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Conserved domains on  [gi|1831513055|ref|NP_001368408|]
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UNC-44 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 167-271 9.54e-48

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.22  E-value: 9.54e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055   167 PSFLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVI 246
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1831513055   247 LEVPHFASLRDREREIVILRSDDGQ 271
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 498-633 4.40e-47

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


The actual alignment was detected with superfamily member pfam17809:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 164.18  E-value: 4.40e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  498 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 577
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513055  578 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 633
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 664-741 1.28e-26

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260029  Cd Length: 84  Bit Score: 104.27  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  664 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 740
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82


                   .
gi 1831513055  741 I 741
Cdd:cd08317     83 C 83
 
Name Accession Description Interval E-value
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 167-271 9.54e-48

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.22  E-value: 9.54e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055   167 PSFLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVI 246
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1831513055   247 LEVPHFASLRDREREIVILRSDDGQ 271
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 498-633 4.40e-47

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 164.18  E-value: 4.40e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  498 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 577
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513055  578 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 633
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 172-268 2.21e-41

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 146.90  E-value: 2.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  172 SFLVDARGGAMRGCrHSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILEVPH 251
Cdd:pfam00791    2 SGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80

                           90
                   ....*....|....*..
gi 1831513055  252 FASLRDREREIVILRSD 268
Cdd:pfam00791   81 CASLRPEEWEIVLKRSD 97
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 664-741 1.28e-26

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 104.27  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  664 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 740
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82


                   .
gi 1831513055  741 I 741
Cdd:cd08317     83 C 83
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 662-743 2.76e-16

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 74.75  E-value: 2.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055   662 DLPEFVHQNVLKG-IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 737
Cdd:smart00005    2 ELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDA 81


                    ....*.
gi 1831513055   738 VRSIAY 743
Cdd:smart00005   82 VELLRS 87
Death pfam00531
Death domain;
660-743 5.76e-16

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 73.94  E-value: 5.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  660 EKDLPEFVhqNVLKGIGADWPRLGRALEVPHRDIQHIRQNYP--GQECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 737
Cdd:pfam00531    1 RKQLDRLL--DPPPPLGKDWRELARKLGLSENEIDEIESENPrlRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                   ....*.
gi 1831513055  738 VRSIAY 743
Cdd:pfam00531   79 AEKIQS 84
 
Name Accession Description Interval E-value
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 167-271 9.54e-48

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.22  E-value: 9.54e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055   167 PSFLISFLVDARGGAMRGCRhSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVI 246
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 1831513055   247 LEVPHFASLRDREREIVILRSDDGQ 271
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 498-633 4.40e-47

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 164.18  E-value: 4.40e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  498 IPYMAKFAVFARRTFPVEGQLRVFCMTDDKEDKTLEKQEHFKLIAKSRDVEVLKGKHQFLEFSGNLVPITKSGDQLSLFF 577
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831513055  578 LPFQENRLAFMVKTRsndDNEAATEGRIGFMAEPKIRSDAlpPQQPICTLAISLPE 633
Cdd:pfam17809   81 KAFRENRLDGSVRVK---DPSDPPKGLLSFMRDAKVDGGT--VSQPLCTLNIVLPQ 131
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 172-268 2.21e-41

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 146.90  E-value: 2.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  172 SFLVDARGGAMRGCrHSGVRIIVPPRKASQPIRVTCRYLRKDKLAHPPPLSEGEELASRILEMAPAGAKFLGPVILEVPH 251
Cdd:pfam00791    2 SGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80

                           90
                   ....*....|....*..
gi 1831513055  252 FASLRDREREIVILRSD 268
Cdd:pfam00791   81 CASLRPEEWEIVLKRSD 97
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 664-741 1.28e-26

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 104.27  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  664 PEFVHQNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRS 740
Cdd:cd08317      3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNslaQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIVEK 82


                   .
gi 1831513055  741 I 741
Cdd:cd08317     83 C 83
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 662-743 2.76e-16

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 74.75  E-value: 2.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055   662 DLPEFVHQNVLKG-IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 737
Cdd:smart00005    2 ELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDA 81


                    ....*.
gi 1831513055   738 VRSIAY 743
Cdd:smart00005   82 VELLRS 87
Death pfam00531
Death domain;
660-743 5.76e-16

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 73.94  E-value: 5.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513055  660 EKDLPEFVhqNVLKGIGADWPRLGRALEVPHRDIQHIRQNYP--GQECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDI 737
Cdd:pfam00531    1 RKQLDRLL--DPPPPLGKDWRELARKLGLSENEIDEIESENPrlRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                   ....*.
gi 1831513055  738 VRSIAY 743
Cdd:pfam00531   79 AEKIQS 84
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 673-741 2.14e-13

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 66.15  E-value: 2.14e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513055  673 KGIGADWPRLGRALEVPHRDIQHIRQNYPGQE---CKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIVRSI 741
Cdd:cd01670      7 EELGRDWKKLARKLGLSEGDIDQIEEDNRDDLkeqAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKL 78
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 665-730 2.39e-07

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 49.22  E-value: 2.39e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831513055  665 EFVHQNVlkgiGADWPRLGRALEVPHRDIQHIRQNYP------GQECkntLKIWIHLKKEDANQDNLDQALR 730
Cdd:cd08306      6 DVICENL----GRDWRQLARKLGLSETKIESISEAHPrnlreqVRQS---LREWKKIKKAEATVADLIKALR 70
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 669-742 2.81e-06

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 46.15  E-value: 2.81e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831513055  669 QNVLKGIGADWPRLGRALEVPHRDIQHIRQNYPG--QECK-NTLKIWIHLKKEDAN-QDNLDQALRQIGRDDIVRSIA 742
Cdd:cd08779      6 LSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDdlDEQIlDMLFSWAKTLPTSPDkVGLLVTALSKSGRSDLAEELR 83
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 675-738 2.06e-03

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260067  Cd Length: 84  Bit Score: 38.03  E-value: 2.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513055  675 IGADWPRLGRALEVPHRDIQHIRQNYPG---QECKNTLKIWIHLKKEDANQDNLDQALRQIGRDDIV 738
Cdd:cd08805     14 LGLSWAELARELQFSVEDINRIRVENPNsllEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 676-741 2.48e-03

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260025  Cd Length: 80  Bit Score: 37.65  E-value: 2.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513055  676 GADWPRLGRALEVPHRDIQHI-RQNYPgqeCKNTLKIWIHlkKEDANQDNLDQALRQIGRDDIVRSI 741
Cdd:cd08311     18 GSDWRALAGELGYSAEEIDSFaREADP---CRALLTDWSA--QDGATLGVLLTALRKIGRDDIVEIL 79
 
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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