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Conserved domains on  [gi|1887789622|ref|NP_001373095|]
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ankyrin-2 isoform 65 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 124-253 2.00e-57

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: 195.38  E-value: 2.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  124 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 203
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789622  204 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 253
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 2367-2450 7.37e-50

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) 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-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066  Cd Length: 84  Bit Score: 171.81  E-value: 7.37e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08804     81 HLME 84
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 478-757 7.91e-10

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.81  E-value: 7.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  478 EGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQkeeglQASAEKAELKKGSSEESLGEDPGLA------------- 544
Cdd:PHA03307   112 SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPP-----AASPPAAGASPAAVASDAASSRQAAlplsspeetarap 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  545 PEPLPTVKATSPLIEETPIGSIKDKVKAL-----------QKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSL 613
Cdd:PHA03307   187 SSPPAEPPPSTPPAAASPRPPRRSSPISAsasspapapgrSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  614 KSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSS--KTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHS 691
Cdd:PHA03307   267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSpgSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789622  692 PVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKT 757
Cdd:PHA03307   347 PSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
1949-2195 2.99e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14949:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 944  Bit Score: 49.72  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 1949 EGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQ---MGISASTETPTKEAVSVGTKDL 2025
Cdd:PRK14949   412 TEQTTAQQQVQAANAEAVAEADASAEPADTVEQALDDESELLAALNAEQAVILSQaqsQGFEASSSLDADNSAVPEQIDS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2026 PTVQTgDIPPLSGVKQI--------SCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDS----------SPEEQKSVIEI 2087
Cdd:PRK14949   492 TAEQS-VVNPSVTDTQVddtsasnnSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLdayqddyvafSSESYNALSDD 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2088 PTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEyESSVSEDFLSSV-----------DEENKADEAKPKSKLPVK--VPL 2154
Cdd:PRK14949   571 EQHSANVQSAQSAAEAQPSSQSLSPISAVTTAA-ASLADDDILDAVlaardsllsdlDALSPKEGDGKKSSADRKpkTPP 649

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789622 2155 QRVEQQLSDLDTSV----QKTVAPQGQDMASIAPDNRSKSESDAS 2195
Cdd:PRK14949   650 SRAPPASLSKPASSpdasQTSASFDLDPDFELATHQSVPEAALAS 694
PTZ00121 super family cl31754
MAEBL; Provisional
 333-960 5.78e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  333 KVKELVKAAEEEPGEPFEIVERVKEDLEKVN--EILRSGTCTR--DESSVQSSRSERGLVEEEWVIVSDE--EIEEARQK 406
Cdd:PTZ00121  1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRkfEEARMAHFARRQAAIKAEEARKADElkKAEEKKKA 1292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  407 APLEITEypcvEVRIDKEIKGKVEKDSTGlvnyltddlntcvplpkEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDE 486
Cdd:PTZ00121  1293 DEAKKAE----EKKKADEAKKKAEEAKKA-----------------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  487 TQSTQKQHKPSLGIKKPVRRKLKEKQKQKeeglQASAEKAELKKGSSE-ESLGEDPGLAPEPLPTVKATSPLIEETpigs 565
Cdd:PTZ00121  1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEA---- 1423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  566 ikdKVKALQKRVEDEQKGRSKlpirVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPV 645
Cdd:PTZ00121  1424 ---KKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  646 SPSSKTEKHSPVSPSA----KTERHSPASSSSKTEKHSPVSPSTKTERhspvsSTKTERHPPVSPSGKTDKRPPVSPSGR 721
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAEE-----KKKADELKKAEELKKAEEKKKAEEAKK 1571

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  722 TEKHPPVSPGRTEkrlpVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQppvspTSKTERIEETMSVRELMKAFQSGQ 801
Cdd:PTZ00121  1572 AEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----KIKAEELKKAEEEKKKVEQLKKKE 1642

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  802 DPSKHKTGLF--EHKSAKQKQPQEKGKVRVEKEKGpiltqREAQKTENQTIKRGQRLPvtGTAESKRGV----RVSSIGV 875
Cdd:PTZ00121  1643 AEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALK--KEAEEAKKAeelkKKEAEEK 1715

