NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|554812705|ref|XP_005917193|]
View 

heterogeneous nuclear ribonucleoprotein Ub [Haplochromis burtoni]

Protein Classification

SPRY_hnRNP and AAA_33 domain-containing protein( domain architecture ID 12213148)

protein containing domains SAP, PLN03124, SPRY_hnRNP, and AAA_33

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 210-386 1.80e-105

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: 321.07  E-value: 1.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 210 VCLDSYNSDLHFKVSRDRYSASSLTMESFAYLWSGGKATYGVNKGKACFEMKITEKIPVKHISSKNMEIHDVQVGWSLET 289
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 290 GTLLLGEEEHSYAYSGKAKKTTNCVTEEFGETYEENDVICCLIDFEGEEVVLSYSKNGGEPAVAFQVGKDSLNGRALFPH 369
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*..
gi 554812705 370 VICRNCAVEFNFGQLET 386
Cdd:cd12884  161 VLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 422-565 9.61e-36

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


:

Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 132.05  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  422 IVMVGLPGSGKTTWVNKHIQENPgkYYILGSDTIVEKMMIgsmkRQSKDITKLTAISQRAPLFLGKFIEIAARKKRNYIL 501
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG--AVRLSSDDERKRLFG----EGRPSISYYTDATDRTYERLHELARIALRAGRPVIL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554812705  502 DHTNLSAPGQKRKMCLF--AGFQRKAVVVCPSDEDYKQRVQKKVETDGK--EVPEHALLKMKGFFSLP 565
Cdd:pfam13671  76 DATNLRRDERARLLALAreYGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 3.41e-11

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 58.27  E-value: 3.41e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 554812705     6 VKKLKVNELKDELKKRNLSDKGLKAELMDRLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 210-386 1.80e-105

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: 321.07  E-value: 1.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 210 VCLDSYNSDLHFKVSRDRYSASSLTMESFAYLWSGGKATYGVNKGKACFEMKITEKIPVKHISSKNMEIHDVQVGWSLET 289
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 290 GTLLLGEEEHSYAYSGKAKKTTNCVTEEFGETYEENDVICCLIDFEGEEVVLSYSKNGGEPAVAFQVGKDSLNGRALFPH 369
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*..
gi 554812705 370 VICRNCAVEFNFGQLET 386
Cdd:cd12884  161 VLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 422-565 9.61e-36

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 132.05  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  422 IVMVGLPGSGKTTWVNKHIQENPgkYYILGSDTIVEKMMIgsmkRQSKDITKLTAISQRAPLFLGKFIEIAARKKRNYIL 501
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG--AVRLSSDDERKRLFG----EGRPSISYYTDATDRTYERLHELARIALRAGRPVIL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554812705  502 DHTNLSAPGQKRKMCLF--AGFQRKAVVVCPSDEDYKQRVQKKVETDGK--EVPEHALLKMKGFFSLP 565
Cdd:pfam13671  76 DATNLRRDERARLLALAreYGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 253-384 6.97e-16

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: 74.64  E-value: 6.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705   253 KGKACFEMKITEKipvkhissknmeiHDVQVGWSLE----TGTLLLGEEEHSYAYSG-KAKKTTNCVTEEFGETY-EEND 326
Cdd:smart00449   1 SGRHYFEVEIGDG-------------GHWRVGVATKsvprGYFALLGEDKGSWGYDGdGGKKYHNSTGPEYGLPLqEPGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705   327 VICCLIDFEGEEVvlSYSKNG-GEPAVAFqvgKDSLNGRALFPHVICRN-CAVEFNFGQL 384
Cdd:smart00449  68 VIGCFLDLEAGTI--SFYKNGkYLHGLAF---FDVKFSGPLYPAFSLGSgNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 279-383 4.37e-13

