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Conserved domains on  [gi|13194576|gb|AAK15469|]
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RANBPM [Homo sapiens]

Protein Classification

SPRY_RanBP9_10 and CRA domain-containing protein (domain architecture ID 10191544)

protein containing domains SPRY_RanBP9_10, LisH, CTLH, and CRA

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 ...
1-102 4.93e-75

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: 232.80  E-value: 4.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909  42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                        90       100
                ....*....|....*....|...
gi 13194576  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909 122 KgNLYPTVGLRTPGEHVEANFGQ 144
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
387-479 2.26e-19

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


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 2.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576    387 AIERMIHFGRELQAMSEqlrrdcGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 464
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75
                           90
                   ....*....|....*
gi 13194576    465 QPPLALAMGQATQCL 479
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
174-230 4.78e-14

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


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 66.44  E-value: 4.78e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13194576    174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
135-168 4.69e-05

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: 40.11  E-value: 4.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13194576    135 EWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTV 168
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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 ...
1-102 4.93e-75

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: 232.80  E-value: 4.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909  42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                        90       100
                ....*....|....*....|...
gi 13194576  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909 122 KgNLYPTVGLRTPGEHVEANFGQ 144
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1-102 7.29e-24

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: 96.21  E-value: 7.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576      1 MGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHSFCSSgTGQPYGPTFT-TGDVIGCCVNLINNTCFYTKNGHSLGI-AF 76
Cdd:smart00449  16 WRVGVATKSVPrgYFALLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLQePGDVIGCFLDLEAGTISFYKNGKYLHGlAF 94
                           90       100
                   ....*....|....*....|....*...
gi 13194576     77 TDLPPN--LYPTVGLQtPGEVVDANFGQ 102
Cdd:smart00449  95 FDVKFSgpLYPAFSLG-SGNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown ...
1-102 2.86e-22

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown function. Distant homologs are domains in butyrophilin/marenostrin/pyrin homologs.


Pssm-ID: 334177  Cd Length: 121  Bit Score: 91.62  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576     1 MGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFT 77
Cdd:pfam00622  16 WRVGWATKDYPRkgERFLGDDSGSWGYDGWNGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEEGTISFTKNGKSLGYAFR 94
                          90       100
                  ....*....|....*....|....*..
gi 13194576    78 DLP--PNLYPTVGLQtPGEVVDANFGQ 102
Cdd:pfam00622  95 DVPftGPLFPAVSLG-SGEGLQFNLGL 120
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
387-479 2.26e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 2.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576    387 AIERMIHFGRELQAMSEqlrrdcGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 464
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75
                           90
                   ....*....|....*
gi 13194576    465 QPPLALAMGQATQCL 479
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
174-230 4.78e-14

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 66.44  E-value: 4.78e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13194576    174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CLTH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
174-228 7.19e-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: 337802 [Multi-domain]  Cd Length: 143  Bit Score: 68.35  E-value: 7.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13194576   174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILESILNGDLEEALEWCNENKPELLKINSNLEFELRLQQFIELIREGK 55
CLTH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
388-479 3.06e-12

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: 337802 [Multi-domain]  Cd Length: 143  Bit Score: 63.73  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   388 IERMIHFGRElqamseQLRrdcGKNTANKKMLKDAFSLLAYSDPWN-SPVGNQLDPIQREPVCSALNSAILETHNLPKQP 466
Cdd:pfam10607  56 ILEALEYARE------NLA---PFAKEHLKEIQKLMGLLAFPPPTDsSPYKDLLSPSRWEKLASEFNRAILKLLGLSSES 126
                          90
                  ....*....|...
gi 13194576   467 PLALAMGQATQCL 479
Cdd:pfam10607 127 PLEILLKAGLSAL 139
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
135-168 4.69e-05

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: 40.11  E-value: 4.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13194576    135 EWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTV 168
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerisation. The ...
139-164 3.73e-04

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerisation. 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: 337084  Cd Length: 27  Bit Score: 37.29  E-value: 3.73e-04
                          10        20
                  ....*....|....*....|....*.
gi 13194576   139 MIQKMVSSYLVHHGYCATAEAFARST 164
Cdd:pfam08513   2 ELNRLIYDYLVKSGYKETAEAFEKEA 27
 
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 ...
1-102 4.93e-75

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: 232.80  E-value: 4.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12909  42 IGIGFSTKDVNLNRLPGWEPHSWGYHGDDGHSFCSSGTGKPYGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIK 121
                        90       100
                ....*....|....*....|...
gi 13194576  81 P-NLYPTVGLQTPGEVVDANFGQ 102
Cdd:cd12909 122 KgNLYPTVGLRTPGEHVEANFGQ 144
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
2-101 3.88e-41

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: 143.57  E-value: 3.88e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP 81
Cdd:cd12885  32 SIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGENYGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVK 111
                        90       100
                ....*....|....*....|.
gi 13194576  82 N-LYPTVGLQTPGEVVDANFG 101
Cdd:cd12885 112 GrLYPTVGLGSPGVKVRVNFG 132
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1-102 7.29e-24

