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Conserved domains on  [gi|2075850389|emb|CAG5106876|]
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Similar to SF3B2: Splicing factor 3B subunit 2 (Homo sapiens) [Cotesia congregata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF382 pfam04037
Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b ...
 1144-1256 1.81e-73

Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b subunit 2 and it's orthologues. Splicing factor 3b subunit 2 or SAP145 is a suppressor of U2 snRNA mutations. Pre-mRNA splicing is catalyzed by a large ribonucleoprotein complex called the spliceosome. Spliceosomes are multi-component enzymes that catalyze pre-mRNA splicing and form step-wise by the ordered interaction of UsnRNPs and non-snRNP proteins with short conserved regions of the pre-mRNA at the 5' and 3' splice sites and branch site.


:

Pssm-ID: 461140  Cd Length: 126  Bit Score: 240.10  E-value: 1.81e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1144 DPKLLVQLKAHRNTVPVPRHWCFKRKYLQGKRGIEKPPFDLPDFIKRTGITEMRASLQERDDGRTLKAKMRERARPKLGK 1223
Cdd:pfam04037   14 DPYLLVHLKSSRNTVPVPSHWSQKRKYLSGKRGIEKPPFQLPDFIEDTGIEEMRDALLEKEDEKSLKQKQRERVQPKMGK 93

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2075850389 1224 IDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKE 1256
Cdd:pfam04037   94 LDIDYQKLHDAFFKFQTKPRLTPFGDLYYEGKE 126
HOIP-UBA super family cl28811
HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like ...
 1026-1129 1.55e-33

HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like proteins. E3 ubiquitin-protein ligase RNF31 is often referred to as HOIL-1L binding partner. The interaction of HOIL-1L and HOIP is thus via the UBL-UBA interaction. this interaction is important in E3 complex formation and the subsequent activation of NF-kappaB. This family contains two UBA-like domains.


The actual alignment was detected with superfamily member pfam16678:

Pssm-ID: 465229 [Multi-domain]  Cd Length: 150  Bit Score: 126.99  E-value: 1.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1026 TLTRQGLEIVELLREAERQGFSADDIQVALAQ-GAVNPIDWLINQWPHLIETVQILVSTRGKEMPdcKNDIGFLSIVEAK 1104
Cdd:pfam16678    1 KMREEGLELVHLIREAEKYGFSPEEVYAALRYsGGSNPLQWLKTEWPHLLDTVAALAASEGKELK--ENTVGVLSRAEAR 78

                           90       100
                   ....*....|....*....|....*
gi 2075850389 1105 EVLRACKGDVWTSVTRAIQLRQQKL 1129
Cdd:pfam16678   79 LALLEAGGDVEKAVKECVRDRRKKV 103
PSP smart00581
proline-rich domain in spliceosome associated proteins;
1261-1319 1.07e-24

proline-rich domain in spliceosome associated proteins;


:

Pssm-ID: 128850  Cd Length: 54  Bit Score: 98.20  E-value: 1.07e-24
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075850389  1261 LKEKKPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPPSYPNLKIPGLNAPIPE 1319
Cdd:smart00581    1 FKHFKPGRISDELREALGLPPG-----QPPPWLYRMRRLGYPPGYPRLKIPGLNAPIPL 54
Bbox1_HOIP cd19815
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ...
 110-152 5.54e-14

B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


:

Pssm-ID: 380873  Cd Length: 43  Bit Score: 67.36  E-value: 5.54e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2075850389  110 KCALCGAHNLFARCDACNENFCETCDDMNHKHPKRRGHVRRRI 152
Cdd:cd19815      1 LCDLCGEAAASVFCASCEDKLCLSCDDLYHKHPARRSHHRQPI 43
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 742-763 4.79e-05

