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Conserved domains on  [gi|630972136|ref|XP_007882476|]
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uncharacterized protein PFL1_06739 [Pseudozyma flocculosa PF-1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 1133-1260 6.80e-33

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


:

Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 123.56  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136 1133 KELDAAFVRDISFPDGSAVAAGSRFDKVWLIRNTGSQPWPKDVGLKLIstcGRSLFDGTRSRLEPIGAdfdgrlVKPGEE 1212
Cdd:cd14947     1 PGLSAAFVEDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFV---GGDPGLLSAPERVPVPS------TVPGEE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 630972136 1213 VEVcCADLRAPDEAGKVQVFWRLATPGRVPsqpdasFGEQLWVAVNVV 1260
Cdd:cd14947    72 VDV-SVELRAPSEPGRYISYWRLVTPDGLP------FGDRLWVDITVE 112
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 735-784 1.89e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


:

Pssm-ID: 239080  Cd Length: 43  Bit Score: 74.22  E-value: 1.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 630972136  735 IRCDGCDGPVFGPRFKCCACPDFDYCRQCEALPTqdHaqrhgPEHLFVKI 784
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGV--H-----PEHAMLKI 43
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 671-715 4.77e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


:

Pssm-ID: 239080  Cd Length: 43  Bit Score: 73.06  E-value: 4.77e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 630972136  671 AICDLCQATIYGVRYKCLDCPDWDCCGAChaETAAKHPDHRFVRI 715
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESC--EAKGVHPEHAMLKI 43
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 230-491 2.84e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 58.05  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   230 SRKPLDASLGAPAQASVKAPKEAPKEAPKEAASSQHGSTAQKQPQVEGKTKTKTSSHASGGATKDTSSTrVPDDKTATTI 309
Cdd:pfam17823  134 IAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPARGI 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   310 ATSFTGGKVASSSPTSQAAPPGSAGQGRAPGSVPLNRFAELLAILNGQNVLPPKEGQKSvqaTNRPLSDLVSEMKaHLQS 389
Cdd:pfam17823  213 STAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN---MGDPHARRLSPAK-HMPS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   390 PGGSFNPAP----------------KPAHTTGSAPLDPLAEMQAALNRLRSSYKKDMAPAQTTTApsvhisKPKEPASSL 453
Cdd:pfam17823  289 DTMARNPAApmgaqaqgpiiqvstdQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKA------QAKEPSASP 362

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 630972136   454 FPLPPLNLKPSLTAAgAPTCASKPLPTFKfGSAAPDQP 491
Cdd:pfam17823  363 VPVLHTSMIPEVEAT-SPTTQPSPLLPTQ-GAAGPGIL 398
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 1133-1260 6.80e-33

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 123.56  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136 1133 KELDAAFVRDISFPDGSAVAAGSRFDKVWLIRNTGSQPWPKDVGLKLIstcGRSLFDGTRSRLEPIGAdfdgrlVKPGEE 1212
Cdd:cd14947     1 PGLSAAFVEDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFV---GGDPGLLSAPERVPVPS------TVPGEE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 630972136 1213 VEVcCADLRAPDEAGKVQVFWRLATPGRVPsqpdasFGEQLWVAVNVV 1260
Cdd:cd14947    72 VDV-SVELRAPSEPGRYISYWRLVTPDGLP------FGDRLWVDITVE 112
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 1144-1259 1.89e-26

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 104.58  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136  1144 SFPDGSAVAAGSRFDKVWLIRNTGSQPWPKDVGLKLIstCGRSLFDGTRSRLEPigadfdgrlVKPGEEVEVcCADLRAP 1223
Cdd:pfam16158    1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFV--GGDNMGNVSTVLVPP---------VAPGEEVDV-SVELKAP 68

