 130
Cdd:PHA03307  174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR-RSSPISASASSPAP 222
 
Name Accession Description Interval E-value
VPS10 smart00602
VPS10 domain;
170-776 0e+00

VPS10 domain;


Pssm-ID: 214740 [Multi-domain]  Cd Length: 612  Bit Score: 756.55  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    170 HADMGKVLESSLWRSSDFGTTYTKLTL--QPGVTTVIDNFYICPANKRKIILvssslgdREQSLFLSTDEGATFQKYPVP 247
Cdd:smart00602    1 SLLLGSAEESSVYISEDYGKTWKKIDEieGVIIETVISDFFNSSANKFKTIL-------VKGYIFISSDEGKSFQKFTLP 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    248 FL-VEMLLFHPKEEDKVLAYTKDS---KLYVSSDLGKKWTLLQERVTKDHVFWAVSGVDDDPNLVHVEAQDLSGgyrYYT 323
Cdd:smart00602   74 FPpLPSLLYHPKHPDYVLAYSKDCnykVLYVSKDFGKTWTEIQENVESCEFSWGSMGVYDFPDLVHISVKENSG---ALT 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    324 CLIYNCSAQPHIAPFSGPIDRGSLTVQDEYIFLKATST--NRTKYYVSYRRSDFVLMKLPKY-ALPK--DLQIISTDEQQ 398
Cdd:smart00602  151 ELVSSIDFFQRYDQSTIFLDIVGFLLTDEYLFVAVTDEdtTSRKLYVSNDRSTFAMAKFPKYhALGKqqAYTILDSDEDS 230
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    399 VFVAVQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEenvvIDILEVRGVKGVFLANQK--VDGKVTTVITYNKGRD 476
Cdd:smart00602  231 VFLHVSENNQNDTGNLYISDSRGTKFSLSLENVNRYTGGY----IDFYKVEGLKGIYIANIVskVDKQLQTKITFDKGGD 306
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    477 WDYLRPPSTDMNGKPTNCQPPD---CYLHLHLRWADNPYvSGTVHTKDTAPGLIMGAGNLGSQLVEYKEE-MYITSDCGH 552
Cdd:smart00602  307 WSLLKPPDVDNEGKKFNCDLTSlekCSLHLHLRYSESPY-SGDIASSKSAPGIIIASGNVGDGLASYWEPsTFISSDGGL 385
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    553 TWRQVFEEEHHVLYLDHGGVIAAIKDTSiPLKILKFSVDEGHTWSTHNFTSTSVFVDGLLSEPGDETLVMTVFGHISFR- 631
Cdd:smart00602  386 TWRLVFDGPHLYAYGDHGGIIVAIEYNS-PTNELKYSTDEGKTWKTYTFTSTPVFVKGLLTEPGGSTLVFTLFGFTKERg 464
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    632 SDWELVKVDFRPSFPRQCGEDDYSSWDLTDLQG--DHCIMGQQRSYRKRKSTSWCVKGRSFTS-ALTSRVCKCRDSDFLC 708
Cdd:smart00602  465 SSWSLYTIDFKDIFERQCEEDDYKTWNLDDKRGsrDGCLLGHKTIFKRRKPTSQCLVGKSDYDlSLVSSPCSCTREDFEC 544
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124301217    709 DYGFERSSSSESTankCSA--NFWFNPLspPEDCVLGQTYTS---SLGYRKVVSNVCEGGVDLQQSPVQLQCP 776
Cdd:smart00602  545 DFGFYRLSEGDST---CVPdpNLSGNPL--SDDCKKGKSYTEyvkSLGYRKIPGDKCKGGVKLEAEDIPHPCP 612
Sortilin-Vps10 pfam15902
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
179-611 1.84e-136

Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.


Pssm-ID: 464929 [Multi-domain]  Cd Length: 444  Bit Score: 421.22  E-value: 1.84e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   179 SSLWRSSDFGTTYTKLTLQPGVTtVIDNFYICPANKRKIILVSSSlgdreQSLFLSTDEGATFQKYPVPFLVEM----LL 254
Cdd:pfam15902    1 SEVYRSHDYGKTWKKVKDVPDGE-AILAIYPHPYDNDRAYLLTDG-----KKHYYTTDRGKTFRSFKLPFPPNLfgppLS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   255 FHPKEEDKVLAYTK-------DSKLYVSSDLGKKWTLLQERVTKdhVFWAVSGVDDDPNLVHVEAQDLSGGYRYYTCLIY 327
Cdd:pfam15902   75 FHPKDPDWLIWYGGkcfsgdcHSVAYYSTDGGKSWKLLLEYVRR--CEWAVSSKADENLIFCEVYENESGNADDVKLRLV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   328 NCS---AQPHIAPFSGPIDrgsLTVQDEYIFLKATSTNRT--KYYVSYRRSDFVLMKLPKYALPKDLQIISTDEQQVFVA 402
Cdd:pfam15902  153 SSDdffKSDKVLFDDGVVG---FAVVGEFIVVAVKSENTSelALYVSYDGKTFARAQFPHVLEQQAYTVLESSTHSIFLH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   403 VQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEenvvIDILEVRGVKGVFLANQ---------KVDGKVTTVITYNK 473
Cdd:pfam15902  230 VTTSSDNPYGSLYKSNSNGTYFVLSLENVNRNERGY----VDFEKVAGLEGVYLANVvsnaeevgkGADKKLKTKITFND 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   474 GRDWDYLRPPSTDMNGKPTNCQPPDCYLHLHLRWADNPYVSGTVHTKDTAPGLIMGAGNLGSQLVEYKE-EMYITSDCGH 552
Cdd:pfam15902  306 GGTWQPLKPPDKDSEYKCSGKGLEKCSLHLHGYTERLVNIGRDTFSSPSAPGLIMGVGNVGDSLGPYEDaDTFISRDGGI 385
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124301217   553 TWRQVFEEEHHVLYLDHGGVIAAIKDTSIPLKILKFSVDEGHTWSTHNFTSTSVFVDGL 611
Cdd:pfam15902  386 TWKEVLKGPHKWEFGDQGSIIVAVKDEGDPTDEISYSLDEGKTWETYKFADEKIRVLDL 444
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
809-869 1.45e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 44.57  E-value: 1.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124301217   809 GDVLTTKYQVDLGDGfkamyvnLTLTGEPIRHHYESPGIYRVSVRAENMAGHDEAVLFVQV 869
Cdd:pfam18911   30 PDGDILSYRWDFGDG-------TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1-130 1.02e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    1 MAHRGPPSAPKRPGPTAPDRSFQALLPPcwPRSWPLLLLLLVLVAACGAMGRSPQPGrqgPGVQITRLlPAGRTESGDRK 80
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPASPP--PSPAPDLSEMLRPVGSPGPPPAASPPA---AGASPAAV-ASDAASSRQAA 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 124301217   81 DPQARESEPSVPGLGPGSASGPSTDGAPAPGKGRRaRAVPVAGAASASRA 130
Cdd:PHA03307  174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR-RSSPISASASSPAP 222
GH32_Inu-like cd18622
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This ...
229-287 2.70e-03

glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350134  Cd Length: 289  Bit Score: 41.06  E-value: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124301217  229 QSLFLSTDEGATFQKY---PVPFLVEMLLFH-PK----EEDK----VLAYTKDSKLYVSSDLgKKWTLLQE 287
Cdd:cd18622   100 QSLAYSTDGGRTFTKYegnPVLPNPGSTDFRdPKvfwhEPSGkwvmVLAEGDKIGFYTSPDL-KNWTYLSE 169
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
814-869 4.46e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 37.05  E-value: 4.46e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 124301217    814 TKYQVDLGDGFKAMYVNLTLTgepirhhYESPGIYRVSVRAENMAGHDEAVLFVQV 869
Cdd:smart00089   30 VSYTWDFGDGTSSTGPTVTHT-------YTKPGTYTVTLTVTNAVGSASATVTVVV 78
 
Name Accession Description Interval E-value
VPS10 smart00602
VPS10 domain;
170-776 0e+00

VPS10 domain;


Pssm-ID: 214740 [Multi-domain]  Cd Length: 612  Bit Score: 756.55  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    170 HADMGKVLESSLWRSSDFGTTYTKLTL--QPGVTTVIDNFYICPANKRKIILvssslgdREQSLFLSTDEGATFQKYPVP 247
Cdd:smart00602    1 SLLLGSAEESSVYISEDYGKTWKKIDEieGVIIETVISDFFNSSANKFKTIL-------VKGYIFISSDEGKSFQKFTLP 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    248 FL-VEMLLFHPKEEDKVLAYTKDS---KLYVSSDLGKKWTLLQERVTKDHVFWAVSGVDDDPNLVHVEAQDLSGgyrYYT 323
Cdd:smart00602   74 FPpLPSLLYHPKHPDYVLAYSKDCnykVLYVSKDFGKTWTEIQENVESCEFSWGSMGVYDFPDLVHISVKENSG---ALT 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    324 CLIYNCSAQPHIAPFSGPIDRGSLTVQDEYIFLKATST--NRTKYYVSYRRSDFVLMKLPKY-ALPK--DLQIISTDEQQ 398
Cdd:smart00602  151 ELVSSIDFFQRYDQSTIFLDIVGFLLTDEYLFVAVTDEdtTSRKLYVSNDRSTFAMAKFPKYhALGKqqAYTILDSDEDS 230
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    399 VFVAVQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEenvvIDILEVRGVKGVFLANQK--VDGKVTTVITYNKGRD 476
Cdd:smart00602  231 VFLHVSENNQNDTGNLYISDSRGTKFSLSLENVNRYTGGY----IDFYKVEGLKGIYIANIVskVDKQLQTKITFDKGGD 306
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    477 WDYLRPPSTDMNGKPTNCQPPD---CYLHLHLRWADNPYvSGTVHTKDTAPGLIMGAGNLGSQLVEYKEE-MYITSDCGH 552
Cdd:smart00602  307 WSLLKPPDVDNEGKKFNCDLTSlekCSLHLHLRYSESPY-SGDIASSKSAPGIIIASGNVGDGLASYWEPsTFISSDGGL 385
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    553 TWRQVFEEEHHVLYLDHGGVIAAIKDTSiPLKILKFSVDEGHTWSTHNFTSTSVFVDGLLSEPGDETLVMTVFGHISFR- 631
Cdd:smart00602  386 TWRLVFDGPHLYAYGDHGGIIVAIEYNS-PTNELKYSTDEGKTWKTYTFTSTPVFVKGLLTEPGGSTLVFTLFGFTKERg 464
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    632 SDWELVKVDFRPSFPRQCGEDDYSSWDLTDLQG--DHCIMGQQRSYRKRKSTSWCVKGRSFTS-ALTSRVCKCRDSDFLC 708
Cdd:smart00602  465 SSWSLYTIDFKDIFERQCEEDDYKTWNLDDKRGsrDGCLLGHKTIFKRRKPTSQCLVGKSDYDlSLVSSPCSCTREDFEC 544
                           570       580       590       600       610       620       630
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124301217    709 DYGFERSSSSESTankCSA--NFWFNPLspPEDCVLGQTYTS---SLGYRKVVSNVCEGGVDLQQSPVQLQCP 776
Cdd:smart00602  545 DFGFYRLSEGDST---CVPdpNLSGNPL--SDDCKKGKSYTEyvkSLGYRKIPGDKCKGGVKLEAEDIPHPCP 612
Sortilin-Vps10 pfam15902
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
179-611 1.84e-136

Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.


Pssm-ID: 464929 [Multi-domain]  Cd Length: 444  Bit Score: 421.22  E-value: 1.84e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   179 SSLWRSSDFGTTYTKLTLQPGVTtVIDNFYICPANKRKIILVSSSlgdreQSLFLSTDEGATFQKYPVPFLVEM----LL 254
Cdd:pfam15902    1 SEVYRSHDYGKTWKKVKDVPDGE-AILAIYPHPYDNDRAYLLTDG-----KKHYYTTDRGKTFRSFKLPFPPNLfgppLS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   255 FHPKEEDKVLAYTK-------DSKLYVSSDLGKKWTLLQERVTKdhVFWAVSGVDDDPNLVHVEAQDLSGGYRYYTCLIY 327
Cdd:pfam15902   75 FHPKDPDWLIWYGGkcfsgdcHSVAYYSTDGGKSWKLLLEYVRR--CEWAVSSKADENLIFCEVYENESGNADDVKLRLV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   328 NCS---AQPHIAPFSGPIDrgsLTVQDEYIFLKATSTNRT--KYYVSYRRSDFVLMKLPKYALPKDLQIISTDEQQVFVA 402
Cdd:pfam15902  153 SSDdffKSDKVLFDDGVVG---FAVVGEFIVVAVKSENTSelALYVSYDGKTFARAQFPHVLEQQAYTVLESSTHSIFLH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   403 VQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEenvvIDILEVRGVKGVFLANQ---------KVDGKVTTVITYNK 473
Cdd:pfam15902  230 VTTSSDNPYGSLYKSNSNGTYFVLSLENVNRNERGY----VDFEKVAGLEGVYLANVvsnaeevgkGADKKLKTKITFND 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   474 GRDWDYLRPPSTDMNGKPTNCQPPDCYLHLHLRWADNPYVSGTVHTKDTAPGLIMGAGNLGSQLVEYKE-EMYITSDCGH 552
Cdd:pfam15902  306 GGTWQPLKPPDKDSEYKCSGKGLEKCSLHLHGYTERLVNIGRDTFSSPSAPGLIMGVGNVGDSLGPYEDaDTFISRDGGI 385
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124301217   553 TWRQVFEEEHHVLYLDHGGVIAAIKDTSIPLKILKFSVDEGHTWSTHNFTSTSVFVDGL 611
Cdd:pfam15902  386 TWKEVLKGPHKWEFGDQGSIIVAVKDEGDPTDEISYSLDEGKTWETYKFADEKIRVLDL 444
Sortilin_C pfam15901
Sortilin, neurotensin receptor 3, C-terminal; Sortilin_C is the C-terminal cytoplasmic tail of ...
613-775 2.12e-58