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 41.53  E-value: 4.79e-05
                            10        20
                    ....*....|....*....|..
gi 2075850389   742 EWACEHCTFINEAKERVCIVCC 763
Cdd:smart00547    2 DWECPACTFLNFASRSKCFACG 23
PTZ00121 super family cl31754
MAEBL; Provisional
 516-881 1.26e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  516 EFRSVSSRQQSEnddiRRRRNTMDHYLSSRQNSETDDSRgRKRTEPTNVNPDSRSRLMSSRHNSETEDdhrlRRKTESFN 595
Cdd:PTZ00121  1556 ELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELK 1626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  596 NDEKLMKNNGTLRsrrKSNAEYER--EVLNKKTNSNTTRN----RFANSSDSTGEliTTNNNNNSNNKRAESVVREI-KK 668
Cdd:PTZ00121  1627 KAEEEKKKVEQLK---KKEAEEKKkaEELKKAEEENKIKAaeeaKKAEEDKKKAE--EAKKAEEDEKKAAEALKKEAeEA 1701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  669 SPLREVRKSVEREVireptpkesikeptpEKNHKVQPDENIKQDKINEAKSSASQIKKTSQQPAAEE----KTEEDKEWA 744
Cdd:PTZ00121  1702 KKAEELKKKEAEEK---------------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkKIAHLKKEE 1766

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  745 CEHCTFINEAKERVCIVCCKTKRSALPPNPE----NTPESSENVQESTPEPATKVSSIKmsngeesgdSTATTQSKDVEI 820
Cdd:PTZ00121  1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikDIFDNFANIIEGGKEGNLVINDSK---------EMEDSAIKEVAD 1837

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075850389  821 VKNDQELNSNIVEDNQTNKlesvlNSslrENIKTHASISTSTSPIKELEETTSEVIKTQDN 881
Cdd:PTZ00121  1838 SKNMQLEEADAFEKHKFNK-----NN---ENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
 
Name Accession Description Interval E-value
DUF382 pfam04037
Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b ...
 1144-1256 1.81e-73

Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b subunit 2 and it's orthologues. Splicing factor 3b subunit 2 or SAP145 is a suppressor of U2 snRNA mutations. Pre-mRNA splicing is catalyzed by a large ribonucleoprotein complex called the spliceosome. Spliceosomes are multi-component enzymes that catalyze pre-mRNA splicing and form step-wise by the ordered interaction of UsnRNPs and non-snRNP proteins with short conserved regions of the pre-mRNA at the 5' and 3' splice sites and branch site.


Pssm-ID: 461140  Cd Length: 126  Bit Score: 240.10  E-value: 1.81e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1144 DPKLLVQLKAHRNTVPVPRHWCFKRKYLQGKRGIEKPPFDLPDFIKRTGITEMRASLQERDDGRTLKAKMRERARPKLGK 1223
Cdd:pfam04037   14 DPYLLVHLKSSRNTVPVPSHWSQKRKYLSGKRGIEKPPFQLPDFIEDTGIEEMRDALLEKEDEKSLKQKQRERVQPKMGK 93

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2075850389 1224 IDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKE 1256
Cdd:pfam04037   94 LDIDYQKLHDAFFKFQTKPRLTPFGDLYYEGKE 126
CUS1 COG5182
Splicing factor 3b, subunit 2 [RNA processing and modification];
1144-1346 8.48e-70

Splicing factor 3b, subunit 2 [RNA processing and modification];


Pssm-ID: 227509 [Multi-domain]  Cd Length: 429  Bit Score: 241.43  E-value: 8.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1144 DPKLLVQLKAHRNTVPVPRHWCFKRKYLQGKRGIEKPPFDLPDFIKRTGITEMRASLQERDDGRTLKAKMRERARPKLGK 1223
Cdd:COG5182    158 DPMSLNRMKGCSNGVPVPRHWRSKSRYLSGHGYHKPRPFELPRHIIGTGIPQMRRMMREREAGMSLRERIRERVQPKMGG 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1224 IDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKEFETRLKEKKPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPP 1303
Cdd:COG5182    238 LDVDYRKLHDAFFSLGPKPYLSKFGEFYEEVDNDYRFVKKKRPGAISAELREALGIDSG-----TPPPWLFNMQKHGMPP 312

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2075850389 1304 SYPNLKIPGLN-APIP-EGCAFGYHAGGWGKPPVDETGRPLYGDV 1346
Cdd:COG5182    313 SYPDLKIPGLNwAPIPlEGDVYGYQPPGWHEPLFEVGPETAEGEL 357
HOIP-UBA pfam16678
HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like ...
 1026-1129 1.55e-33

HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like proteins. E3 ubiquitin-protein ligase RNF31 is often referred to as HOIL-1L binding partner. The interaction of HOIL-1L and HOIP is thus via the UBL-UBA interaction. this interaction is important in E3 complex formation and the subsequent activation of NF-kappaB. This family contains two UBA-like domains.


