NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46488930|ref|NP_996992|]
View 

astrotactin-2 isoform b precursor [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
160-705 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: 622.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    160 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVAL 239
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    240 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDYEEEEEpprrA 317
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    318 NHVSRE-----DEFGSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 392
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    393 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 470
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    471 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPDTG------ 544
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    545 --ECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 622
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    623 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 702
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 46488930    703 DGS 705
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 ...
977-1192 1.89e-149

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: 450.53  E-value: 1.89e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    977 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1056
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1057 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 1136
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 46488930   1137 FADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 1192
Cdd:pfam19743  161 FADDLLSGLGTSCVAAGRSHGDVPESSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 216
Annexin_like pfam18411
Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an ...
1203-1295 6.59e-60

Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. The annexin-like domain is closest in fold to repeat three of human annexin V and similarly binds calcium, yet shares no sequence homology with it. Notably, this ASTN-2 annexin-like domain is closer in structure to human annexin repeat 3 than human annexin repeat 3 is to repeat 1. Annexin-like domains are known for their capacity to remodel membranes, triggered by calcium binding, and have also been suggested to be involved in the formation of pores in membranes both are possible biological roles of the ASTN-2 annexin-like domain.


:

Pssm-ID: 465756  Cd Length: 93  Bit Score: 200.09  E-value: 6.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1203 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQTAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 1282
Cdd:pfam18411    1 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMELGAPMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 80
                           90
                   ....*....|...
gi 46488930   1283 LERVSSHCSSLLR 1295
Cdd:pfam18411   81 LEKVSSHCSSLLR 93
MACPF smart00457
membrane-attack complex / perforin;
865-1048 8.30e-43

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 154.90  E-value: 8.30e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     865 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 944
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     945 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1014
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 46488930    1015 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1048
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
ASTN_2_hairpin pfam18577
Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the ...
1299-1345 5.28e-26

Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the C-terminal region of astrotactin 2 proteins (ASTN-2). ASTN-2 is an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. it consists of multiple polypeptide folds: a perforin-like domain, a minimal epidermal growth factor-like module, a fibronectin type III domain Fn (III) and an annexin-like domain as well as the beta hairpin domain which packs across the fibronectin domain.


:

Pssm-ID: 436591  Cd Length: 47  Bit Score: 101.45  E-value: 5.28e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46488930   1299 IQSRVDTIPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNT 1345
Cdd:pfam18577    1 IQSRTDTVPYLFCRSEEVRPPGMVWHSSLKDTKVTCEEKLMSMPRNT 47
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
716-763 2.28e-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: 2.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 46488930    716 CSDGfNGGCEQLCLqqtlplpyDTTSStifMFCGCVEEYKLAPDGKSC 763
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) ...
160-705 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: 622.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    160 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVAL 239
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    240 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDYEEEEEpprrA 317
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    318 NHVSRE-----DEFGSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 392
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    393 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 470
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    471 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPDTG------ 544
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    545 --ECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 622
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    623 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 702
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 46488930    703 DGS 705
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 ...
977-1192 1.89e-149

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: 450.53  E-value: 1.89e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    977 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1056
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1057 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 1136
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 46488930   1137 FADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 1192
Cdd:pfam19743  161 FADDLLSGLGTSCVAAGRSHGDVPESSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 216
Annexin_like pfam18411
Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an ...
1203-1295 6.59e-60

Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. The annexin-like domain is closest in fold to repeat three of human annexin V and similarly binds calcium, yet shares no sequence homology with it. Notably, this ASTN-2 annexin-like domain is closer in structure to human annexin repeat 3 than human annexin repeat 3 is to repeat 1. Annexin-like domains are known for their capacity to remodel membranes, triggered by calcium binding, and have also been suggested to be involved in the formation of pores in membranes both are possible biological roles of the ASTN-2 annexin-like domain.


Pssm-ID: 465756  Cd Length: 93  Bit Score: 200.09  E-value: 6.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1203 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQTAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 1282
Cdd:pfam18411    1 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMELGAPMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 80
                           90
                   ....*....|...
gi 46488930   1283 LERVSSHCSSLLR 1295
Cdd:pfam18411   81 LEKVSSHCSSLLR 93
MACPF smart00457
membrane-attack complex / perforin;
865-1048 8.30e-43

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 154.90  E-value: 8.30e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     865 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 944
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     945 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1014
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 46488930    1015 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1048
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
ASTN_2_hairpin pfam18577
Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the ...
1299-1345 5.28e-26

Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the C-terminal region of astrotactin 2 proteins (ASTN-2). ASTN-2 is an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. it consists of multiple polypeptide folds: a perforin-like domain, a minimal epidermal growth factor-like module, a fibronectin type III domain Fn (III) and an annexin-like domain as well as the beta hairpin domain which packs across the fibronectin domain.