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: 66.60  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  279 HDVQVGWSLE----TGTLLLGEEEHSYAYSG-KAKKTTNCVTEEFGE-TYEENDVICCLIDFEGEEVvlSYSKNGGEPAV 352
Cdd:pfam00622  14 GGWRVGWATKsvprKGERFLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAGTI--SFTKNGKSLGY 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 554812705  353 AFQVGKDSLngrALFPHVICR-NCAVEFNFGQ 383
Cdd:pfam00622  92 AFRDVPFAG---PLFPAVSLGaGEGLKFNFGL 120
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 3.41e-11

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 58.27  E-value: 3.41e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 554812705     6 VKKLKVNELKDELKKRNLSDKGLKAELMDRLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 6-40 1.87e-10

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 56.25  E-value: 1.87e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 554812705    6 VKKLKVNELKDELKKRNLSDKGLKAELMDRLQAAL 40
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
COG4639 COG4639
Predicted kinase [General function prediction only];
419-575 8.32e-09

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 54.84  E-value: 8.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 419 CEIIVMVGLPGSGKTTWVNKHIQEnpgkYYILGSDTIVEKMmigSMKRQSKDITKLT---AISQraplflgkfIEIAARK 495
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFARRLFAP----TEVVSSDDIRALL---GGDENDQSAWGDVfqlAHEI---------ARARLRA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 496 KRNYILDHTNLSApgQKRKMC--LFAGFQR--KAVVVCPSDEDYKQRVQKKvetdGKEVPEHALLKMKGFF-SLPEEGES 570
Cdd:COG4639   66 GRLTVVDATNLQR--EARRRLlaLARAYGAlvVAVVLDVPLEVCLARNAAR----DRQVPEEVIRRMLRRLrRPPLPEEG 139


                 ....*
gi 554812705 571 FNEVI 575
Cdd:COG4639  140 FRVVY 144
pseT PHA02530
polynucleotide kinase; Provisional
 419-558 3.84e-08

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 55.80  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 419 CEIIVMVGLPGSGKTTWVNKHIQENPgKYYILGSDTIvEKMMIGSMKRQ----SKDITKLTAISQRAplflgKFIEIAAR 494
Cdd:PHA02530   2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDL-RQSLFGHGEWGeykfTKEKEDLVTKAQEA-----AALAALKS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554812705 495 KKrNYILDHTNLSaPGQKRKMCLFA---GFQRKAVVVCPSDEDYKQRVQKKVEtdgKEVPEHALLKM 558
Cdd:PHA02530  75 GK-SVIISDTNLN-PERRRKWKELAkelGAEFEEKVFDVPVEELVKRNRKRGE---RAVPEDVLRSM 136
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 417-529 8.01e-05

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 46.17  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  417 ADCEIIVMVGLPGSGKTTWVNKHIQenPGKYYILGSDTivekmmIGSMKRQskditkLTAisqraplflgkfIEIAARKK 496
Cdd:TIGR01663 367 APCEMVIAVGFPGAGKSHFCKKFFQ--PAGYKHVNADT------LGSTQNC------LTA------------CERALDQG 420

                          90       100       110
                  ....*....|....*....|....*....|...
gi 554812705  497 RNYILDHTNLSAPGQKRkmclFAGFQRKAVVVC 529
Cdd:TIGR01663 421 KRCAIDNTNPDAASRAK----FLQCARAAGIPC 449
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 8-65 3.15e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.06  E-value: 3.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 554812705   8 KLKVNELKDELKKRNLSDKGLKAELMDRLQAALDEEALASPQEQAAEADDGFEQAADQ 65
Cdd:PLN03124   4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQ 61
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 210-386 1.80e-105

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: 321.07  E-value: 1.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 210 VCLDSYNSDLHFKVSRDRYSASSLTMESFAYLWSGGKATYGVNKGKACFEMKITEKIPVKHISSKNMEIHDVQVGWSLET 289
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 290 GTLLLGEEEHSYAYSGKAKKTTNCVTEEFGETYEENDVICCLIDFEGEEVVLSYSKNGGEPAVAFQVGKDSLNGRALFPH 369
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*..
gi 554812705 370 VICRNCAVEFNFGQLET 386
Cdd:cd12884  161 VLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 422-565 9.61e-36