Pssm-ID: 465229 [Multi-domain]  Cd Length: 150  Bit Score: 126.99  E-value: 1.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1026 TLTRQGLEIVELLREAERQGFSADDIQVALAQ-GAVNPIDWLINQWPHLIETVQILVSTRGKEMPdcKNDIGFLSIVEAK 1104
Cdd:pfam16678    1 KMREEGLELVHLIREAEKYGFSPEEVYAALRYsGGSNPLQWLKTEWPHLLDTVAALAASEGKELK--ENTVGVLSRAEAR 78

                           90       100
                   ....*....|....*....|....*
gi 2075850389 1105 EVLRACKGDVWTSVTRAIQLRQQKL 1129
Cdd:pfam16678   79 LALLEAGGDVEKAVKECVRDRRKKV 103
PSP smart00581
proline-rich domain in spliceosome associated proteins;
1261-1319 1.07e-24

proline-rich domain in spliceosome associated proteins;


Pssm-ID: 128850  Cd Length: 54  Bit Score: 98.20  E-value: 1.07e-24
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075850389  1261 LKEKKPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPPSYPNLKIPGLNAPIPE 1319
Cdd:smart00581    1 FKHFKPGRISDELREALGLPPG-----QPPPWLYRMRRLGYPPGYPRLKIPGLNAPIPL 54
PSP pfam04046
PSP; Proline rich domain found in numerous spliceosome associated proteins.
 1265-1315 3.42e-23

PSP; Proline rich domain found in numerous spliceosome associated proteins.


Pssm-ID: 461145  Cd Length: 46  Bit Score: 93.66  E-value: 3.42e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2075850389 1265 KPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPPSYPNLKIPGLNA 1315
Cdd:pfam04046    1 KPGKLSDELREALGLPEG-----QPPPWLYRMQRLGPPPSYPNLKIPGLNA 46
Bbox1_HOIP cd19815
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ...
 110-152 5.54e-14

B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380873  Cd Length: 43  Bit Score: 67.36  E-value: 5.54e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2075850389  110 KCALCGAHNLFARCDACNENFCETCDDMNHKHPKRRGHVRRRI 152
Cdd:cd19815      1 LCDLCGEAAASVFCASCEDKLCLSCDDLYHKHPARRSHHRQPI 43
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 742-763 4.79e-05

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 41.53  E-value: 4.79e-05
                            10        20
                    ....*....|....*....|..
gi 2075850389   742 EWACEHCTFINEAKERVCIVCC 763
Cdd:smart00547    2 DWECPACTFLNFASRSKCFACG 23
PTZ00121 PTZ00121
MAEBL; Provisional
 516-881 1.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  516 EFRSVSSRQQSEnddiRRRRNTMDHYLSSRQNSETDDSRgRKRTEPTNVNPDSRSRLMSSRHNSETEDdhrlRRKTESFN 595
Cdd:PTZ00121  1556 ELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELK 1626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  596 NDEKLMKNNGTLRsrrKSNAEYER--EVLNKKTNSNTTRN----RFANSSDSTGEliTTNNNNNSNNKRAESVVREI-KK 668
Cdd:PTZ00121  1627 KAEEEKKKVEQLK---KKEAEEKKkaEELKKAEEENKIKAaeeaKKAEEDKKKAE--EAKKAEEDEKKAAEALKKEAeEA 1701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  669 SPLREVRKSVEREVireptpkesikeptpEKNHKVQPDENIKQDKINEAKSSASQIKKTSQQPAAEE----KTEEDKEWA 744
Cdd:PTZ00121  1702 KKAEELKKKEAEEK---------------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkKIAHLKKEE 1766