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  876 KKEDAAGGKEKVLSHKIPEPVQSVPEE----ESHRESEVPKEKMADEQGDMDLQISPDRKTStdfSEVIKQELEDNDKYQ 951
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDEEDEKR 1792


                   ....*....
gi 1887789622  952 QFRLSEETE 960
Cdd:PTZ00121  1793 RMEVDKKIK 1801
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 124-253 2.00e-57

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: 195.38  E-value: 2.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  124 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 203
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789622  204 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 253
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 2367-2450 7.37e-50

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) 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-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066  Cd Length: 84  Bit Score: 171.81  E-value: 7.37e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08804     81 HLME 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 2366-2451 2.76e-24

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: 99.02  E-value: 2.76e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  2366 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 2444
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1887789622  2445 IVHLMET 2451
Cdd:smart00005   81 AVELLRS 87
Death pfam00531
Death domain;
2370-2450 3.81e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 3.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2370 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1887789622 2447 HLME 2450
Cdd:pfam00531   80 EKIQ 83
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 478-757 7.91e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.81  E-value: 7.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  478 EGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQkeeglQASAEKAELKKGSSEESLGEDPGLA------------- 544
Cdd:PHA03307   112 SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPP-----AASPPAAGASPAAVASDAASSRQAAlplsspeetarap 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  545 PEPLPTVKATSPLIEETPIGSIKDKVKAL-----------QKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSL 613
Cdd:PHA03307   187 SSPPAEPPPSTPPAAASPRPPRRSSPISAsasspapapgrSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  614 KSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSS--KTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHS 691
Cdd:PHA03307   267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSpgSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789622  692 PVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKT 757
Cdd:PHA03307   347 PSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 1949-2195 2.99e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 49.72  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 1949 EGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQ---MGISASTETPTKEAVSVGTKDL 2025
Cdd:PRK14949   412 TEQTTAQQQVQAANAEAVAEADASAEPADTVEQALDDESELLAALNAEQAVILSQaqsQGFEASSSLDADNSAVPEQIDS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2026 PTVQTgDIPPLSGVKQI--------SCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDS----------SPEEQKSVIEI 2087
Cdd:PRK14949   492 TAEQS-VVNPSVTDTQVddtsasnnSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLdayqddyvafSSESYNALSDD 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2088 PTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEyESSVSEDFLSSV-----------DEENKADEAKPKSKLPVK--VPL 2154
Cdd:PRK14949   571 EQHSANVQSAQSAAEAQPSSQSLSPISAVTTAA-ASLADDDILDAVlaardsllsdlDALSPKEGDGKKSSADRKpkTPP 649

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789622 2155 QRVEQQLSDLDTSV----QKTVAPQGQDMASIAPDNRSKSESDAS 2195
Cdd:PRK14949   650 SRAPPASLSKPASSpdasQTSASFDLDPDFELATHQSVPEAALAS 694
PTZ00121 PTZ00121
MAEBL; Provisional
 333-960 5.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  333 KVKELVKAAEEEPGEPFEIVERVKEDLEKVN--EILRSGTCTR--DESSVQSSRSERGLVEEEWVIVSDE--EIEEARQK 406
Cdd:PTZ00121  1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRkfEEARMAHFARRQAAIKAEEARKADElkKAEEKKKA 1292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  407 APLEITEypcvEVRIDKEIKGKVEKDSTGlvnyltddlntcvplpkEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDE 486
Cdd:PTZ00121  1293 DEAKKAE----EKKKADEAKKKAEEAKKA-----------------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  487 TQSTQKQHKPSLGIKKPVRRKLKEKQKQKeeglQASAEKAELKKGSSE-ESLGEDPGLAPEPLPTVKATSPLIEETpigs 565
Cdd:PTZ00121  1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEA---- 1423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  566 ikdKVKALQKRVEDEQKGRSKlpirVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPV 645
Cdd:PTZ00121  1424 ---KKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  646 SPSSKTEKHSPVSPSA----KTERHSPASSSSKTEKHSPVSPSTKTERhspvsSTKTERHPPVSPSGKTDKRPPVSPSGR 721
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAEE-----KKKADELKKAEELKKAEEKKKAEEAKK 1571