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 132.05  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  422 IVMVGLPGSGKTTWVNKHIQENPgkYYILGSDTIVEKMMIgsmkRQSKDITKLTAISQRAPLFLGKFIEIAARKKRNYIL 501
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG--AVRLSSDDERKRLFG----EGRPSISYYTDATDRTYERLHELARIALRAGRPVIL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554812705  502 DHTNLSAPGQKRKMCLF--AGFQRKAVVVCPSDEDYKQRVQKKVETDGK--EVPEHALLKMKGFFSLP 565
Cdd:pfam13671  76 DATNLRRDERARLLALAreYGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 212-383 3.88e-28

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: 110.74  E-value: 3.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 212 LDSYNSDLHFKVSRDRYSASSltMESFAylWSGGKATYGV-NKGKACFEMKITEKipvkhissknmeiHDVQVGWSLETG 290
Cdd:cd12873    1 MNPYDRDAALAISPDGLLCQS--REEKG--WQGCRATKGVkGKGKYYYEVTVTDE-------------GLCRVGWSTEDA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 291 TLLLGEEEHSYAYSGKAKKTTNCVTEEFGETYEENDVICCLIDFEGEEVvlSYSKNGGEPAVAFQVgKDSLNGRALFPHV 370
Cdd:cd12873   64 SLDLGTDKFGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTI--SFSKNGKDLGKAFDI-PPHLRNSALFPAV 140

                        170
                 ....*....|...
gi 554812705 371 ICRNCAVEFNFGQ 383
Cdd:cd12873  141 CLKNAEVEFNFGD 153
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 253-384 6.97e-16

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: 74.64  E-value: 6.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705   253 KGKACFEMKITEKipvkhissknmeiHDVQVGWSLE----TGTLLLGEEEHSYAYSG-KAKKTTNCVTEEFGETY-EEND 326
Cdd:smart00449   1 SGRHYFEVEIGDG-------------GHWRVGVATKsvprGYFALLGEDKGSWGYDGdGGKKYHNSTGPEYGLPLqEPGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705   327 VICCLIDFEGEEVvlSYSKNG-GEPAVAFqvgKDSLNGRALFPHVICRN-CAVEFNFGQL 384
Cdd:smart00449  68 VIGCFLDLEAGTI--SFYKNGkYLHGLAF---FDVKFSGPLYPAFSLGSgNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 279-383 4.37e-13

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: 66.60  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  279 HDVQVGWSLE----TGTLLLGEEEHSYAYSG-KAKKTTNCVTEEFGE-TYEENDVICCLIDFEGEEVvlSYSKNGGEPAV 352
Cdd:pfam00622  14 GGWRVGWATKsvprKGERFLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAGTI--SFTKNGKSLGY 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 554812705  353 AFQVGKDSLngrALFPHVICR-NCAVEFNFGQ 383
Cdd:pfam00622  92 AFRDVPFAG---PLFPAVSLGaGEGLKFNFGL 120
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 254-380 6.49e-13

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: 65.92  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 254 GKACFEMKItekipvkhissKNMEIHDVQVGWSLET----GTLLLGEEEHSYAYSGKAKKT-TNCVTEEFGETYEENDVI 328
Cdd:cd11709    1 GKWYWEVRV-----------DSGNGGLIQVGWATKSfsldGEGGVGDDEESWGYDGSRLRKgHGGSSGPGGRPWKSGDVV 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 554812705 329 CCLIDFegEEVVLSYSKNGGEPAVAFQVGKdsLNGRALFPHV-ICRNCAVEFN 380
Cdd:cd11709   70 GCLLDL--DEGTLSFSLNGKDLGVAFTNLF--LKGGGLYPAVsLGSGQGVTIN 118
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 3.41e-11

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 58.27  E-value: 3.41e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 554812705     6 VKKLKVNELKDELKKRNLSDKGLKAELMDRLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 6-40 1.87e-10

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 56.25  E-value: 1.87e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 554812705    6 VKKLKVNELKDELKKRNLSDKGLKAELMDRLQAAL 40
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 246-382 4.84e-10