Pssm-ID: 436591  Cd Length: 47  Bit Score: 101.45  E-value: 5.28e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46488930   1299 IQSRVDTIPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNT 1345
Cdd:pfam18577    1 IQSRTDTVPYLFCRSEEVRPPGMVWHSSLKDTKVTCEEKLMSMPRNT 47
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
716-763 2.28e-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: 2.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 46488930    716 CSDGfNGGCEQLCLqqtlplpyDTTSStifMFCGCVEEYKLAPDGKSC 763
Cdd:pfam14670    1 CSVN-NGGCSHLCL--------NTPGG---YTCSCPEGYELQDDGRTC 36
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
876-1043 1.36e-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: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    876 LYRVKLST---ITLSAGFTNVLK---ILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQqlwLQYQKE 949
Cdd:pfam01823   32 LYQFTLKRsnkLQLSDEFLQALSdlpDNYDYAAKATYIQFFDKYGTHYITSVTLGGKIVYVLKLDKSQLED---LKLKGE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    950 TTELGSKKELKSmpFITYLSG-------LLTAQMLSDDQLISgvEIRCEEKG-RCPSTchlcRRPGKE--------QLSP 1013
Cdd:pfam01823  109 DVKICLSASAGA--SIGSVNLkgcsknsSSTKEKKSFNQEIE--SSITLVIGgTPESI----DDDSKTysdwaesvKDNP 180
                          170       180       190
                   ....*....|....*....|....*....|.
gi 46488930   1014 TPVLLEInrvVPLYTLIQDNGTK-EAFKNAL 1043
Cdd:pfam01823  181 MPIDFEL---TPISELLKGVPLKkENLRKAL 208
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1079-1201 4.63e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.86  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930 1079 PQPVLRLSPTVEPSSTVVsLEWvDVQPAIGTKVSDYILQHKKVDEYTDTDLytgeflsfaddllsglgtscvaagrshgE 1158
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVT-LSW-TPPEDDGGPITGYVVEYREKGSGDWKEV----------------------------E 50
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 46488930 1159 VPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRT 1201
Cdd:cd00063   51 VTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
 
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) ...
160-705 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: 622.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    160 EMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVAL 239
Cdd:pfam19441    1 EISGNTDDIPLVRWRQQWLENGTLLFHIHHQDGAPNLPGFDPTDEPQTESAEEELRILHISVMGGMAAALLSILCLSLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    240 YAQRRWQKRRRI--PQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDYEEEEEpprrA 317
Cdd:pfam19441   81 TPRRKGCKRQRAaePQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDL----R 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    318 NHVSRE-----DEFGSQMTHALDSLgRPGEEKVEFEKKAAAEATQEtveSLMQKFKESFRANTPVEIGQLQPASRSSTSA 392
Cdd:pfam19441  157 HHLQREcmnggEDFASQVTRTLDSL-QGCNEKASMDLTPGSDNAKL---SLMNKYKDNIIATSPVDSNHQQATLLSHTSS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    393 GKRKR-RNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSK-GLLKSPVNKTALTLIAVSSCILAMVCGNQMSC 470
Cdd:pfam19441  233 SQRKQiGGKARAGRAFDNPEGDEGQERARDPLLGFSCDPSRGRGRPGlGSAPSGGNAASLTLISVCFCVISLVCARHAIC 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    471 PLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPDTG------ 544
Cdd:pfam19441  313 PLEIKFSLHLGEHKIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWALDLCARRLLDPCEHQCDPETGkrefel 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    545 --ECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELS 622
Cdd:pfam19441  393 gtEALCGAGRMKDAVDKHLCIRNEWGMNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    623 INPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMK 702
Cdd:pfam19441  473 INPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSRDNGGCSKNFRCISDRKLDSTGCVCPAGLSPMK 552

                   ...
gi 46488930    703 DGS 705
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 ...
977-1192 1.89e-149

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: 450.53  E-value: 1.89e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    977 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVI 1056
Cdd:pfam19743    1 LSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNVTKEAFKSALMSSYWCSGKGDVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1057 DDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 1136
Cdd:pfam19743   81 DDWCRCDLSAFDKDGLPNCSPLPQPVLRLSPYVEPSSTVVSLEWMDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 46488930   1137 FADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 1192
Cdd:pfam19743  161 FADDLLSGLGTSCVAAGRSHGDVPESSIYSVIFKCLEPDGLYKFTLYAVDTRGRHS 216
Annexin_like pfam18411
Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an ...
1203-1295 6.59e-60