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  745 CEHCTFINEAKERVCIVCCKTKRSALPPNPE----NTPESSENVQESTPEPATKVSSIKmsngeesgdSTATTQSKDVEI 820
Cdd:PTZ00121  1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikDIFDNFANIIEGGKEGNLVINDSK---------EMEDSAIKEVAD 1837

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075850389  821 VKNDQELNSNIVEDNQTNKlesvlNSslrENIKTHASISTSTSPIKELEETTSEVIKTQDN 881
Cdd:PTZ00121  1838 SKNMQLEEADAFEKHKFNK-----NN---ENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
 
Name Accession Description Interval E-value
DUF382 pfam04037
Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b ...
 1144-1256 1.81e-73

Domain of unknown function (DUF382); This domain is specific to the human splicing factor 3b subunit 2 and it's orthologues. Splicing factor 3b subunit 2 or SAP145 is a suppressor of U2 snRNA mutations. Pre-mRNA splicing is catalyzed by a large ribonucleoprotein complex called the spliceosome. Spliceosomes are multi-component enzymes that catalyze pre-mRNA splicing and form step-wise by the ordered interaction of UsnRNPs and non-snRNP proteins with short conserved regions of the pre-mRNA at the 5' and 3' splice sites and branch site.


Pssm-ID: 461140  Cd Length: 126  Bit Score: 240.10  E-value: 1.81e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1144 DPKLLVQLKAHRNTVPVPRHWCFKRKYLQGKRGIEKPPFDLPDFIKRTGITEMRASLQERDDGRTLKAKMRERARPKLGK 1223
Cdd:pfam04037   14 DPYLLVHLKSSRNTVPVPSHWSQKRKYLSGKRGIEKPPFQLPDFIEDTGIEEMRDALLEKEDEKSLKQKQRERVQPKMGK 93

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2075850389 1224 IDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKE 1256
Cdd:pfam04037   94 LDIDYQKLHDAFFKFQTKPRLTPFGDLYYEGKE 126
CUS1 COG5182
Splicing factor 3b, subunit 2 [RNA processing and modification];
1144-1346 8.48e-70

Splicing factor 3b, subunit 2 [RNA processing and modification];


Pssm-ID: 227509 [Multi-domain]  Cd Length: 429  Bit Score: 241.43  E-value: 8.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1144 DPKLLVQLKAHRNTVPVPRHWCFKRKYLQGKRGIEKPPFDLPDFIKRTGITEMRASLQERDDGRTLKAKMRERARPKLGK 1223
Cdd:COG5182    158 DPMSLNRMKGCSNGVPVPRHWRSKSRYLSGHGYHKPRPFELPRHIIGTGIPQMRRMMREREAGMSLRERIRERVQPKMGG 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1224 IDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKEFETRLKEKKPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPP 1303
Cdd:COG5182    238 LDVDYRKLHDAFFSLGPKPYLSKFGEFYEEVDNDYRFVKKKRPGAISAELREALGIDSG-----TPPPWLFNMQKHGMPP 312

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2075850389 1304 SYPNLKIPGLN-APIP-EGCAFGYHAGGWGKPPVDETGRPLYGDV 1346
Cdd:COG5182    313 SYPDLKIPGLNwAPIPlEGDVYGYQPPGWHEPLFEVGPETAEGEL 357
HOIP-UBA pfam16678
HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like ...
 1026-1129 1.55e-33

HOIP UBA domain pair; HOIP-UB is a binding domain on E3 ubiquitin-protein ligase RNF31 like proteins. E3 ubiquitin-protein ligase RNF31 is often referred to as HOIL-1L binding partner. The interaction of HOIL-1L and HOIP is thus via the UBL-UBA interaction. this interaction is important in E3 complex formation and the subsequent activation of NF-kappaB. This family contains two UBA-like domains.