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  722 TEKHPPVSPGRTEkrlpVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQppvspTSKTERIEETMSVRELMKAFQSGQ 801
Cdd:PTZ00121  1572 AEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----KIKAEELKKAEEEKKKVEQLKKKE 1642

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  802 DPSKHKTGLF--EHKSAKQKQPQEKGKVRVEKEKGpiltqREAQKTENQTIKRGQRLPvtGTAESKRGV----RVSSIGV 875
Cdd:PTZ00121  1643 AEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALK--KEAEEAKKAeelkKKEAEEK 1715

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  876 KKEDAAGGKEKVLSHKIPEPVQSVPEE----ESHRESEVPKEKMADEQGDMDLQISPDRKTStdfSEVIKQELEDNDKYQ 951
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDEEDEKR 1792


                   ....*....
gi 1887789622  952 QFRLSEETE 960
Cdd:PTZ00121  1793 RMEVDKKIK 1801
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
608-737 8.87e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.19  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  608 AASPSLKSERHA-PGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTeKHSPVSPSTK 686
Cdd:pfam05539  214 SSTEPVGTQGTTtSSNPEPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRS-PHSTATPPPT 292

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622  687 TERHS-------PVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRL 737
Cdd:pfam05539  293 TKRQEtgrptprPTATTQSGSSPPHSSPPGVQANPTTQNLVDCKELDPPKPNSICYGV 350
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 124-253 2.00e-57

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: 195.38  E-value: 2.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  124 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 203
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1887789622  204 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 253
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 2367-2450 7.37e-50

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) 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-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066  Cd Length: 84  Bit Score: 171.81  E-value: 7.37e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08804     81 HLME 84
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 2367-2450 1.26e-36

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: 133.93  E-value: 1.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08317     81 EKCE 84
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 2367-2450 3.07e-27

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) 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-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. 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: 176781  Cd Length: 84  Bit Score: 107.07  E-value: 3.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08803     81 TLLE 84
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 2367-2450 1.19e-26

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: 105.44  E-value: 1.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2367 ERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 1887789622 2447 HLME 2450
Cdd:cd08805     81 NILE 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 2366-2451 2.76e-24

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: 99.02  E-value: 2.76e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  2366 QERIEERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMD 2444
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*..
gi 1887789622  2445 IVHLMET 2451
Cdd:smart00005   81 AVELLRS 87
Death pfam00531
Death domain;
2370-2450 3.81e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 3.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2370 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIV 2446
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1887789622 2447 HLME 2450
Cdd:pfam00531   80 EKIQ 83
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 2373-2450 8.60e-19

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: 82.71  E-value: 8.60e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622 2373 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLME 2450
Cdd:cd01670      2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 478-757 7.91e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.81  E-value: 7.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  478 EGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQkeeglQASAEKAELKKGSSEESLGEDPGLA------------- 544
Cdd:PHA03307   112 SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPP-----AASPPAAGASPAAVASDAASSRQAAlplsspeetarap 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  545 PEPLPTVKATSPLIEETPIGSIKDKVKAL-----------QKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSL 613
Cdd:PHA03307   187 SSPPAEPPPSTPPAAASPRPPRRSSPISAsasspapapgrSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  614 KSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSS--KTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHS 691
Cdd:PHA03307   267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSpgSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887789622  692 PVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKT 757
Cdd:PHA03307   347 PSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
PHA03247 PHA03247
large tegument protein UL36; Provisional
 598-778 1.56e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.72  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  598 PKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPpvSPSSKTEKHSPVSP--SAKTERHSPASSSSKT 675
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP--SPWDPADPPAAVLApaAALPPAASPAGPLPPP 2831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  676 EKHSPVSPSTKTERHSPVSSTKTErhppVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAG 755
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGS----VAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPER 2907

