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Conserved domains on  [gi|19075883|ref|NP_588383|]
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exocyst complex subunit Exo5-like, F-box protein Pof6 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sec10 super family cl20335
Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 ...
202-862 3.14e-60

Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 residues long) of the eukaryotic exocyst complex, which specifically affects the synthesis and delivery of secretory and basolateral plasma membrane proteins.


The actual alignment was detected with superfamily member pfam07393:

Pssm-ID: 399988  Cd Length: 704  Bit Score: 217.99  E-value: 3.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   202 RTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMY 281
Cdd:pfam07393  72 DKKLECAQIARQLLSIAQKLDPLPKTENTRANIEKYSERLEKELLKEFDAAYRKEDFERMKECAKILQEFNGGASVIQLF 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   282 LaKQTDFVRSFFHFDPYSLFISNNLEEIHINWNI-------LESVVNDTIKLLESESKFSEATLPEPELVQVPYAKDILG 354
Cdd:pfam07393 152 V-NQHQFFIDRDVTDEVDGLDDEIWEKLADPDQHpsiveesLQALFSEVVVVVKEEAAIIKRVFPNPEVVMQKFIQRVFA 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   355 NSLKDYVISICEHIGEEETELFLVFISGFYGLCKKF------FSIPNGPALVDT-------IFQPQIDIFISQELHYFKT 421
Cdd:pfam07393 231 QVIQQRLEALLDKAKSISQLAYLRSLHSLYSQTLKLvkdlkeFGSTENPDLSAFldqltedLFVPHLDSYLEREKKSLEE 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   422 VGWSLVDQWDQkLEEKEDATECFfyknvsQNTAKNNFLETFKNVMllpvslftipSENNSASNLAEKAIEQKEEEDPELS 501
Cdd:pfam07393 311 LYESLLSKFTT-LHERAISAKSL------TNKDKKDFLTSFKASL----------MGSKLASKSKLSQINRFLKSSLERT 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   502 KLDAARFVPANiyvskdrlkhlptteLAAQAAVLDSKLEGISTMFSLELALKIVHLCKVSLARAKVF-MGTSVPQDddik 580
Cdd:pfam07393 374 LKRAGLFENID---------------SSAKAAINPIELEGIDSLLSIEVALSMLKWAAESLGRALELsSPTELPKN---- 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   581 glSKDLFVQLLRELGQGHLKHGFDRAIEHLSSFDPRRdfssNTVEPVVKFLELINVGDMIQQMMDSFFNEEMSP-ICVKD 659
Cdd:pfam07393 435 --IEALFDLLLRALGHEYIETALEAALYALSSQEIAE----KTGVPDLSFLEVVRVCDEILSLMSVYIKQILIPlLTNSP 508
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   660 DMFDPAIAEKKKFEQLLDERAAFGLHKGINVLIEHADFLLeTKTPMNLFSDQTiGSITNTIEPTAAAKNVVQFLGFHMRI 739
Cdd:pfam07393 509 DIRREMVKKKNSFISRLEEKVNAGLQKTIDVLMGWVKYIL-SKQKKTDFRPKE-DELTMDVQPTEACQEVVDFLSSVHSQ 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   740 LVGRADHEILDVFYKEVGMRLFDSLTRYIKSHKFSVDGGLKLLSDCNLYYEFIHSLHQSSLLPYFKTLKEIAHLFIIDGK 819
Cdd:pfam07393 587 LVGSLDGSNLEAFLTEIGLRLHRLLLEHLKKFTVNSEGGLILTKDINEYQKFVKSWGIPELLEKFELLRELGNLFIVQPD 666
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 19075883   820 NAEEigkLATDTSrfSSAFHTEEVYEILHSRIDWLNIKYEVDK 862
Cdd:pfam07393 667 LLKE---LVTEGA--LANLDRELIREYIQLREDYNQIKLDVEL 704
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
30-74 1.07e-13

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438911  Cd Length: 45  Bit Score: 65.73  E-value: 1.07e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19075883  30 FGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKL 74
Cdd:cd22139   1 WLCLPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 45
 
Name Accession Description Interval E-value
Sec10 pfam07393
Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 ...
202-862 3.14e-60

Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 residues long) of the eukaryotic exocyst complex, which specifically affects the synthesis and delivery of secretory and basolateral plasma membrane proteins.