Annexin-like domain; This annexin-like domain can be found in astrotactin 2 (Astn-2), an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. The annexin-like domain is closest in fold to repeat three of human annexin V and similarly binds calcium, yet shares no sequence homology with it. Notably, this ASTN-2 annexin-like domain is closer in structure to human annexin repeat 3 than human annexin repeat 3 is to repeat 1. Annexin-like domains are known for their capacity to remodel membranes, triggered by calcium binding, and have also been suggested to be involved in the formation of pores in membranes both are possible biological roles of the ASTN-2 annexin-like domain.


Pssm-ID: 465756  Cd Length: 93  Bit Score: 200.09  E-value: 6.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930   1203 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQTAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 1282
Cdd:pfam18411    1 CPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMELGAPMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRR 80
                           90
                   ....*....|...
gi 46488930   1283 LERVSSHCSSLLR 1295
Cdd:pfam18411   81 LEKVSSHCSSLLR 93
MACPF smart00457
membrane-attack complex / perforin;
865-1048 8.30e-43

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 154.90  E-value: 8.30e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     865 PMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLwL 944
Cdd:smart00457    1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKG-L 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930     945 QYQKETTELG--------SKKELKSMPFITYLSGLLTAQ-MLSDDQLISG-VEIRCEEKgRCPSTCHLCRRPGKEQLSPT 1014
Cdd:smart00457   80 TSEDISKCLAgssnsfagSVSAEHCLQSSSYIKYLSTSLrRESHTQVLGGhVTVLCDLL-RGPSSNSLDFSDWAESVPNE 158
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 46488930    1015 PVLLEInRVVPLYTLIQDN----GTKEAFKNALMSSYW 1048
Cdd:smart00457  159 PVLIDV-SLAPIYELLPPNpelsQKREALRQALRSYLK 195
ASTN_2_hairpin pfam18577
Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the ...
1299-1345 5.28e-26

Astrotactin-2 C-terminal beta-hairpin domain; This is a beta-hairpin domain found at the C-terminal region of astrotactin 2 proteins (ASTN-2). ASTN-2 is an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. it consists of multiple polypeptide folds: a perforin-like domain, a minimal epidermal growth factor-like module, a fibronectin type III domain Fn (III) and an annexin-like domain as well as the beta hairpin domain which packs across the fibronectin domain.


Pssm-ID: 436591  Cd Length: 47  Bit Score: 101.45  E-value: 5.28e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46488930   1299 IQSRVDTIPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNT 1345
Cdd:pfam18577    1 IQSRTDTVPYLFCRSEEVRPPGMVWHSSLKDTKVTCEEKLMSMPRNT 47
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
716-763 2.28e-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: 2.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 46488930    716 CSDGfNGGCEQLCLqqtlplpyDTTSStifMFCGCVEEYKLAPDGKSC 763
Cdd:pfam14670    1 CSVN-NGGCSHLCL--------NTPGG---YTCSCPEGYELQDDGRTC 36
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
876-1043 1.36e-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: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    876 LYRVKLST---ITLSAGFTNVLK---ILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQqlwLQYQKE 949
Cdd:pfam01823   32 LYQFTLKRsnkLQLSDEFLQALSdlpDNYDYAAKATYIQFFDKYGTHYITSVTLGGKIVYVLKLDKSQLED---LKLKGE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930    950 TTELGSKKELKSmpFITYLSG-------LLTAQMLSDDQLISgvEIRCEEKG-RCPSTchlcRRPGKE--------QLSP 1013
Cdd:pfam01823  109 DVKICLSASAGA--SIGSVNLkgcsknsSSTKEKKSFNQEIE--SSITLVIGgTPESI----DDDSKTysdwaesvKDNP 180
                          170       180       190
                   ....*....|....*....|....*....|.
gi 46488930   1014 TPVLLEInrvVPLYTLIQDNGTK-EAFKNAL 1043
Cdd:pfam01823  181 MPIDFEL---TPISELLKGVPLKkENLRKAL 208
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1079-1201 4.63e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.86  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46488930 1079 PQPVLRLSPTVEPSSTVVsLEWvDVQPAIGTKVSDYILQHKKVDEYTDTDLytgeflsfaddllsglgtscvaagrshgE 1158
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVT-LSW-TPPEDDGGPITGYVVEYREKGSGDWKEV----------------------------E 50
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 46488930 1159 VPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRT 1201
Cdd:cd00063   51 VTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH