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Conserved domains on  [gi|24652442|ref|NP_610585|]
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Ran-binding protein M, isoform C [Drosophila melanogaster]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 10191544)

WD40 repeat domain-containing protein similar to topless-related protein that may act as transcription corepressor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 80-222 8.90e-103

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


:

Pssm-ID: 293966  Cd Length: 144  Bit Score: 307.14  E-value: 8.90e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  80 YKGVGKQHSDAASVRTAYPIPSSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSSGNG 159
Cdd:cd12909   1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652442 160 QTYGPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPT-KLYPTVGLQTPGEEVDANFGQ 222
Cdd:cd12909  81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 484-582 6.08e-17

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 76.18  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442    484 IEKILEFGKELSSmgqQLEKENlmtEEERQMLEDAFSLIAYSNP-WSSPLGWLLCPSRRESVSTTLNSAILESL-NFERR 561
Cdd:smart00757   3 IEEALAYARELLA---PFAKEH---EKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSSE 76

                           90       100
                   ....*....|....*....|.
gi 24652442    562 PPLEYLVAHASELIKVIGQHS 582
Cdd:smart00757  77 SPLEILLSAGLAALKTLLEKG 97
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 293-349 1.40e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 45.64  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24652442    293 SIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIE 349
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 258-279 3.42e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


:

Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.99  E-value: 3.42e-03
                          10        20
                  ....*....|....*....|..
gi 24652442   258 LMNRLVSTYLVHNAFSKTAEAF 279
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAF 22
 
Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 80-222 8.90e-103

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 307.14  E-value: 8.90e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  80 YKGVGKQHSDAASVRTAYPIPSSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSSGNG 159
Cdd:cd12909   1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652442 160 QTYGPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPT-KLYPTVGLQTPGEEVDANFGQ 222
Cdd:cd12909  81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 103-223 5.60e-28

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 108.54  E-value: 5.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442    103 CGLYYFEVRIiskGRNGYMGIGLTAQQFR--MNRLPGWDKQSYGYHGDDGNSFSSSgNGQTYGPTFT-TGDVIGCCVNFV 179
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPrgYFALLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLQePGDVIGCFLDLE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 24652442    180 NNTCFYTKNGVDLGI-AFRDLP--TKLYPTVGLQtPGEEVDANFGQE 223
Cdd:smart00449  77 AGTISFYKNGKYLHGlAFFDVKfsGPLYPAFSLG-SGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 106-222 7.35e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 108.20  E-value: 7.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   106 YYFEVRIiSKGRNGYMGIGLTAQQFRM--NRLPGWDKQSYGYHGDDGNSFSSSGNGQTYGPTFTTGDVIGCCVNFVNNTC 183
Cdd:pfam00622   2 HYFEVEI-FGQDGGGWRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24652442   184 FYTKNGVDLGIAFRDLP--TKLYPTVGLQtPGEEVDANFGQ 222
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPfaGPLFPAVSLG-AGEGLKFNFGL 120
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 484-582 6.08e-17

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 76.18  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442    484 IEKILEFGKELSSmgqQLEKENlmtEEERQMLEDAFSLIAYSNP-WSSPLGWLLCPSRRESVSTTLNSAILESL-NFERR 561
Cdd:smart00757   3 IEEALAYARELLA---PFAKEH---EKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSSE 76

                           90       100
                   ....*....|....*....|.
gi 24652442    562 PPLEYLVAHASELIKVIGQHS 582
Cdd:smart00757  77 SPLEILLSAGLAALKTLLEKG 97
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 293-576 1.51e-14

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 71.06  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   293 SIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIEnvnnkvtattqtmptnqtsviqs 372
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKIL----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   373 tktfkhsksgsgngnvninqtqqqnntaipavikpqggdrpdiknmlvddnsnkcvehdsnsmdvemepcqshsnggdss 452
Cdd:pfam10607     --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   453 sngnasavrnsldaideemdvspssrncgrvieKILEFGKElssmgqqlekeNLMTEEERQM--LEDAFSLIAYSNPW-S 529
Cdd:pfam10607  58 ---------------------------------EALEYARE-----------NLAPFNEEHLkeLEKLMGLLAFPDPTdS 93