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 630972136  1224 DEAGKVQVFWRLATPGRVPsqpdasFGEQLWVAVNV 1259
Cdd:pfam16158   69 SRPGRYISYWRLKTPDGTP------FGDRLWVDITV 98
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 735-784 1.89e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 74.22  E-value: 1.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 630972136  735 IRCDGCDGPVFGPRFKCCACPDFDYCRQCEALPTqdHaqrhgPEHLFVKI 784
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGV--H-----PEHAMLKI 43
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 671-715 4.77e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 73.06  E-value: 4.77e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 630972136  671 AICDLCQATIYGVRYKCLDCPDWDCCGAChaETAAKHPDHRFVRI 715
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESC--EAKGVHPEHAMLKI 43
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 230-491 2.84e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 58.05  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   230 SRKPLDASLGAPAQASVKAPKEAPKEAPKEAASSQHGSTAQKQPQVEGKTKTKTSSHASGGATKDTSSTrVPDDKTATTI 309
Cdd:pfam17823  134 IAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPARGI 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   310 ATSFTGGKVASSSPTSQAAPPGSAGQGRAPGSVPLNRFAELLAILNGQNVLPPKEGQKSvqaTNRPLSDLVSEMKaHLQS 389
Cdd:pfam17823  213 STAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN---MGDPHARRLSPAK-HMPS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   390 PGGSFNPAP----------------KPAHTTGSAPLDPLAEMQAALNRLRSSYKKDMAPAQTTTApsvhisKPKEPASSL 453
Cdd:pfam17823  289 DTMARNPAApmgaqaqgpiiqvstdQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKA------QAKEPSASP 362

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 630972136   454 FPLPPLNLKPSLTAAgAPTCASKPLPTFKfGSAAPDQP 491
Cdd:pfam17823  363 VPVLHTSMIPEVEAT-SPTTQPSPLLPTQ-GAAGPGIL 398
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 667-711 4.01e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 50.52  E-value: 4.01e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 630972136    667 VKHTAICDLCQATIYGVRYKCLDCPDWDCCGACHAETAAkHPDHR 711
Cdd:smart00291    1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSA-GGEHS 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 730-779 2.53e-07

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 48.20  E-value: 2.53e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 630972136    730 PCHRAIrCDGCDGPVFGPRFKCCACPDFDYCRQCEAlptqdhAQRHGPEH 779
Cdd:smart00291    1 VHHSYS-CDTCGKPIVGVRYHCLVCPDYDLCQSCFA------KGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 668-711 1.77e-06

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 45.94  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 630972136   668 KHTAICDLCQAT-IYGVRYKCLDCPDWDCCGAChaETAAKHPDHR 711
Cdd:pfam00569    2 HKVYTCNGCSNDpSIGVRYHCLRCSDYDLCQSC--FQTHKGGNHQ 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 732-764 8.34e-03

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 35.54  E-value: 8.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 630972136   732 HRAIRCDGC-DGPVFGPRFKCCACPDFDYCRQCE 764
Cdd:pfam00569    2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCF 35
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 1133-1260 6.80e-33

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 123.56  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136 1133 KELDAAFVRDISFPDGSAVAAGSRFDKVWLIRNTGSQPWPKDVGLKLIstcGRSLFDGTRSRLEPIGAdfdgrlVKPGEE 1212
Cdd:cd14947     1 PGLSAAFVEDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFV---GGDPGLLSAPERVPVPS------TVPGEE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 630972136 1213 VEVcCADLRAPDEAGKVQVFWRLATPGRVPsqpdasFGEQLWVAVNVV 1260
Cdd:cd14947    72 VDV-SVELRAPSEPGRYISYWRLVTPDGLP------FGDRLWVDITVE 112
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 1144-1259 1.89e-26

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 104.58  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136  1144 SFPDGSAVAAGSRFDKVWLIRNTGSQPWPKDVGLKLIstCGRSLFDGTRSRLEPigadfdgrlVKPGEEVEVcCADLRAP 1223
Cdd:pfam16158    1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFV--GGDNMGNVSTVLVPP---------VAPGEEVDV-SVELKAP 68