                          170       180
                   ....*....|....*....|...
gi 1887789622  756 KTEKHLPVSPSGKTEKQPPVSPT 778
Cdd:PHA03247  2908 PPQPQAPPPPQPQPQPPPPPQPQ 2930
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 2376-2446 2.20e-08

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: 53.45  E-value: 2.20e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789622 2376 IADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKInRMDIV 2446
Cdd:cd08306      8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDC-QLNLV 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
 541-904 6.27e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 6.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  541 PGLAPEPLPTVKATSPLIEETPIGSIKDKVKALQKRvEDEQKGRSKLPIRV--KGKEDVPKKTTHRPHPAASP----SLK 614
Cdd:PHA03247  2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRArrLGRAAQASSPPQRPRRRAARptvgSLT 2696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  615 SERHAPGSPSPKTERHSTLSSSAKTERHP-------------PVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPV 681
Cdd:PHA03247  2697 SLADPPPPPPTPEPAPHALVSATPLPPGPaaarqaspalpaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  682 SPSTKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKH-----PPVSPGRTEkrLPVSPSGRTDKHQPVSTAGK 756
Cdd:PHA03247  2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaaspaGPLPPPTSA--QPTAPPPPPGPPPPSLPLGG 2854

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  757 TekhlpVSPSGKTEKQPPVSPTSKTERIEETMSVRELmkafqSGQDPSKHKTGLFEHKSAKQKQPQEKGKVRVEKEKGPI 836
Cdd:PHA03247  2855 S-----VAPGGDVRRRPPSRSPAAKPAAPARPPVRRL-----ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887789622  837 LTQREAQKTENQTIKRGQRLPVTGTA---ESKRGVRVSSIGVkkedAAGGKEKVLSHKIPEPVQSVPEEES 904
Cdd:PHA03247  2925 PPPQPQPPPPPPPRPQPPLAPTTDPAgagEPSGAVPQPWLGA----LVPGRVAVPRFRVPQPAPSREAPAS 2991
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 2370-2441 1.68e-07

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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: 260031  Cd Length: 83  Bit Score: 50.79  E-value: 1.68e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887789622 2370 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKIN 2441
Cdd:cd08319      2 DRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 2362-2450 2.22e-07

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: 50.36  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2362 PQDEQERIEERLAyiADHLGFSWTELARELDFTEEQIHQIrienpNSLQDQSHALLKYWLERDGkhATDTNLVECLTKIN 2441
Cdd:cd08311      1 PPHKQEEVEKLLN--AGREGSDWRALAGELGYSAEEIDSF-----AREADPCRALLTDWSAQDG--ATLGVLLTALRKIG 71


                   ....*....
gi 1887789622 2442 RMDIVHLME 2450
Cdd:cd08311     72 RDDIVEILQ 80
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 566-779 2.53e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 56.62  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  566 IKDKVKALQKRV-----EDEQK--------GRSKLPIRVKG------KEDVPKKTTHRPHPAASPSLKSERHAPGSPSPK 626
Cdd:PTZ00449   485 IKKLIKKSKKKLapieeEDSDKhdeppegpEASGLPPKAPGdkegeeGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPA 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  627 TER-------HSTLSSSAKTERHPPvSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHSPVSSTKte 699
Cdd:PTZ00449   565 KEHkpskiptLSKKPEFPKDPKHPK-DPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQR-- 641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  700 rhpPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEK----------RLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKT 769
Cdd:PTZ00449   642 ---PSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKfyddyldaaaKSKETKTTVVLDESFESILKETLPETPGTPFTTP 718

                          250
                   ....*....|
gi 1887789622  770 EKQPPVSPTS 779
Cdd:PTZ00449   719 RPLPPKLPRD 728
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 554-819 4.77e-07