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 24652442   530 SPLGWLLCPSRRESVSTTLNSAILESLNFERRPPLEYLVAHASELIK 576
Cdd:pfam10607  94 SPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALK 140
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 293-349 1.40e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 45.64  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24652442    293 SIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIE 349
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 258-279 3.42e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.99  E-value: 3.42e-03
                          10        20
                  ....*....|....*....|..
gi 24652442   258 LMNRLVSTYLVHNAFSKTAEAF 279
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAF 22
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 256-279 4.82e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.10  E-value: 4.82e-03
                           10        20
                   ....*....|....*....|....
gi 24652442    256 ENLMNRLVSTYLVHNAFSKTAEAF 279
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETL 26
 
Name Accession Description Interval E-value
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 80-222 8.90e-103

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 307.14  E-value: 8.90e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  80 YKGVGKQHSDAASVRTAYPIPSSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSSGNG 159
Cdd:cd12909   1 YKGPGKTDKDAAAVRANHPIPPQCGIYYFEVKIISKGRDGYIGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652442 160 QTYGPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPT-KLYPTVGLQTPGEEVDANFGQ 222
Cdd:cd12909  81 KPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKgNLYPTVGLRTPGEHVEANFGQ 144
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 91-221 1.41e-54

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 181.32  E-value: 1.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  91 ASVRTAYPIPSSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSSGNGQTYGPTFTTGD 170
Cdd:cd12885   1 GSVRADHPIPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24652442 171 VIGCCVNFVNNTCFYTKNGVDLGIAFRDL-PTKLYPTVGLQTPGEEVDANFG 221
Cdd:cd12885  81 VVGCGINFKTGEVFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
 78-216 4.08e-33

SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes.


Pssm-ID: 293965  Cd Length: 171  Bit Score: 124.72  E-value: 4.08e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  78 VTYKGVGKQhsDAASVRTAYPI-PSSCglyYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSS 156
Cdd:cd12908  14 LEYHGRGIG--DVGLAQARRPLsPDNH---YFEVEIVDPGVRCYIAIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGS 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 157 GNGQTYGPTFTTGDVIGCCVNFVNN-----------------TCFYTKNGVDLGIafRDLPTK---LYPTVGLQTPGEEV 216
Cdd:cd12908  89 GVGDQFGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVFFTRNGKEVGR--TEVPLPpggFYPAVGMHSEGEKV 166
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 103-223 5.60e-28

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 108.54  E-value: 5.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442    103 CGLYYFEVRIiskGRNGYMGIGLTAQQFR--MNRLPGWDKQSYGYHGDDGNSFSSSgNGQTYGPTFT-TGDVIGCCVNFV 179
Cdd:smart00449   1 SGRHYFEVEI---GDGGHWRVGVATKSVPrgYFALLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLQePGDVIGCFLDLE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 24652442    180 NNTCFYTKNGVDLGI-AFRDLP--TKLYPTVGLQtPGEEVDANFGQE 223
Cdd:smart00449  77 AGTISFYKNGKYLHGlAFFDVKfsGPLYPAFSLG-SGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 106-222 7.35e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 108.20  E-value: 7.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   106 YYFEVRIiSKGRNGYMGIGLTAQQFRM--NRLPGWDKQSYGYHGDDGNSFSSSGNGQTYGPTFTTGDVIGCCVNFVNNTC 183
Cdd:pfam00622   2 HYFEVEI-FGQDGGGWRVGWATKSVPRkgERFLGDESGSWGYDGWTGKKYWASTSPLTGLPLFEPGDVIGCFLDYEAGTI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24652442   184 FYTKNGVDLGIAFRDLP--TKLYPTVGLQtPGEEVDANFGQ 222
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPfaGPLFPAVSLG-AGEGLKFNFGL 120
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 92-222 2.67e-24

SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes.


Pssm-ID: 293967  Cd Length: 192  Bit Score: 100.51  E-value: 2.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  92 SVRTAYPIPSSCG-LYYFEVRIISKGR--NGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSF-SSSGNGQTYGPTFT 167
Cdd:cd12910  42 SVQTNLPLPTGRPkTIYFEVKIFELPRadDTSVAIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYiNDPFGGKDFTPPFR 121

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24652442 168 TGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPTK--------------LYPTVGLQTPGEEVDANFGQ 222
Cdd:cd12910 122 EGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEELDaeddgvtglegfhdLYAAIGVFGGECEVHVNPGQ 190
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 104-219 1.87e-20

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 87.10  E-value: 1.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISkGRNGYMGIGLTAQQFRMN--RLPGWDKQSYGYHGD---DGNSFSSSGngqtYGPTFTTGDVIGCCVNF 178
Cdd:cd11709   1 GKWYWEVRVDS-GNGGLIQVGWATKSFSLDgeGGVGDDEESWGYDGSrlrKGHGGSSGP----GGRPWKSGDVVGCLLDL 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24652442 179 VNNTCFYTKNGVDLGIAFRDLPTK---LYPTVGLqTPGEEVDAN 219
Cdd:cd11709  76 DEGTLSFSLNGKDLGVAFTNLFLKgggLYPAVSL-GSGQGVTIN 118
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 104-224 7.43e-19

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 83.78  E-value: 7.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISKG--------RNGYMGIGLtaqqfrmnrlpgwDKQSYGYhGDDGnSFSSSGNGQTYGPTFTTGDVIGCC 175
Cdd:cd12873  40 GKYYYEVTVTDEGlcrvgwstEDASLDLGT-------------DKFGFGY-GGTG-KKSHGRQFDDYGEPFGLGDVIGCY 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24652442 176 VNFVNNTCFYTKNGVDLGIAFrDLPTK-----LYPTVGLQtpGEEVDANFGQEP 224
Cdd:cd12873 105 LDLDNGTISFSKNGKDLGKAF-DIPPHlrnsaLFPAVCLK--NAEVEFNFGDKP 155
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 484-582 6.08e-17

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 76.18  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442    484 IEKILEFGKELSSmgqQLEKENlmtEEERQMLEDAFSLIAYSNP-WSSPLGWLLCPSRRESVSTTLNSAILESL-NFERR 561
Cdd:smart00757   3 IEEALAYARELLA---PFAKEH---EKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSSE 76

                           90       100
                   ....*....|....*....|.
gi 24652442    562 PPLEYLVAHASELIKVIGQHS 582
Cdd:smart00757  77 SPLEILLSAGLAALKTLLEKG 97
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 104-221 2.97e-16

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 75.62  E-value: 2.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISKGRNGYMGIGL-TAQQFRMNRLPGWDKQSYGYHG--DDGNSFSSSGNGQTYGPTFTTGDVIGCCVNFVN 180
Cdd:cd12886   1 GKWYWEVTVVSSAASTYAGIGVaNAAATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATYGAGFTAGDVIGVALDLDA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24652442 181 NTCFYTKNGVDLG---IAFRDLP----TKLYPTVGLQ-TPGEEVDANFG 221
Cdd:cd12886  81 GKIWFYKNGVWQGggdPAPGTNPafagTAMYPAVTGGsSTGGSFTANFG 129
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 71-221 1.22e-15

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 74.48  E-value: 1.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  71 LSQNNLRVT-YKGvgkqHSdaaSVRTAYPIPSscGLYYFEVRIISKGRNGY----MGIGLtaqqfRMNRL--P-GWDKQS 142
Cdd:cd12872   3 LSEDRLTVTgEKG----YR---MARANHGVRE--GKWYFEVKILEGGGTETghvrVGWSR-----REASLqaPvGYDKYS 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 143 YGYHGDDGNSFSSSgNGQTYG-PTFTTGDVIGCCVNFVNNTCFytKNGVDLGIAFRDLPTKL--YPTVGLQTPGeEVDAN 219
Cdd:cd12872  69 YAIRDKDGSKFHQS-RGKPYGePGFKEGDVIGFLITLPKIEFF--KNGKSQGVAFEDIYGTGgyYPAVSLYKGA-TVTIN 144


                ..
gi 24652442 220 FG 221
Cdd:cd12872 145 FG 146
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 91-224 1.24e-15

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 74.93  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  91 ASVRTAYPIPSscGLYYFEVRIISKGRNGYmgIGLTAQQFRMNRLpGW-----------DKQSYGYhgdDGN-SFSSSGN 158
Cdd:cd12884  34 AGARATYGVTK--GKVCFEVKVTENLPVKH--LPTEETDPHVVRV-GWsvdssslqlgeEEFSYGY---GSTgKKSTNCK 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652442 159 GQTYGPTFTTGDVIGCCVNFVNNTC--FYTKNGVDLGIAFR----DLPTK-LYPTVglQTPGEEVDANFGQEP 224
Cdd:cd12884 106 FEDYGEPFGENDVIGCYLDFESEPVeiSFSKNGKDLGVAFKiskeELGGKaLFPHV--LTKNCAVEVNFGQKE 176
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 293-576 1.51e-14