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 630972136  1224 DEAGKVQVFWRLATPGRVPsqpdasFGEQLWVAVNV 1259
Cdd:pfam16158   69 SRPGRYISYWRLKTPDGTP------FGDRLWVDITV 98
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 735-784 1.89e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 74.22  E-value: 1.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 630972136  735 IRCDGCDGPVFGPRFKCCACPDFDYCRQCEALPTqdHaqrhgPEHLFVKI 784
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGV--H-----PEHAMLKI 43
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 671-715 4.77e-16

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 73.06  E-value: 4.77e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 630972136  671 AICDLCQATIYGVRYKCLDCPDWDCCGAChaETAAKHPDHRFVRI 715
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESC--EAKGVHPEHAMLKI 43
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 672-715 3.25e-13

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 65.15  E-value: 3.25e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 630972136  672 ICDLCQATIYGVRYKCLDCPDWDCCGACHAETAAKH-PDHRFVRI 715
Cdd:cd02249     2 SCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHpPDHSFTEI 46
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 735-784 1.41e-11

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 60.53  E-value: 1.41e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 630972136  735 IRCDGCDGPVFGPRFKCCACPDFDYCRQCealpTQDHAQRHGPEHLFVKI 784
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSC----YAKGKKGHPPDHSFTEI 46
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 671-715 1.60e-09

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 54.77  E-value: 1.60e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 630972136  671 AICDLC-QATIYGVRYKCLDCPDWDCCGACHAETaaKH-PDHRFVRI 715
Cdd:cd02339     1 IICDTCrKQGIIGIRWKCAECPNYDLCTTCYHGD--KHdLEHRFYRY 45
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 735-776 2.02e-08

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 51.43  E-value: 2.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 630972136  735 IRCDGCDG-PVFGPRFKCCACPDFDYCRQCeaLPTQDHAQRHG 776
Cdd:cd02344     1 VTCDGCQMfPINGPRFKCRNCDDFDFCENC--FKTRKHNTRHT 41
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 230-491 2.84e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 58.05  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   230 SRKPLDASLGAPAQASVKAPKEAPKEAPKEAASSQHGSTAQKQPQVEGKTKTKTSSHASGGATKDTSSTrVPDDKTATTI 309
Cdd:pfam17823  134 IAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPARGI 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   310 ATSFTGGKVASSSPTSQAAPPGSAGQGRAPGSVPLNRFAELLAILNGQNVLPPKEGQKSvqaTNRPLSDLVSEMKaHLQS 389
Cdd:pfam17823  213 STAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN---MGDPHARRLSPAK-HMPS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630972136   390 PGGSFNPAP----------------KPAHTTGSAPLDPLAEMQAALNRLRSSYKKDMAPAQTTTApsvhisKPKEPASSL 453
Cdd:pfam17823  289 DTMARNPAApmgaqaqgpiiqvstdQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKA------QAKEPSASP 362

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 630972136   454 FPLPPLNLKPSLTAAgAPTCASKPLPTFKfGSAAPDQP 491
Cdd:pfam17823  363 VPVLHTSMIPEVEAT-SPTTQPSPLLPTQ-GAAGPGIL 398
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 735-784 3.47e-08

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 50.92  E-value: 3.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 630972136  735 IRCDGC-DGPVFGPRFKCCACPDFDYCRQCEalptqdHAQRHGPEHLFVKI 784
Cdd:cd02339     1 IICDTCrKQGIIGIRWKCAECPNYDLCTTCY------HGDKHDLEHRFYRY 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 667-711 4.01e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 50.52  E-value: 4.01e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 630972136    667 VKHTAICDLCQATIYGVRYKCLDCPDWDCCGACHAETAAkHPDHR 711
Cdd:smart00291    1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSA-GGEHS 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 730-779 2.53e-07