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 55.32  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  554 TSPLieeTPIGSIKDKVKAlqKRVEdeqkgrSKLPIRVKGKEDVPKKtthrPHPAASPSLKSERhapGSPSPKTERHSTL 633
Cdd:PLN03209   310 TAPL---TPMEELLAKIPS--QRVP------PKESDAADGPKPVPTK----PVTPEAPSPPIEE---EPPQPKAVVPRPL 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  634 SS-SAKTERHPPVSPSsktekhsPVSPSAKTERHSPASSSSK--TEKHSPVSPSTKTERHSPVSSTKTERHPPVSPSGK- 709
Cdd:PLN03209   372 SPyTAYEDLKPPTSPI-------PTPPSSSPASSKSVDAVAKpaEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARy 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  710 TDKRPPVSPSgRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSP-SGKTEKQPPVSPT-SKTERIEET 787
Cdd:PLN03209   445 EDLKPPTSPS-PTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPyAVYDDLKPPTSPSpAAPVGKVAP 523

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1887789622  788 MSVRELMKAFQSGQDPSKHKTGlfEHKSAKQK 819
Cdd:PLN03209   524 SSTNEVVKVGNSAPPTALADEQ--HHAQPKPR 553
PHA03247 PHA03247
large tegument protein UL36; Provisional
 528-806 8.73e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 8.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  528 LKKGSSEESLGEDPGLAPEPLPTVKATS---PLIEETPIGSikdKVKALQKRVE-DEQKGRSKLPIrvkGKEDVPkktth 603
Cdd:PHA03247  2540 LEELASDDAGDPPPPLPPAAPPAAPDRSvppPRPAPRPSEP---AVTSRARRPDaPPQSARPRAPV---DDRGDP----- 2608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  604 rPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTekhsPVSP 683
Cdd:PHA03247  2609 -RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP----PQRP 2683

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  684 STKTERHSPVSSTKTERHPPvsPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPV 763
Cdd:PHA03247  2684 RRRAARPTVGSLTSLADPPP--PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPP 2761

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1887789622  764 SPSGKTEKQPPVSPTSKTER---IEETMSVRELMKAFQSGQDPSKH 806
Cdd:PHA03247  2762 TTAGPPAPAPPAAPAAGPPRrltRPAVASLSESRESLPSPWDPADP 2807
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 531-783 1.34e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  531 GSSEESLGEDPGLAPEPLPTVKATSPliEETPIGSIKDKVKALQKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHpAAS 610
Cdd:PHA03307    98 ASPAREGSPTPPGPSSPDPPPPTPPP--ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ-AAL 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  611 PSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKT---ERHSPASSSSKTE-KHSPVSPSTK 686
Cdd:PHA03307   175 PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSaadDAGASSSDSSSSEsSGCGWGPENE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  687 TERHSPVSSTKTER-----HPPVSPSGKTDKRPPVSPSGRtekHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGkTEKHL 761
Cdd:PHA03307   255 CPLPRPAPITLPTRiweasGWNGPSSRPGPASSSSSPRER---SPSPSPSSPGSGPAPSSPRASSSSSSSRESS-SSSTS 330

                          250       260
                   ....*....|....*....|..
gi 1887789622  762 PVSPSgktEKQPPVSPTSKTER 783
Cdd:PHA03307   331 SSSES---SRGAAVSPGPSPSR 349
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 470-807 4.59e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 4.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  470 AVGRSSEKEGKDIPPDETQSTQKQHKPslgikkpvrrklkekqkqkeeglqasaekaelkKGSSEESLGEDPGLAPEPLP 549
Cdd:PTZ00449   523 APGDKEGEEGEHEDSKESDEPKEGGKP---------------------------------GETKEGEVGKKPGPAKEHKP 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  550 tvkatsplieetpigsikdkvkalqkrvedeqkgrSKLPIRVKgKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTER 629
Cdd:PTZ00449   570 -----------------------------------SKIPTLSK-KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPK 613

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  630 HSTLSSSAKTERHP--PVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTK-------TERHSPVSSTKTER 700
Cdd:PTZ00449   614 LPELLDIPKSPKRPesPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKekfyddyLDAAAKSKETKTTV 693

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  701 HPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGR-TEKRLPVSPSGRTDKHQPVSTAGKTEkhlPVSPSGKTEKQPPVSPTS 779
Cdd:PTZ00449   694 VLDESFESILKETLPETPGTPFTTPRPLPPKLpRDEEFPFEPIGDPDAEQPDDIEFFTP---PEEERTFFHETPADTPLP 770