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: 96.21  E-value: 7.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576      1 MGIGLSAQGVN--MNRLPGWDKHSYGYHGDDGHSFCSSgTGQPYGPTFT-TGDVIGCCVNLINNTCFYTKNGHSLGI-AF 76
Cdd:smart00449  16 WRVGVATKSVPrgYFALLGEDKGSWGYDGDGGKKYHNS-TGPEYGLPLQePGDVIGCFLDLEAGTISFYKNGKYLHGlAF 94
                           90       100
                   ....*....|....*....|....*...
gi 13194576     77 TDLPPN--LYPTVGLQtPGEVVDANFGQ 102
Cdd:smart00449  95 FDVKFSgpLYPAFSLG-SGNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown ...
1-102 2.86e-22

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor. Domain of unknown function. Distant homologs are domains in butyrophilin/marenostrin/pyrin homologs.


Pssm-ID: 334177  Cd Length: 121  Bit Score: 91.62  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576     1 MGIGLSAQGVNM--NRLPGWDKHSYGYHGDDGHSFCSSgTGQPYG-PTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFT 77
Cdd:pfam00622  16 WRVGWATKDYPRkgERFLGDDSGSWGYDGWNGKKYWAS-TSPLTGlPLFEPGDVIGCFLDYEEGTISFTKNGKSLGYAFR 94
                          90       100
                  ....*....|....*....|....*..
gi 13194576    78 DLP--PNLYPTVGLQtPGEVVDANFGQ 102
Cdd:pfam00622  95 DVPftGPLFPAVSLG-SGEGLQFNLGL 120
SPRYD3 cd12908
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ...
2-96 6.02e-21

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: 89.66  E-value: 6.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINN-----------------TCF 64
Cdd:cd12908  54 AIGLAPQDYPLDRHPGWNPGSVAYHADDGKLFKGSGVGDQFGPRCTKGDRMGCGIRFPRDydtdsedqgdeeegrtvQVF 133
                        90       100       110
                ....*....|....*....|....*....|...
gi 13194576  65 YTKNGHSLGIAFTDLPPN-LYPTVGLQTPGEVV 96
Cdd:cd12908 134 FTRNGKEVGRTEVPLPPGgFYPAVGMHSEGEKV 166
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
387-479 2.26e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 82.73  E-value: 2.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576    387 AIERMIHFGRELQAMSEqlrrdcGKNTANKKMLKDAFSLLAYSDP-WNSPVGNQLDPIQREPVCSALNSAILET-HNLPK 464
Cdd:smart00757   2 KIEEALAYARELLAPFA------KEHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSS 75
                           90
                   ....*....|....*
gi 13194576    465 QPPLALAMGQATQCL 479
Cdd:smart00757  76 ESPLEILLSAGLAAL 90
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
2-102 4.36e-18

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: 82.02  E-value: 4.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   2 GIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCS-SGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP 80
Cdd:cd12910  75 AIGFATKPYPPFRLPGWHRGSLAVHSDDGHRYINdPFGGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGWDLGEE 154
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13194576  81 P--------------NLYPTVGL-QTPGEVVdANFGQ 102
Cdd:cd12910 155 LdaeddgvtglegfhDLYAAIGVfGGECEVH-VNPGQ 190
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
17-105 2.19e-16

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: 76.02  E-value: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576  17 GWDKHSYGYHGDDGHSFcSSGTGQPYG-PTFTTGDVIGCCVNL--INntcFYtKNGHSLGIAFTDLPPNL--YPTVGLQT 91
Cdd:cd12872  63 GYDKYSYAIRDKDGSKF-HQSRGKPYGePGFKEGDVIGFLITLpkIE---FF-KNGKSQGVAFEDIYGTGgyYPAVSLYK 137
                        90
                ....*....|....
gi 13194576  92 PGeVVDANFGQHPF 105
Cdd:cd12872 138 GA-TVTINFGPDFK 150
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
1-99 1.46e-14

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: 69.77  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGLSAQGVNMN--RLPGWDKHSYGYHGDDGHSfCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTD 78
Cdd:cd11709  17 IQVGWATKSFSLDgeGGVGDDEESWGYDGSRLRK-GHGGSSGPGGRPWKSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTN 95
                        90       100
                ....*....|....*....|....
gi 13194576  79 L---PPNLYPTVGLqTPGEVVDAN 99
Cdd:cd11709  96 LflkGGGLYPAVSL-GSGQGVTIN 118
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
174-230 4.78e-14

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 66.44  E-value: 4.78e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13194576    174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSE 230
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
17-104 6.03e-14

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: 69.14  E-value: 6.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576  17 GWDKHSYGYHGDDGHSFCSSGTGqpYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFtDLPPN-----LYPTVGLQT 91
Cdd:cd12873  68 GTDKFGFGYGGTGKKSHGRQFDD--YGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAF-DIPPHlrnsaLFPAVCLKN 144
                        90
                ....*....|...
gi 13194576  92 pGEVVdANFGQHP 104
Cdd:cd12873 145 -AEVE-FNFGDKP 155
CLTH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
174-228 7.19e-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: 337802 [Multi-domain]  Cd Length: 143  Bit Score: 68.35  E-value: 7.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13194576   174 SIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTD 228
Cdd:pfam10607   1 VFKERNRILESILNGDLEEALEWCNENKPELLKINSNLEFELRLQQFIELIREGK 55
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
17-104 8.60e-13