Pssm-ID: 465229 [Multi-domain]  Cd Length: 150  Bit Score: 126.99  E-value: 1.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389 1026 TLTRQGLEIVELLREAERQGFSADDIQVALAQ-GAVNPIDWLINQWPHLIETVQILVSTRGKEMPdcKNDIGFLSIVEAK 1104
Cdd:pfam16678    1 KMREEGLELVHLIREAEKYGFSPEEVYAALRYsGGSNPLQWLKTEWPHLLDTVAALAASEGKELK--ENTVGVLSRAEAR 78

                           90       100
                   ....*....|....*....|....*
gi 2075850389 1105 EVLRACKGDVWTSVTRAIQLRQQKL 1129
Cdd:pfam16678   79 LALLEAGGDVEKAVKECVRDRRKKV 103
PSP smart00581
proline-rich domain in spliceosome associated proteins;
1261-1319 1.07e-24

proline-rich domain in spliceosome associated proteins;


Pssm-ID: 128850  Cd Length: 54  Bit Score: 98.20  E-value: 1.07e-24
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075850389  1261 LKEKKPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPPSYPNLKIPGLNAPIPE 1319
Cdd:smart00581    1 FKHFKPGRISDELREALGLPPG-----QPPPWLYRMRRLGYPPGYPRLKIPGLNAPIPL 54
PSP pfam04046
PSP; Proline rich domain found in numerous spliceosome associated proteins.
 1265-1315 3.42e-23

PSP; Proline rich domain found in numerous spliceosome associated proteins.


Pssm-ID: 461145  Cd Length: 46  Bit Score: 93.66  E-value: 3.42e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2075850389 1265 KPGELSDELRTALGMPVGpnchkVPPPWLIAMQRYGPPPSYPNLKIPGLNA 1315
Cdd:pfam04046    1 KPGKLSDELREALGLPEG-----QPPPWLYRMQRLGPPPSYPNLKIPGLNA 46
Bbox1_HOIP cd19815
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ...
 110-152 5.54e-14

B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380873  Cd Length: 43  Bit Score: 67.36  E-value: 5.54e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2075850389  110 KCALCGAHNLFARCDACNENFCETCDDMNHKHPKRRGHVRRRI 152
Cdd:cd19815      1 LCDLCGEAAASVFCASCEDKLCLSCDDLYHKHPARRSHHRQPI 43
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 110-152 5.71e-07

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 47.49  E-value: 5.71e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2075850389  110 KCALCGAHNLFARCDACNENFCETCDDMNHKHPK-RRGHVRRRI 152
Cdd:cd19757      1 LCDECEEREATVYCLECEEFLCDDCSDAIHRRGKlTRSHKLVPL 44
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 742-763 4.79e-05

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 41.53  E-value: 4.79e-05
                            10        20
                    ....*....|....*....|..
gi 2075850389   742 EWACEHCTFINEAKERVCIVCC 763
Cdd:smart00547    2 DWECPACTFLNFASRSKCFACG 23
Bbox1_DUF2009 cd20208
B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; ...
 111-152 9.06e-05

B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; This group is composed of uncharacterized proteins containing a zinc finger B-box domain and a DUF2009 domain, and similar zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380909 [Multi-domain]  Cd Length: 43  Bit Score: 41.21  E-value: 9.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2075850389  111 CALCGAHNLFARCDACNENFCETCDDMNHKHPKRRGHVRRRI 152
Cdd:cd20208      2 CIECEDQPAEVRCEECGDEFCEVCFQSQHRKGKRRLHSFRPV 43
Bbox2_MYCBP2 cd19799
B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, ...
 123-155 9.06e-04

B-box-type 2 zinc finger found in Myc-binding protein 2 (MYCBP2) and similar proteins; MYCBP2, also termed protein associated with Myc (Pam), is an atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. MYCBP2 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380857  Cd Length: 50  Bit Score: 38.53  E-value: 9.06e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2075850389  123 CDACNENFCETCDDMNHKHPKRRGHVRRRIVTD 155
Cdd:cd19799     17 CCDCGNYLCAECDRFLHLHRKNRSHQRQVFKEE 49
Bbox1_CYLD cd19816
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ...
 111-152 9.06e-04