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: 58.11  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 246 KATYGVNKGKACFEMkitekipvkHISSKNMeihdVQVGW-------SLETGtllLGEEEHSYAYSGKAKKTTNCVTEEF 318
Cdd:cd12882    3 RANACVYKGKWMYEV---------TLGTKGI----MQIGWatiscrfTQEEG---VGDTRDSYAYDGNRVRKWNVSTQKY 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554812705 319 GETYEENDVICCLIDFEGEEVvlSYSKNGGEPAVAFQvGKDSLNGRALFPHV-ICRNCAVEFNFG 382
Cdd:cd12882   67 GEPWVAGDVIGCCIDLDKGTI--SFYRNGRSLGVAFD-NVRRGPGLAYFPAVsLSFGERLELNFG 128
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 222-389 2.61e-09

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: 56.37  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 222 KVSRDRYSASSLTmesfayLWSGGKATYGVNKGKACFEMKITEkipvkhiSSKNMEIHdVQVGWSLETGTL--LLGEEEH 299
Cdd:cd12872    2 KLSEDRLTVTGEK------GYRMARANHGVREGKWYFEVKILE-------GGGTETGH-VRVGWSRREASLqaPVGYDKY 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 300 SYAY-SGKAKKTTNCVTEEFGE-TYEENDVICCLIDFEgeevVLSYSKNGGEPAVAFqvgKDSLNGRALFPHVIC-RNCA 376
Cdd:cd12872   68 SYAIrDKDGSKFHQSRGKPYGEpGFKEGDVIGFLITLP----KIEFFKNGKSQGVAF---EDIYGTGGYYPAVSLyKGAT 140

                        170
                 ....*....|...
gi 554812705 377 VEFNFGqletPYF 389
Cdd:cd12872  141 VTINFG----PDF 149
COG4639 COG4639
Predicted kinase [General function prediction only];
419-575 8.32e-09

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 54.84  E-value: 8.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 419 CEIIVMVGLPGSGKTTWVNKHIQEnpgkYYILGSDTIVEKMmigSMKRQSKDITKLT---AISQraplflgkfIEIAARK 495
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFARRLFAP----TEVVSSDDIRALL---GGDENDQSAWGDVfqlAHEI---------ARARLRA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 496 KRNYILDHTNLSApgQKRKMC--LFAGFQR--KAVVVCPSDEDYKQRVQKKvetdGKEVPEHALLKMKGFF-SLPEEGES 570
Cdd:COG4639   66 GRLTVVDATNLQR--EARRRLlaLARAYGAlvVAVVLDVPLEVCLARNAAR----DRQVPEEVIRRMLRRLrRPPLPEEG 139


                 ....*
gi 554812705 571 FNEVI 575
Cdd:COG4639  140 FRVVY 144
pseT PHA02530
polynucleotide kinase; Provisional
 419-558 3.84e-08

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 55.80  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 419 CEIIVMVGLPGSGKTTWVNKHIQENPgKYYILGSDTIvEKMMIGSMKRQ----SKDITKLTAISQRAplflgKFIEIAAR 494
Cdd:PHA02530   2 MKIILTVGVPGSGKSTWAREFAAKNP-KAVNVNRDDL-RQSLFGHGEWGeykfTKEKEDLVTKAQEA-----AALAALKS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554812705 495 KKrNYILDHTNLSaPGQKRKMCLFA---GFQRKAVVVCPSDEDYKQRVQKKVEtdgKEVPEHALLKM 558
Cdd:PHA02530  75 GK-SVIISDTNLN-PERRRKWKELAkelGAEFEEKVFDVPVEELVKRNRKRGE---RAVPEDVLRSM 136
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 245-347 5.02e-07

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: 49.61  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 245 GKATYGVNKGKACFEMKItekipvkhISSKNMeihdvQVGWSLETGT--LLLGEEEHSYAYSG-KAKKTTNCvTEEFGET 321
Cdd:cd12878    5 AEKTYAVTSGKWYFEFEV--------LTSGYM-----RVGWARPGFRpdLELGSDDLSYAFDGfLARKWHQG-SESFGKQ 70