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: 66.46  E-value: 8.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576  17 GWDKHSYGYhGDDGhSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTC--FYTKNGHSLGIAFT----DLPPN-LYPTVgl 89
Cdd:cd12884  86 GEEEFSYGY-GSTG-KKSTNCKFEDYGEPFGENDVIGCYLDFESEPVeiSFSKNGKDLGVAFKiskeELGGKaLFPHV-- 161
                        90
                ....*....|....*
gi 13194576  90 QTPGEVVDANFGQHP 104
Cdd:cd12884 162 LTKNCAVEVNFGQKE 176
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
22-101 1.20e-12

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: 64.66  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576  22 SYGYhgdDGHSFCS-SGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP--PNL--YPTVGLqTPGEVV 96
Cdd:cd12882  48 SYAY---DGNRVRKwNVSTQKYGEPWVAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRrgPGLayFPAVSL-SFGERL 123

                ....*
gi 13194576  97 DANFG 101
Cdd:cd12882 124 ELNFG 128
CLTH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
388-479 3.06e-12

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: 337802 [Multi-domain]  Cd Length: 143  Bit Score: 63.73  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   388 IERMIHFGRElqamseQLRrdcGKNTANKKMLKDAFSLLAYSDPWN-SPVGNQLDPIQREPVCSALNSAILETHNLPKQP 466
Cdd:pfam10607  56 ILEALEYARE------NLA---PFAKEHLKEIQKLMGLLAFPPPTDsSPYKDLLSPSRWEKLASEFNRAILKLLGLSSES 126
                          90
                  ....*....|...
gi 13194576   467 PLALAMGQATQCL 479
Cdd:pfam10607 127 PLEILLKAGLSAL 139
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
1-101 3.67e-08

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: 51.74  E-value: 3.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGL-SAQGVNMNRLPGWDKHSYGYHG--DDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLG---I 74
Cdd:cd12886  18 AGIGVaNAAATGNNGLNGIELSSIGYSLgvYSGNKLSNGSSVATYGAGFTAGDVIGVALDLDAGKIWFYKNGVWQGggdP 97
                        90       100       110
                ....*....|....*....|....*....|..
gi 13194576  75 AFTDLPPNL----YPTVGLQ-TPGEVVDANFG 101
Cdd:cd12886  98 APGTNPAFAgtamYPAVTGGsSTGGSFTANFG 129
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
17-87 4.09e-08

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: 52.93  E-value: 4.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576  17 GWDKHSYGY-------HGddghsfcssGTGQPYGPTFTT-GDVIGCCVNLINNTCFYTKNGHSLGIAFTDLP--PNLYPT 86
Cdd:cd12876  84 GEDEESWGLsykgllwHD---------GQSRPYTSPFGNqGTIIGVHLDMWRGTLTFYKNGKPLGVAFTGLNgvKPLYPM 154

                .
gi 13194576  87 V 87
Cdd:cd12876 155 V 155
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
135-168 4.69e-05

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: 40.11  E-value: 4.69e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13194576    135 EWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTV 168
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
SPRY_Fbox cd12907
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ...
15-87 4.85e-05

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: 43.92  E-value: 4.85e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13194576  15 LPGWDKHSYGYHGDDGHSFCSSGTGQPY-----GPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPP-NLYPTV 87
Cdd:cd12907  77 LLGSDDQSWGWNLVDNHLLHNGDSQGNYpqcnnAPKYQVGERIRVILDCEDNTLAFERGYEFLGVAFRGLPPtKLYPAV 155
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerisation. The ...
139-164 3.73e-04

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerisation. 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: 337084  Cd Length: 27  Bit Score: 37.29  E-value: 3.73e-04
                          10        20
                  ....*....|....*....|....*.
gi 13194576   139 MIQKMVSSYLVHHGYCATAEAFARST 164
Cdd:pfam08513   2 ELNRLIYDYLVKSGYKETAEAFEKEA 27
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
44-93 7.80e-04

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: 40.02  E-value: 7.80e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 13194576  44 PTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPN-LYPTVGLQTPG 93
Cdd:cd12881 102 SKFHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEDVDATeLYPCVMFYSSG 152
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
45-101 1.45e-03

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  Cd Length: 150  Bit Score: 39.04  E-value: 1.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13194576  45 TFTTGDVIGC-----CVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFG 101
Cdd:cd13735  87 TLSIGDVAGCgwertDTPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFG 148
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
1-80 3.85e-03

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: 37.28  E-value: 3.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13194576   1 MGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFcsSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGH----SLG--I 74
Cdd:cd12878  28 MRVGWARPGFRPDLELGSDDLSYAFDGFLARKW--HQGSESFGKQWQPGDVVGCMLDLVDRTISFTLNGEllidSSGseV 105

                ....*.
gi 13194576  75 AFTDLP 80
Cdd:cd12878 106 AFKDIE 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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