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 48.20  E-value: 2.53e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 630972136    730 PCHRAIrCDGCDGPVFGPRFKCCACPDFDYCRQCEAlptqdhAQRHGPEH 779
Cdd:smart00291    1 VHHSYS-CDTCGKPIVGVRYHCLVCPDYDLCQSCFA------KGSAGGEH 43
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 668-711 1.77e-06

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 45.94  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 630972136   668 KHTAICDLCQAT-IYGVRYKCLDCPDWDCCGAChaETAAKHPDHR 711
Cdd:pfam00569    2 HKVYTCNGCSNDpSIGVRYHCLRCSDYDLCQSC--FQTHKGGNHQ 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 673-712 1.95e-05

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 43.10  E-value: 1.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 630972136  673 CDLCQATIY-GVRYKCLDCPDWDCCGACHaETAAKHPDHRF 712
Cdd:cd02338     3 CDGCGKSNFtGRRYKCLICYDYDLCADCY-DSGVTTERHLF 42
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 735-779 4.50e-05

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 41.95  E-value: 4.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 630972136  735 IRCDGCD-GPVFGPRFKCCACPDFDYCRQCeaLPTQDHAQRHGPEH 779
Cdd:cd02338     1 VSCDGCGkSNFTGRRYKCLICYDYDLCADC--YDSGVTTERHLFDH 44
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 673-715 5.84e-05

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 41.65  E-value: 5.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 630972136  673 CDLC-QATIYGVRYKCLDCPDWDC--CGACHAETAAKHPDHRFVRI 715
Cdd:cd02341     3 CDSCgIEPIPGTRYHCSECDDGDFdlCQDCVVKGESHQEDHWLVKI 48
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 673-712 1.30e-04

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 40.74  E-value: 1.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 630972136  673 CDLCQATIYG-VRYKCLDCPDWDCCGACH---AETAAKHPDHRF 712
Cdd:cd02335     3 CDYCSKDITGtIRIKCAECPDFDLCLECFsagAEIGKHRNDHNY 46
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 735-776 4.32e-04

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 39.20  E-value: 4.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 630972136  735 IRCDGCDGPVFG-PRFKCCACPDFDYCRQC--EALPTQDHAQRHG 776
Cdd:cd02335     1 YHCDYCSKDITGtIRIKCAECPDFDLCLECfsAGAEIGKHRNDHN 45
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 673-715 1.35e-03

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 37.95  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 630972136  673 CDLCQA-TIYGVRYKCLDCPDWDCCGACHaETAAKHPDHRFVRI 715
Cdd:cd02344     3 CDGCQMfPINGPRFKCRNCDDFDFCENCF-KTRKHNTRHTFGRI 45
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 671-714 2.68e-03

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 36.95  E-value: 2.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 630972136  671 AICDLCQAT-IYGVRYKCLDCPDWDCCGAC--HAETAAKHPDHRFVR 714
Cdd:cd02334     1 AKCNICKEFpITGFRYRCLKCFNYDLCQSCffSGRTSKSHKNSHPMK 47
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 735-763 3.62e-03

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 36.79  E-value: 3.62e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 630972136  735 IRCDGCD-GPVFGPRFKCCACPDFDYCRQC 763
Cdd:cd02342     1 IQCDGCGvLPITGPRYKSKVKEDYDLCTIC 30
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 732-764 8.34e-03

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 35.54  E-value: 8.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 630972136   732 HRAIRCDGC-DGPVFGPRFKCCACPDFDYCRQCE 764
Cdd:pfam00569    2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCF 35
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 735-784 9.60e-03

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 35.75  E-value: 9.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 630972136  735 IRCDGCDGPVFGPRFKCCACPDFDYCRQCeaLPTQDHAQRHGPEHLFVKI 784
Cdd:cd02343     1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTC--FLGGVKPEGHEDDHEMVNM 48
 
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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