Pssm-ID: 399988  Cd Length: 704  Bit Score: 217.99  E-value: 3.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   202 RTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMY 281
Cdd:pfam07393  72 DKKLECAQIARQLLSIAQKLDPLPKTENTRANIEKYSERLEKELLKEFDAAYRKEDFERMKECAKILQEFNGGASVIQLF 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   282 LaKQTDFVRSFFHFDPYSLFISNNLEEIHINWNI-------LESVVNDTIKLLESESKFSEATLPEPELVQVPYAKDILG 354
Cdd:pfam07393 152 V-NQHQFFIDRDVTDEVDGLDDEIWEKLADPDQHpsiveesLQALFSEVVVVVKEEAAIIKRVFPNPEVVMQKFIQRVFA 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   355 NSLKDYVISICEHIGEEETELFLVFISGFYGLCKKF------FSIPNGPALVDT-------IFQPQIDIFISQELHYFKT 421
Cdd:pfam07393 231 QVIQQRLEALLDKAKSISQLAYLRSLHSLYSQTLKLvkdlkeFGSTENPDLSAFldqltedLFVPHLDSYLEREKKSLEE 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   422 VGWSLVDQWDQkLEEKEDATECFfyknvsQNTAKNNFLETFKNVMllpvslftipSENNSASNLAEKAIEQKEEEDPELS 501
Cdd:pfam07393 311 LYESLLSKFTT-LHERAISAKSL------TNKDKKDFLTSFKASL----------MGSKLASKSKLSQINRFLKSSLERT 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   502 KLDAARFVPANiyvskdrlkhlptteLAAQAAVLDSKLEGISTMFSLELALKIVHLCKVSLARAKVF-MGTSVPQDddik 580
Cdd:pfam07393 374 LKRAGLFENID---------------SSAKAAINPIELEGIDSLLSIEVALSMLKWAAESLGRALELsSPTELPKN---- 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   581 glSKDLFVQLLRELGQGHLKHGFDRAIEHLSSFDPRRdfssNTVEPVVKFLELINVGDMIQQMMDSFFNEEMSP-ICVKD 659
Cdd:pfam07393 435 --IEALFDLLLRALGHEYIETALEAALYALSSQEIAE----KTGVPDLSFLEVVRVCDEILSLMSVYIKQILIPlLTNSP 508
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   660 DMFDPAIAEKKKFEQLLDERAAFGLHKGINVLIEHADFLLeTKTPMNLFSDQTiGSITNTIEPTAAAKNVVQFLGFHMRI 739
Cdd:pfam07393 509 DIRREMVKKKNSFISRLEEKVNAGLQKTIDVLMGWVKYIL-SKQKKTDFRPKE-DELTMDVQPTEACQEVVDFLSSVHSQ 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   740 LVGRADHEILDVFYKEVGMRLFDSLTRYIKSHKFSVDGGLKLLSDCNLYYEFIHSLHQSSLLPYFKTLKEIAHLFIIDGK 819
Cdd:pfam07393 587 LVGSLDGSNLEAFLTEIGLRLHRLLLEHLKKFTVNSEGGLILTKDINEYQKFVKSWGIPELLEKFELLRELGNLFIVQPD 666
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 19075883   820 NAEEigkLATDTSrfSSAFHTEEVYEILHSRIDWLNIKYEVDK 862
Cdd:pfam07393 667 LLKE---LVTEGA--LANLDRELIREYIQLREDYNQIKLDVEL 704
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
30-74 1.07e-13

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438911  Cd Length: 45  Bit Score: 65.73  E-value: 1.07e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19075883  30 FGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKL 74
Cdd:cd22139   1 WLCLPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 45
FBOX smart00256
A Receptor for Ubiquitination Targets;
33-73 3.34e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 44.35  E-value: 3.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 19075883     33 LTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKK 73
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
F-box-like pfam12937
F-box-like; This is an F-box-like family.
39-70 1.73e-05

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 42.47  E-value: 1.73e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19075883    39 LKIFTLISTPDLCNCRLVCRKFQQLCDYNSIY 70
Cdd:pfam12937  10 LQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
 
Name Accession Description Interval E-value
Sec10 pfam07393
Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 ...
202-862 3.14e-60

Exocyst complex component Sec10; This family contains the Sec10 component (approximately 650 residues long) of the eukaryotic exocyst complex, which specifically affects the synthesis and delivery of secretory and basolateral plasma membrane proteins.


