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Conserved domains on  [gi|1958774273|ref|XP_017448598|]
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astrotactin-2 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASTN_1_2_N super family cl44858
Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) ...
162-707 0e+00

Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) proteins 1 and 2, which includes the transmembrane and cytosolic regions. These are vertebrate-specific proteins involved in neuronal migration during neurodevelopment. ASTN1 is a neuronal receptor required for neuroblasts migration along glial fibers, especially in the cerebellum. ASTN2 is an endosome membrane protein that binds ASTN1 and mediates its recycling by promoting ASTN1 internalization and transport during its endocytosis.


The actual alignment was detected with superfamily member pfam19441:

Pssm-ID: 437273  Cd Length: 555  Bit Score: 625.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  162 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQLHILHISVMGGLIALLLLLLVFTVAL 241
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  242 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSTRLQAHNSVIGVPIRETPILDDYDYEEEEDpprrA 319
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  320 NHVSRE-----DEFDSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 394
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  395 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 472
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  473 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETG------ 546
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  547 --ECSCHEGYAPDPVHRHLCIRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 624
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  625 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 704
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 1958774273  705 DGS 707
Cdd:pfam19441  553 DGT 555
ASTN1_2_EGF_Fn super family cl45145
ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane ...
979-1133 8.22e-107

ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane proteins with a large C-terminal domain, extracellular for ASTN1 and endosome luminal for ASTN-2. They play critical roles in neurodevelopment, and ASTN-2 is also involved in the planar cell polarity pathway in hair cells. This is a domain found in the middle of the C-terminal of ASTN-1 and 2, which comprises a EGF- like domain (EGF4) and a fibronectin type III (Fn(III)) domain. These subdomains are located between the MACPF and annexin- like domains. The structure of Fn(III) from ASTN2 revealed an unexpected feature which has two additional beta strands folded across the core. The junction between EGF-4 and Fn(III) domains in ASTN2 (but not in ASTN1) is thought to be an inositol triphosphate binding site.


The actual alignment was detected with superfamily member pfam19743:

Pssm-ID: 437575  Cd Length: 216  Bit Score: 333.81  E-value: 8.22e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  979 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1058
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774273 1059 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWIDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 1133
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 155
MACPF smart00457
membrane-attack complex / perforin;
867-1050 1.79e-43

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 156.82  E-value: 1.79e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   867 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 946
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   947 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1016
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1958774273  1017 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1050
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
718-765 2.27e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.31  E-value: 2.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774273  718 CSDGfNGGCEQLCLqqtmplpydATSSTifMFCGCVEEYKLAPDGKSC 765
Cdd:pfam14670    1 CSVN-NGGCSHLCL---------NTPGG--YTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
ASTN_1_2_N pfam19441
Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) ...
162-707 0e+00

Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) proteins 1 and 2, which includes the transmembrane and cytosolic regions. These are vertebrate-specific proteins involved in neuronal migration during neurodevelopment. ASTN1 is a neuronal receptor required for neuroblasts migration along glial fibers, especially in the cerebellum. ASTN2 is an endosome membrane protein that binds ASTN1 and mediates its recycling by promoting ASTN1 internalization and transport during its endocytosis.


Pssm-ID: 437273  Cd Length: 555  Bit Score: 625.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  162 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQLHILHISVMGGLIALLLLLLVFTVAL 241
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  242 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSTRLQAHNSVIGVPIRETPILDDYDYEEEEDpprrA 319
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  320 NHVSRE-----DEFDSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 394
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  395 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 472
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  473 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETG------ 546
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  547 --ECSCHEGYAPDPVHRHLCIRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 624
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  625 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 704
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 1958774273  705 DGS 707
Cdd:pfam19441  553 DGT 555
ASTN1_2_EGF_Fn pfam19743
ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane ...
979-1133 8.22e-107

ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane proteins with a large C-terminal domain, extracellular for ASTN1 and endosome luminal for ASTN-2. They play critical roles in neurodevelopment, and ASTN-2 is also involved in the planar cell polarity pathway in hair cells. This is a domain found in the middle of the C-terminal of ASTN-1 and 2, which comprises a EGF- like domain (EGF4) and a fibronectin type III (Fn(III)) domain. These subdomains are located between the MACPF and annexin- like domains. The structure of Fn(III) from ASTN2 revealed an unexpected feature which has two additional beta strands folded across the core. The junction between EGF-4 and Fn(III) domains in ASTN2 (but not in ASTN1) is thought to be an inositol triphosphate binding site.