Sortilin, neurotensin receptor 3, C-terminal; Sortilin_C is the C-terminal cytoplasmic tail of sortilin, a Vps10p domain-containing family of proteins. Most sortilin is expressed within intracellular compartments, where it chaperones diverse ligands, including proBDNF and acid hydrolases. The sortilin cytoplasmic tail is homologous to mannose 6-phosphate receptor and is required for the intracellular trafficking of cargo proteins via interactions with distinct adaptor molecules. In addition to mediating lysosomal targeting of specific acid hydrolases, the sortilin cytoplasmic tail also directs trafficking of BDNF to the secretory pathway in neurons, where it can be released in response to depolarization to modulate cell survival and synaptic plasticity.


Pssm-ID: 464928 [Multi-domain]  Cd Length: 164  Bit Score: 198.31  E-value: 2.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   613 SEPGDETLVMTVFGHI-SFRSDWELV-KVDFRPSFPRQCGEDDYSSWDLT-DLQGDHCIMGQQRSYRKRKSTSWCVKGRS 689
Cdd:pfam15901    1 TEPDDTSLKFLLFGSSsSSRSDWEVVyTIDFSGLFDRKCTDDDYELWSPRhDQDGPKCLLGHKQKYRRRKPDADCFNGKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217   690 FTSALTSRVCKCRDSDFLCDYGFERSSSSestaNKCSANFWFNPLSPP-EDCVLGQTYTSSLGYRKVVSNVCEGGVDLQQ 768
Cdd:pfam15901   81 FKDPKIEENCECTREDFECDYGFERSAND----GKCVLVPGLLPPDGPkEDCKPGTYYLGSSGYRKIPGNTCEGGLELDK 156

                   ....*...
gi 124301217   769 -SPVQLQC 775
Cdd:pfam15901  157 dEPVEHPC 164
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
809-869 1.45e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 44.57  E-value: 1.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124301217   809 GDVLTTKYQVDLGDGfkamyvnLTLTGEPIRHHYESPGIYRVSVRAENMAGHDEAVLFVQV 869
Cdd:pfam18911   30 PDGDILSYRWDFGDG-------TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
798-863 3.09e-05

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 43.14  E-value: 3.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124301217   798 EDVLFVVRQEQGDVLTtkYQVDLGDGfkamyVNLTLTGEPIRHHYESPGIYRVSVRAENMAGHDEA 863
Cdd:pfam00801   12 QPVTFTATLADGSNVT--YTWDFGDS-----PGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1-130 1.02e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124301217    1 MAHRGPPSAPKRPGPTAPDRSFQALLPPcwPRSWPLLLLLLVLVAACGAMGRSPQPGrqgPGVQITRLlPAGRTESGDRK 80
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPASPP--PSPAPDLSEMLRPVGSPGPPPAASPPA---AGASPAAV-ASDAASSRQAA 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 124301217   81 DPQARESEPSVPGLGPGSASGPSTDGAPAPGKGRRaRAVPVAGAASASRA 130
Cdd:PHA03307  174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR-RSSPISASASSPAP 222
GH32_Inu-like cd18622
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This ...
229-287 2.70e-03

glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350134  Cd Length: 289  Bit Score: 41.06  E-value: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124301217  229 QSLFLSTDEGATFQKY---PVPFLVEMLLFH-PK----EEDK----VLAYTKDSKLYVSSDLgKKWTLLQE 287
Cdd:cd18622   100 QSLAYSTDGGRTFTKYegnPVLPNPGSTDFRdPKvfwhEPSGkwvmVLAEGDKIGFYTSPDL-KNWTYLSE 169
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
814-869 4.46e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 37.05  E-value: 4.46e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 124301217    814 TKYQVDLGDGFKAMYVNLTLTgepirhhYESPGIYRVSVRAENMAGHDEAVLFVQV 869
Cdd:smart00089   30 VSYTWDFGDGTSSTGPTVTHT-------YTKPGTYTVTLTVTNAVGSASATVTVVV 78
 
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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