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1887789622  780 -------KTERI-EETMSVRELMKAFQSgqdPSKHK 807
Cdd:PTZ00449   771 dilaeefKEEDIhAETGEPDEAMKRPDS---PSEHE 803
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 2361-2445 6.98e-06

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. 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: 260030  Cd Length: 86  Bit Score: 46.36  E-value: 6.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2361 DPQDEQERIEErlayIADHLGFSWTELARELDFTEEQIHQIRiENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKI 2440
Cdd:cd08318      2 DKPVTSEQIDV----LANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAA 76


                   ....*
gi 1887789622 2441 NRMDI 2445
Cdd:cd08318     77 GLNEI 81
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 2375-2441 8.17e-06

Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. 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: 260027  Cd Length: 88  Bit Score: 46.49  E-value: 8.17e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622 2375 YIADHLGF-SWTELARELDFTEEQIHQIRIENPNSlQDQSHALLKYWLERDGKHATDTNLVECLTKIN 2441
Cdd:cd08315      4 YFEDIVPFkSWKRLMRALGLSDNEIKLAEANDPGS-QEPLYQMLNKWLNKTGRKASVNTLLDALEDLG 70
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 2383-2450 8.66e-06

Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. 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: 260054  Cd Length: 80  Bit Score: 46.03  E-value: 8.66e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622 2383 SWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLtkiNRMDIVHLME 2450
Cdd:cd08784     13 QWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDL---KKMNLCTLAE 77
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 605-743 2.47e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  605 PHPAASPSLKSERHAPGSPSPKTERH-STLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSP 683
Cdd:PHA03307   294 RSPSPSPSSPGSGPAPSSPRASSSSSsSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSR 373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789622  684 STKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRL----PVSPSG 743
Cdd:PHA03307   374 APSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYarypLLTPSG 437
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 1949-2195 2.99e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 49.72  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 1949 EGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQ---MGISASTETPTKEAVSVGTKDL 2025
Cdd:PRK14949   412 TEQTTAQQQVQAANAEAVAEADASAEPADTVEQALDDESELLAALNAEQAVILSQaqsQGFEASSSLDADNSAVPEQIDS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2026 PTVQTgDIPPLSGVKQI--------SCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDS----------SPEEQKSVIEI 2087
Cdd:PRK14949   492 TAEQS-VVNPSVTDTQVddtsasnnSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLdayqddyvafSSESYNALSDD 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2088 PTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEyESSVSEDFLSSV-----------DEENKADEAKPKSKLPVK--VPL 2154
Cdd:PRK14949   571 EQHSANVQSAQSAAEAQPSSQSLSPISAVTTAA-ASLADDDILDAVlaardsllsdlDALSPKEGDGKKSSADRKpkTPP 649

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1887789622 2155 QRVEQQLSDLDTSV----QKTVAPQGQDMASIAPDNRSKSESDAS 2195
Cdd:PRK14949   650 SRAPPASLSKPASSpdasQTSASFDLDPDFELATHQSVPEAALAS 694
PHA03381 PHA03381
tegument protein VP22; Provisional
 624-780 1.21e-04

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 46.54  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  624 SPKTERHSTLSSSAKTeRHPPVSPSSKTEKHSPVSPSAKTER-HSPASSSSKTEKHS-PVSPSTKTERHSPVSSTKTERH 701
Cdd:PHA03381     6 SPRPKPHGTDEVEADV-YYDFISPDASPARVSFEEPADRARRgAGQARGRSQAERRFhHYDEARADYPYYTGSSSEDERP 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887789622  702 PPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQPPVSPTSK 780
Cdd:PHA03381    85 ADPRPSRRPHAQPEASGPGPARGARGPAGSRGRGRRAESPSPRDPPNPKGASAPRGRKSACADSAALLDAPAPAAPKRQ 163
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 576-777 1.33e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  576 RVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHS 655
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGS 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  656 PVSPSAKTERHSPASSSSKTEKH----SPVSPSTKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHP---PV 728
Cdd:PHA03307   144 PGPPPAASPPAAGASPAAVASDAassrQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASspaPA 223