Pssm-ID: 399988  Cd Length: 704  Bit Score: 217.99  E-value: 3.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   202 RTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMY 281
Cdd:pfam07393  72 DKKLECAQIARQLLSIAQKLDPLPKTENTRANIEKYSERLEKELLKEFDAAYRKEDFERMKECAKILQEFNGGASVIQLF 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   282 LaKQTDFVRSFFHFDPYSLFISNNLEEIHINWNI-------LESVVNDTIKLLESESKFSEATLPEPELVQVPYAKDILG 354
Cdd:pfam07393 152 V-NQHQFFIDRDVTDEVDGLDDEIWEKLADPDQHpsiveesLQALFSEVVVVVKEEAAIIKRVFPNPEVVMQKFIQRVFA 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   355 NSLKDYVISICEHIGEEETELFLVFISGFYGLCKKF------FSIPNGPALVDT-------IFQPQIDIFISQELHYFKT 421
Cdd:pfam07393 231 QVIQQRLEALLDKAKSISQLAYLRSLHSLYSQTLKLvkdlkeFGSTENPDLSAFldqltedLFVPHLDSYLEREKKSLEE 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   422 VGWSLVDQWDQkLEEKEDATECFfyknvsQNTAKNNFLETFKNVMllpvslftipSENNSASNLAEKAIEQKEEEDPELS 501
Cdd:pfam07393 311 LYESLLSKFTT-LHERAISAKSL------TNKDKKDFLTSFKASL----------MGSKLASKSKLSQINRFLKSSLERT 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   502 KLDAARFVPANiyvskdrlkhlptteLAAQAAVLDSKLEGISTMFSLELALKIVHLCKVSLARAKVF-MGTSVPQDddik 580
Cdd:pfam07393 374 LKRAGLFENID---------------SSAKAAINPIELEGIDSLLSIEVALSMLKWAAESLGRALELsSPTELPKN---- 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   581 glSKDLFVQLLRELGQGHLKHGFDRAIEHLSSFDPRRdfssNTVEPVVKFLELINVGDMIQQMMDSFFNEEMSP-ICVKD 659
Cdd:pfam07393 435 --IEALFDLLLRALGHEYIETALEAALYALSSQEIAE----KTGVPDLSFLEVVRVCDEILSLMSVYIKQILIPlLTNSP 508
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   660 DMFDPAIAEKKKFEQLLDERAAFGLHKGINVLIEHADFLLeTKTPMNLFSDQTiGSITNTIEPTAAAKNVVQFLGFHMRI 739
Cdd:pfam07393 509 DIRREMVKKKNSFISRLEEKVNAGLQKTIDVLMGWVKYIL-SKQKKTDFRPKE-DELTMDVQPTEACQEVVDFLSSVHSQ 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075883   740 LVGRADHEILDVFYKEVGMRLFDSLTRYIKSHKFSVDGGLKLLSDCNLYYEFIHSLHQSSLLPYFKTLKEIAHLFIIDGK 819
Cdd:pfam07393 587 LVGSLDGSNLEAFLTEIGLRLHRLLLEHLKKFTVNSEGGLILTKDINEYQKFVKSWGIPELLEKFELLRELGNLFIVQPD 666
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 19075883   820 NAEEigkLATDTSrfSSAFHTEEVYEILHSRIDWLNIKYEVDK 862
Cdd:pfam07393 667 LLKE---LVTEGA--LANLDRELIREYIQLREDYNQIKLDVEL 704
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
30-74 1.07e-13

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438911  Cd Length: 45  Bit Score: 65.73  E-value: 1.07e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19075883  30 FGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKL 74
Cdd:cd22139   1 WLCLPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 45
FBOX smart00256
A Receptor for Ubiquitination Targets;
33-73 3.34e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 44.35  E-value: 3.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 19075883     33 LTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKK 73
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
F-box-like pfam12937
F-box-like; This is an F-box-like family.
39-70 1.73e-05

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 42.47  E-value: 1.73e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19075883    39 LKIFTLISTPDLCNCRLVCRKFQQLCDYNSIY 70
Cdd:pfam12937  10 LQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
37-65 1.92e-04

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 39.35  E-value: 1.92e-04
                        10        20
                ....*....|....*....|....*....
gi 19075883  37 IYLKIFTLISTPDLCNCRLVCRKFQQLCD 65
Cdd:cd09917   7 ILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
32-72 1.92e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 39.45  E-value: 1.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 19075883    32 CLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVK 72
Cdd:pfam00646   3 DLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
30-64 4.87e-03

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438892  Cd Length: 44  Bit Score: 35.82  E-value: 4.87e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19075883  30 FGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLC 64
Cdd:cd22120   1 FDRLPDDVILQIFSHLPTNQLCRCARVCRRWYNLA 35
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
39-67 8.30e-03

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438856  Cd Length: 49  Bit Score: 35.31  E-value: 8.30e-03
                        10        20
                ....*....|....*....|....*....
gi 19075883  39 LKIFTLISTPDLCNCRLVCRKFQQLCDYN 67
Cdd:cd22084  10 LNILSFLDYRDLISCSQVCRRLNQLCSHD 38
 
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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