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 71.06  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   293 SIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIEnvnnkvtattqtmptnqtsviqs 372
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKIL----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   373 tktfkhsksgsgngnvninqtqqqnntaipavikpqggdrpdiknmlvddnsnkcvehdsnsmdvemepcqshsnggdss 452
Cdd:pfam10607     --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442   453 sngnasavrnsldaideemdvspssrncgrvieKILEFGKElssmgqqlekeNLMTEEERQM--LEDAFSLIAYSNPW-S 529
Cdd:pfam10607  58 ---------------------------------EALEYARE-----------NLAPFNEEHLkeLEKLMGLLAFPDPTdS 93

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 24652442   530 SPLGWLLCPSRRESVSTTLNSAILESLNFERRPPLEYLVAHASELIK 576
Cdd:pfam10607  94 SPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALK 140
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 104-221 7.18e-14

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 68.51  E-value: 7.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISKGrngYMGIGLT--AQQFRMNRLPGWDKQSYGYhgdDGNSFSS-SGNGQTYGPTFTTGDVIGCCVNFVN 180
Cdd:cd12882  11 GKWMYEVTLGTKG---IMQIGWAtiSCRFTQEEGVGDTRDSYAY---DGNRVRKwNVSTQKYGEPWVAGDVIGCCIDLDK 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24652442 181 NTCFYTKNGVDLGIAFRDLPT----KLYPTVGLQTpGEEVDANFG 221
Cdd:cd12882  85 GTISFYRNGRSLGVAFDNVRRgpglAYFPAVSLSF-GERLELNFG 128
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
 91-221 7.59e-10

SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis.


Pssm-ID: 293970 [Multi-domain]  Cd Length: 150  Bit Score: 57.53  E-value: 7.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  91 ASVRTAYPIPSSCGLYYFEVRIISKGRNG-----YMGIGLTAQQFRMNRLPGWDKQSYGYHgDDGNSFSSSGNGQTYGPT 165
Cdd:cd13735   3 VFVYANSPIPAQAPSFYWEVEVVSLGETDdsdgpIISVGFAPPAEDRDGAWTNPVGTCLFH-NNGRAVHYRGSSLTQWKS 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652442 166 FTT------GDVIGC-----CVNFVNNTCFYTKNGVDLGIAFRDLPTKLYPTVGLQTPGEEVDANFG 221
Cdd:cd13735  82 IRTdvtlsiGDVAGCgwertDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 60-207 1.51e-09

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 57.56  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  60 WSPHDKCLSIGLSQNNLRVTYkgvgkqHSD----AASVRTAYPIPSscGLYYFEVRIISK--GRNGYMGIG-----LTAQ 128
Cdd:cd12876   4 WDERDKSPAVQLSDNNREVYF------HPDyscgTAAVRGTKPLTN--GQHYWEIKMSSPvyGTDMMVGVGtkkadLHAY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 129 QFRMNRLPGWDKQSYGYhgddgnsfSSSG----NGQT--YGPTFTT-GDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPT 201
Cdd:cd12876  76 RYEFCSLLGEDEESWGL--------SYKGllwhDGQSrpYTSPFGNqGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNG 147


                ....*...
gi 24652442 202 --KLYPTV 207
Cdd:cd12876 148 vkPLYPMV 155
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 104-200 2.19e-08

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 53.07  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISkgrNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSssGNGQTYGPTFTTGDVIGCCVNFVNNTC 183
Cdd:cd12878  14 GKWYFEFEVLT---SGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWH--QGSESFGKQWQPGDVVGCMLDLVDRTI 88

                        90       100
                ....*....|....*....|...
gi 24652442 184 FYTKNGV----DLG--IAFRDLP 200
Cdd:cd12878  89 SFTLNGEllidSSGseVAFKDIE 111
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 60-207 7.76e-08

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 52.46  E-value: 7.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  60 WSPHDKCLSIGLSQNNLRVTYKGVgKQHSDAASVRTAYpipsSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNR----- 134
Cdd:cd12875   3 WNPADCSKNIYIKEDGLTFHRRPV-AQSTDAIRGKKGY----TRGLHAWEVKWISRPRGSHAVVGVATKDAPLQCdgyvt 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652442 135 LPGWDKQSYGYHGDDGNSFSSSGNGQTYGP----TFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPTK-LYPTV 207
Cdd:cd12875  78 LLGSNSESWGWDLGDNKLYHNGKKVIGSYPakseNYQVPDRILVILDMEDGTLAFEANGEYLGVAFRGLPGKlLYPAV 155
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 293-349 1.40e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 45.64  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24652442    293 SIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIE 349
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
 60-207 4.29e-06

SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, related to the suppressor of cytokine signaling (SOCS) proteins and located N-terminal to a SPRY (SPla and the ryanodine receptor) domain. Fbxo45 induces the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. F-box motifs are found in proteins that function as the substrate recognition component of SCF E3 complexes.


Pssm-ID: 293964  Cd Length: 175  Bit Score: 47.39  E-value: 4.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442  60 WSPHDKCLSIGLSQNNLRVTYKGVGkQHSDAASVRTAYpipsSCGLYYFEVRIiskgrNGYMG----IGLTAQQFRMN-- 133
Cdd:cd12907   3 WNPNDCSRNIYIKPNGFTLHRNPVA-QSTDGARGKIGF----SSGRHAWEVWW-----EGPLGtvavVGIATKHAPLQcq 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 134 ---RLPGWDKQSYGYHGDDGNSFSSSGNGQTY-----GPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLP-TKLY 204
Cdd:cd12907  73 gyvALLGSDDQSWGWNLVDNHLLHNGDSQGNYpqcnnAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPpTKLY 152


                ...
gi 24652442 205 PTV 207
Cdd:cd12907 153 PAV 155
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 145-216 2.45e-05

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 45.03  E-value: 2.45e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24652442 145 YHGDDGNSFSSSGNGQTYGPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLP-TKLYPTVGL--QTPGEEV 216
Cdd:cd12881  83 YRAYNGNLYHNGEQLLRLSSKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDaTELYPCVMFysSGPGEKV 157
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 104-221 5.61e-05

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 42.72  E-value: 5.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 104 GLYYFEVRIISkgrNGYMGIGLTAQQFRMNRLPGwdkqsYGYhGDDGNSFSSSGNGQTY----------GPTFTTGDVIG 173
Cdd:cd12883   1 GVWYYEVTVLT---SGVMQIGWATKDSKFLNHEG-----YGI-GDDEYSCAYDGCRQLIwynakskphtHPRWKPGDVLG 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24652442 174 CCVNFVNNTCFYTKNGVDLG---IAFRDLPTKLYPTVGLQTpGEEVDANFG 221
Cdd:cd12883  72 CLLDLNKKQMIFSLNGNRLPperQVFTSAKSGFFAAASFMS-FQQCEFNFG 121
SPRY_NHR_like cd12887
SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat ...
 108-209 1.54e-04

SPRY domain in neuralized homology repeat; This family contains the neuralized homology repeat 1 (NHR1) domain similar to the SPRY domain (known to mediate specific protein-protein interactions) at the C-terminus of a conserved region within eukaryotic neuralized and neuralized-like proteins. In Drosophila, the neuralized protein (Neur) belongs to a group of ubiquitin ligases and is required in a subset of Notch pathway-mediated cell fate decisions during development of the nervous system. Neur binds to the Notch receptor ligand Delta through its first NHR1 domain and mediates its ubiquitination for endocytosis. Multiple copies of this region are found in some members of the family.


Pssm-ID: 293945  Cd Length: 161  Bit Score: 42.50  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652442 108 FEVRIISKGRN--GYMGIGLTAQQFRMNRLPgwdkQS-----YGYHGDDGNSFSSSGN--GQTYGPTF---TTGDVIGCC 175
Cdd:cd12887  43 FEVRIDKLVDRwsGSLEIGVTTLNPETLDLP----PSatdlkSGTWILSGSSVFKNGNkiRENYGPDLdrlRVGDRVGVM 118

                        90       100       110
                ....*....|....*....|....*....|....
gi 24652442 176 VNFVNNTCFYTkNGVDLGIAFRDLPTKLYPTVGL 209
Cdd:cd12887 119 RTSDGTLHFYV-NGEDQGVAASNVPQPVYAVVDL 151
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 258-279 3.42e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.99  E-value: 3.42e-03
                          10        20
                  ....*....|....*....|..
gi 24652442   258 LMNRLVSTYLVHNAFSKTAEAF 279
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAF 22
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 256-279 4.82e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.10  E-value: 4.82e-03
                           10        20
                   ....*....|....*....|....
gi 24652442    256 ENLMNRLVSTYLVHNAFSKTAEAF 279
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETL 26
 
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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