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1887789622  729 SPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQPPVSP 777
Cdd:PHA03307   224 PGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 614-799 2.41e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.61  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  614 KSERHAPGSPSPKTERHSTLSSSAKTERHPPVSP---SSKTEKHSPVSPSAKTERHSPASSSSKTE---------KHSPV 681
Cdd:PTZ00449   491 KSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPgdkEGEEGEHEDSKESDEPKEGGKPGETKEGEvgkkpgpakEHKPS 570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  682 SPSTKTERHSPVSSTKTERHP--------PVSPSGKTDKRPPVSP-SGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVS 752
Cdd:PTZ00449   571 KIPTLSKKPEFPKDPKHPKDPeepkkpkrPRSAQRPTRPKSPKLPeLLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG 650

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789622  753 TAGKTEKHLPVSPsgktekQPPVSPT----------SKTERIEETMSVRELMKAFQS 799
Cdd:PTZ00449   651 PKIIKSPKPPKSP------KPPFDPKfkekfyddylDAAAKSKETKTTVVLDESFES 701
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 2370-2449 1.07e-03

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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: 260048  Cd Length: 86  Bit Score: 40.11  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622 2370 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIE-NPNSLQDQSHALLKYWLERDG-KHATDTNLVECLTKINRMDIVH 2447
Cdd:cd08777      2 EKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDyERDGLKEKVHQMLEKWKMKEGsKGATVGKLAKALEGCIKSDLLV 81


                   ..
gi 1887789622 2448 LM 2449
Cdd:cd08777     82 SL 83
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 2373-2446 1.11e-03

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: 40.38  E-value: 1.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622 2373 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLErdgKHATDTN----LVECLTKINRMDIV 2446
Cdd:cd08779      5 LLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAK---TLPTSPDkvglLVTALSKSGRSDLA 79
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 607-779 1.60e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  607 PAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTK 686
Cdd:PHA03307    71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAA 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  687 TERHSPVSSTKTERHPPVSPSGKtdkrpPVSPSGRTEKHPPVSPGRTEKRLPvSPSGRTDKHQPVSTAGKTEKHLPVSPS 766
Cdd:PHA03307   151 SPPAAGASPAAVASDAASSRQAA-----LPLSSPEETARAPSSPPAEPPPST-PPAAASPRPPRRSSPISASASSPAPAP 224

                          170
                   ....*....|...
gi 1887789622  767 GKTEKQPPVSPTS 779
Cdd:PHA03307   225 GRSAADDAGASSS 237
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 585-742 1.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  585 SKLPIRVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTE--RHPPVSPSSKTEKHSPVSPSAK 662
Cdd:PHA03307   762 SLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASkrKSRSHTPDGGSESSGPARPPGA 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  663 TERHSPASSSSKTEKHS---PVSPSTKTERHSPVSSTKTeRHPPVSPSGKTDKRPPVSPsgrtekhPPVSPGRTEKRLPV 739
Cdd:PHA03307   842 AARPPPARSSESSKSKPaaaGGRARGKNGRRRPRPPEPR-ARPGAAAPPKAAAAAPPAG-------APAPRPRPAPRVKL 913


                   ...
gi 1887789622  740 SPS 742
Cdd:PHA03307   914 GPM 916
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 2384-2447 2.32e-03

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 39.12  E-value: 2.32e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887789622 2384 WTELARELDFTEEQIHQIRIENpnslqDQSHALLKYWLERDgKHATDTNLVECLTKINRMDIVH 2447
Cdd:cd08312     19 WRGLAELMGFDYLEIRNFERQS-----SPTERLLEDWETRP-PGATVGNLLEILEELERKDVLE 76
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 604-781 4.22e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  604 RPHPAASPSLKSERHAPGSPSPKTErhstlSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSP-----ASSSSKTEKH 678
Cdd:PHA03307    85 RSTPTWSLSTLAPASPAREGSPTPP-----GPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPgpppaASPPAAGASP 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  679 SPVSPSTKTERHS--PVSSTKTERHPPVSPSGktdKRPPVSPSGRTEKHPPV--SPGRTEKRLPVSPSGRTDKHQPVSTA 754
Cdd:PHA03307   160 AAVASDAASSRQAalPLSSPEETARAPSSPPA---EPPPSTPPAAASPRPPRrsSPISASASSPAPAPGRSAADDAGASS 236