Pssm-ID: 437575  Cd Length: 216  Bit Score: 333.81  E-value: 8.22e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  979 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1058
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774273 1059 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWIDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 1133
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 155
MACPF smart00457
membrane-attack complex / perforin;
867-1050 1.79e-43

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 156.82  E-value: 1.79e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   867 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 946
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   947 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1016
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1958774273  1017 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1050
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
718-765 2.27e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.31  E-value: 2.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774273  718 CSDGfNGGCEQLCLqqtmplpydATSSTifMFCGCVEEYKLAPDGKSC 765
Cdd:pfam14670    1 CSVN-NGGCSHLCL---------NTPGG--YTCSCPEGYELQDDGRTC 36
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
878-1045 1.14e-04

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 44.70  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  878 LYRVKLST---ITLSAGFTNVLK---ILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQqlwLQYQKE 951
Cdd:pfam01823   32 LYQFTLKRsnkLQLSDEFLQALSdlpDNYDYAAKATYIQFFDKYGTHYITSVTLGGKIVYVLKLDKSQLED---LKLKGE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  952 TTELGSKKELKSmpFITYLSG-------LLTAQMLSDDQLISgvEIRCEEKG-RCPSTchlcRRPGKE--------QLSP 1015
Cdd:pfam01823  109 DVKICLSASAGA--SIGSVNLkgcsknsSSTKEKKSFNQEIE--SSITLVIGgTPESI----DDDSKTysdwaesvKDNP 180
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958774273 1016 TPVLLEInrvVPLYTLIQDNGTK-EAFKNAL 1045
Cdd:pfam01823  181 MPIDFEL---TPISELLKGVPLKkENLRKAL 208
 
Name Accession Description Interval E-value
ASTN_1_2_N pfam19441
Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) ...
162-707 0e+00

Astrotactin 1/2 N-terminal; This entry represents the N-terminal domain of Astrotactin (ASTN) proteins 1 and 2, which includes the transmembrane and cytosolic regions. These are vertebrate-specific proteins involved in neuronal migration during neurodevelopment. ASTN1 is a neuronal receptor required for neuroblasts migration along glial fibers, especially in the cerebellum. ASTN2 is an endosome membrane protein that binds ASTN1 and mediates its recycling by promoting ASTN1 internalization and transport during its endocytosis.


Pssm-ID: 437273  Cd Length: 555  Bit Score: 625.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  162 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQLHILHISVMGGLIALLLLLLVFTVAL 241
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  242 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSTRLQAHNSVIGVPIRETPILDDYDYEEEEDpprrA 319
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  320 NHVSRE-----DEFDSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 394
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  395 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 472
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  473 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETG------ 546
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  547 --ECSCHEGYAPDPVHRHLCIRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 624
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  625 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 704
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 1958774273  705 DGS 707
Cdd:pfam19441  553 DGT 555
ASTN1_2_EGF_Fn pfam19743
ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane ...
979-1133 8.22e-107

ASTN1/2 EGF-like and Fn(III) domains; Astrotactin-1 and 2 (ASTN1/2) are integral membrane proteins with a large C-terminal domain, extracellular for ASTN1 and endosome luminal for ASTN-2. They play critical roles in neurodevelopment, and ASTN-2 is also involved in the planar cell polarity pathway in hair cells. This is a domain found in the middle of the C-terminal of ASTN-1 and 2, which comprises a EGF- like domain (EGF4) and a fibronectin type III (Fn(III)) domain. These subdomains are located between the MACPF and annexin- like domains. The structure of Fn(III) from ASTN2 revealed an unexpected feature which has two additional beta strands folded across the core. The junction between EGF-4 and Fn(III) domains in ASTN2 (but not in ASTN1) is thought to be an inositol triphosphate binding site.


Pssm-ID: 437575  Cd Length: 216  Bit Score: 333.81  E-value: 8.22e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  979 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1058
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774273 1059 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWIDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 1133
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYT 155
MACPF smart00457
membrane-attack complex / perforin;
867-1050 1.79e-43

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 156.82  E-value: 1.79e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   867 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 946
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273   947 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1016
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1958774273  1017 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1050
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
718-765 2.27e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.31  E-value: 2.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774273  718 CSDGfNGGCEQLCLqqtmplpydATSSTifMFCGCVEEYKLAPDGKSC 765
Cdd:pfam14670    1 CSVN-NGGCSHLCL---------NTPGG--YTCSCPEGYELQDDGRTC 36
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
878-1045 1.14e-04

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 44.70  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  878 LYRVKLST---ITLSAGFTNVLK---ILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQqlwLQYQKE 951
Cdd:pfam01823   32 LYQFTLKRsnkLQLSDEFLQALSdlpDNYDYAAKATYIQFFDKYGTHYITSVTLGGKIVYVLKLDKSQLED---LKLKGE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774273  952 TTELGSKKELKSmpFITYLSG-------LLTAQMLSDDQLISgvEIRCEEKG-RCPSTchlcRRPGKE--------QLSP 1015
Cdd:pfam01823  109 DVKICLSASAGA--SIGSVNLkgcsknsSSTKEKKSFNQEIE--SSITLVIGgTPESI----DDDSKTysdwaesvKDNP 180
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958774273 1016 TPVLLEInrvVPLYTLIQDNGTK-EAFKNAL 1045
Cdd:pfam01823  181 MPIDFEL---TPISELLKGVPLKkENLRKAL 208
 
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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