B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; CYLD, also termed ubiquitin carboxyl-terminal hydrolase CYLD, or deubiquitinating enzyme CYLD, or ubiquitin thioesterase CYLD, or ubiquitin-specific-processing protease CYLD, is a microtubule-associated deubiquitinase that specifically cleaves Lys-63-linked polyubiquitin chains. It plays a pivotal role in a wide range of cellular activities, including innate immunity, cell division, and ciliogenesis. CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Structural characterization reveals a small zinc-binding B-box inserted within the ubiquitin specific protease (USP) domain of CYLD. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and is responsible for its intermolecular interaction and cytoplasmic localization. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380874  Cd Length: 56  Bit Score: 38.99  E-value: 9.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2075850389  111 CALCGAHNLFaRCDACNEN---------FCETCDDMNHKHPKRRGHVRRRI 152
Cdd:cd19816      4 CIICGGLAEY-ECRDCYLDpgiggkikaFCKKCNKQTHLHPKRQNHKPRPL 53
PTZ00121 PTZ00121
MAEBL; Provisional
 516-881 1.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  516 EFRSVSSRQQSEnddiRRRRNTMDHYLSSRQNSETDDSRgRKRTEPTNVNPDSRSRLMSSRHNSETEDdhrlRRKTESFN 595
Cdd:PTZ00121  1556 ELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELK 1626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  596 NDEKLMKNNGTLRsrrKSNAEYER--EVLNKKTNSNTTRN----RFANSSDSTGEliTTNNNNNSNNKRAESVVREI-KK 668
Cdd:PTZ00121  1627 KAEEEKKKVEQLK---KKEAEEKKkaEELKKAEEENKIKAaeeaKKAEEDKKKAE--EAKKAEEDEKKAAEALKKEAeEA 1701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  669 SPLREVRKSVEREVireptpkesikeptpEKNHKVQPDENIKQDKINEAKSSASQIKKTSQQPAAEE----KTEEDKEWA 744
Cdd:PTZ00121  1702 KKAEELKKKEAEEK---------------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkKIAHLKKEE 1766

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  745 CEHCTFINEAKERVCIVCCKTKRSALPPNPE----NTPESSENVQESTPEPATKVSSIKmsngeesgdSTATTQSKDVEI 820
Cdd:PTZ00121  1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikDIFDNFANIIEGGKEGNLVINDSK---------EMEDSAIKEVAD 1837

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075850389  821 VKNDQELNSNIVEDNQTNKlesvlNSslrENIKTHASISTSTSPIKELEETTSEVIKTQDN 881
Cdd:PTZ00121  1838 SKNMQLEEADAFEKHKFNK-----NN---ENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 456-753 3.91e-03

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 41.90  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  456 SRSSRNLRRGNVSSRRITGYHDVDDNRSTMSRSRRGNWRSEDRINGMNSSSSRNLDYEDLEFRSVSSRQQSENDDIRRR- 534
Cdd:PTZ00112   128 SSISSSLTNISFFSSPTSIYSCLSNSLSSKHSPKVIKENQSTHVNISSDNSPRNKEISNKQLKKQTNVTHTTCYDKMRRs 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  535 -RNTmdhylSSRQNSETDDSRGRKRTEPTNVNPDSRSRLMSSRHNSETEDDHR------LRRKTESFNNDEKLMKNNgtl 607
Cdd:PTZ00112   208 pRNT-----STIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEKSKVQNShfdvriLRSYTKENKKDEKNVVSG--- 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  608 rsrRKSNAEYEREVLNKKTNSNTTRNRF--ANSSDSTGELITTNNNNNSNNKRAESvvreikKSPLREVRKSVEREviRE 685
Cdd:PTZ00112   280 ---IRSSVLLKRKSQCLRKDSYVYSNHQkkAKTGDPKNIIHRNNGSSNSNNDDTSS------SNHLGSNRISNRNP--SS 348

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075850389  686 PTPKES-IKEPTPEKNhkVQPDENIKQDKINEAKSSASQI-KKTSQQPAAEEKTEEDKEWACEHCTFINE 753
Cdd:PTZ00112   349 PYKKQTtTKHTNNTKN--NKYNKTKTTQKFNHPLRHHATInKRSSMLPMSEQKGRGASEKSEYIKEFTME 416
 
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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