                          170       180
                   ....*....|....*....|....*...
gi 1887789622  755 -GKTEKHLPVSPSGKTEKQPPVSPTSKT 781
Cdd:PHA03307   237 sDSSSSESSGCGWGPENECPLPRPAPIT 264
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 2384-2450 4.54e-03

Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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: 176729  Cd Length: 80  Bit Score: 38.14  E-value: 4.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887789622 2384 WTELARELDFTEEQIHQIRIENpNSLQDQSHALLKYWLERDGKHATDTNLVECltKINRMDIVHLME 2450
Cdd:cd08313     14 WKEFVRRLGLSDNEIERVELDH-RRCRDAQYQMLKVWKERGPRPYATLQHLLS--VLRDMELVGCAE 77
PTZ00121 PTZ00121
MAEBL; Provisional
 333-960 5.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  333 KVKELVKAAEEEPGEPFEIVERVKEDLEKVN--EILRSGTCTR--DESSVQSSRSERGLVEEEWVIVSDE--EIEEARQK 406
Cdd:PTZ00121  1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRkfEEARMAHFARRQAAIKAEEARKADElkKAEEKKKA 1292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  407 APLEITEypcvEVRIDKEIKGKVEKDSTGlvnyltddlntcvplpkEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDE 486
Cdd:PTZ00121  1293 DEAKKAE----EKKKADEAKKKAEEAKKA-----------------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  487 TQSTQKQHKPSLGIKKPVRRKLKEKQKQKeeglQASAEKAELKKGSSE-ESLGEDPGLAPEPLPTVKATSPLIEETpigs 565
Cdd:PTZ00121  1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEA---- 1423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  566 ikdKVKALQKRVEDEQKGRSKlpirVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPV 645
Cdd:PTZ00121  1424 ---KKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  646 SPSSKTEKHSPVSPSA----KTERHSPASSSSKTEKHSPVSPSTKTERhspvsSTKTERHPPVSPSGKTDKRPPVSPSGR 721
Cdd:PTZ00121  1497 KKADEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAEE-----KKKADELKKAEELKKAEEKKKAEEAKK 1571

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  722 TEKHPPVSPGRTEkrlpVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQppvspTSKTERIEETMSVRELMKAFQSGQ 801
Cdd:PTZ00121  1572 AEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----KIKAEELKKAEEEKKKVEQLKKKE 1642

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  802 DPSKHKTGLF--EHKSAKQKQPQEKGKVRVEKEKGpiltqREAQKTENQTIKRGQRLPvtGTAESKRGV----RVSSIGV 875
Cdd:PTZ00121  1643 AEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALK--KEAEEAKKAeelkKKEAEEK 1715

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  876 KKEDAAGGKEKVLSHKIPEPVQSVPEE----ESHRESEVPKEKMADEQGDMDLQISPDRKTStdfSEVIKQELEDNDKYQ 951
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDEEDEKR 1792


                   ....*....
gi 1887789622  952 QFRLSEETE 960
Cdd:PTZ00121  1793 RMEVDKKIK 1801
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
608-737 8.87e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.19  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887789622  608 AASPSLKSERHA-PGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTeKHSPVSPSTK 686
Cdd:pfam05539  214 SSTEPVGTQGTTtSSNPEPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRS-PHSTATPPPT 292

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1887789622  687 TERHS-------PVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRL 737
Cdd:pfam05539  293 TKRQEtgrptprPTATTQSGSSPPHSSPPGVQANPTTQNLVDCKELDPPKPNSICYGV 350
 
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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