                         90       100
                 ....*....|....*....|....*.
gi 554812705 322 YEENDVICCLIDFegEEVVLSYSKNG 347
Cdd:cd12878   71 WQPGDVVGCMLDL--VDRTISFTLNG 94
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 258-382 4.53e-06

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: 46.89  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 258 FEMKITEKIPVKHIS----SKNMEIhDVQVGWsletgtlllgeEEHSYAYSGKAKK--TTNCVTEEFGETYEENDVICCL 331
Cdd:cd12885   18 FEVTILDLGEKGIVSigfcTSGFPL-NRMPGW-----------EDGSYGYHGDDGRvyLGGGEGENYGPPFGTGDVVGCG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 554812705 332 IDFEGEEVvlSYSKNGgepAVAFQVGKDSLNGRaLFP--HVICRNCAVEFNFG 382
Cdd:cd12885   86 INFKTGEV--FFTKNG---ELLGTAFENVVKGR-LYPtvGLGSPGVKVRVNFG 132
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 258-383 4.39e-05

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: 44.05  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 258 FEMKITEKIPVKHISsknmeihdvqVGWSLETGTL--LLGEEEHSYAYSGKAKKTTNCVTE--EFGETYEENDVICCLID 333
Cdd:cd12909   29 FEVKIISKGRDGYIG----------IGFSTKDVNLnrLPGWEPHSWGYHGDDGHSFCSSGTgkPYGPTFTTGDVIGCGIN 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 554812705 334 FegEEVVLSYSKNGGEPAVAFQvgkdSLNGRALFPHVICR--NCAVEFNFGQ 383
Cdd:cd12909   99 F--RDNTAFYTKNGVNLGIAFR----DIKKGNLYPTVGLRtpGEHVEANFGQ 144
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 417-529 8.01e-05

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 46.17  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705  417 ADCEIIVMVGLPGSGKTTWVNKHIQenPGKYYILGSDTivekmmIGSMKRQskditkLTAisqraplflgkfIEIAARKK 496
Cdd:TIGR01663 367 APCEMVIAVGFPGAGKSHFCKKFFQ--PAGYKHVNADT------LGSTQNC------LTA------------CERALDQG 420

                          90       100       110
                  ....*....|....*....|....*....|...
gi 554812705  497 RNYILDHTNLSAPGQKRkmclFAGFQRKAVVVC 529
Cdd:TIGR01663 421 KRCAIDNTNPDAASRAK----FLQCARAAGIPC 449
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
421-575 2.02e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 42.59  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 421 IIVMVGLPGSGKTTwVNKHIQENPGkYYILGSDTIvEKMMIGSMKRQSKDITKLTAISQRAplfLGKFIEIAARKKRNYI 500
Cdd:COG0645    1 LILVCGLPGSGKST-LARALAERLG-AVRLRSDVV-RKRLFGAGLAPLERSPEATARTYAR---LLALARELLAAGRSVI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554812705 501 LDHTNLSApgQKRKMclFAGFQRKA-----VVVCPSDED-YKQRVQK-KVETDGKEVPEHALLKMKGFFSLPEEGESFNE 573
Cdd:COG0645   75 LDATFLRR--AQREA--FRALAEEAgapfvLIWLDAPEEvLRERLEArNAEGGDSDATWEVLERQLAFEEPLTEDEGFLL 150


                 ..
gi 554812705 574 VI 575
Cdd:COG0645  151 VV 152
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 8-65 3.15e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.06  E-value: 3.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 554812705   8 KLKVNELKDELKKRNLSDKGLKAELMDRLQAALDEEALASPQEQAAEADDGFEQAADQ 65
Cdd:PLN03124   4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQ 61
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 320-374 2.52e-03

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: 39.25  E-value: 2.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 554812705 320 ETYEENDVICCLIDFEgeEVVLSYSKNGGEPAVAFqvgkDSLNGRALFPHVICRN 374
Cdd:cd12881  102 SKFHQGDYITVVLDME--EGTLSFGKNGEEPGVAF----EDVDATELYPCVMFYS 150
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH