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Conserved domains on  [gi|1397715756|ref|XP_025104875|]
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heterogeneous nuclear ribonucleoprotein U-like isoform X2 [Pomacea canaliculata]

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

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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, ...
 239-413 3.82e-104

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: 318.76  E-value: 3.82e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 239 LDRYNCDLNLRIQDDGLKACPLTVEGFAFMWAGARSMYGVRSGKVAYEAKLLENLNVDHLPKDETNPHVLRVGWSVDDTS 318
Cdd:cd12884     3 LDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDSSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 319 LQLGEEPLSYGYGGTGKASTDCKFTDFGQTFTAGDIITAYLDMDSDPVTMSYSKNGEDLGVCFEVEKEKLEDKALFPHLL 398
Cdd:cd12884    83 LQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPHVL 162

                         170
                  ....*....|....*
gi 1397715756 399 TKNTEFECNFGQREE 413
Cdd:cd12884   163 TKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 449-593 5.40e-30

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: 115.87  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 449 IMMVGLPGAGKTYWAEKHAGANKekrYFVLGTNNIIDKMKVMGLPRKKNYSGRWDVLIDkatkCLNRMIEIAARKKRNYI 528
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTYE----RLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397715756 529 LDQTNVYASARRRKMQPFE--GFQRKAVVVVPTDEEFKVRVE--KREKEEGKEIPEKAVLEMKANFSLP 593
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAarARAGGDPSDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
7-40 2.98e-12

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 61.35  E-value: 2.98e-12
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1397715756    7 DKLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:smart00513   2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 239-413 3.82e-104

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: 318.76  E-value: 3.82e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 239 LDRYNCDLNLRIQDDGLKACPLTVEGFAFMWAGARSMYGVRSGKVAYEAKLLENLNVDHLPKDETNPHVLRVGWSVDDTS 318
Cdd:cd12884     3 LDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDSSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 319 LQLGEEPLSYGYGGTGKASTDCKFTDFGQTFTAGDIITAYLDMDSDPVTMSYSKNGEDLGVCFEVEKEKLEDKALFPHLL 398
Cdd:cd12884    83 LQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPHVL 162

                         170
                  ....*....|....*
gi 1397715756 399 TKNTEFECNFGQREE 413
Cdd:cd12884   163 TKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 449-593 5.40e-30

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: 115.87  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 449 IMMVGLPGAGKTYWAEKHAGANKekrYFVLGTNNIIDKMKVMGLPRKKNYSGRWDVLIDkatkCLNRMIEIAARKKRNYI 528
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTYE----RLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397715756 529 LDQTNVYASARRRKMQPFE--GFQRKAVVVVPTDEEFKVRVE--KREKEEGKEIPEKAVLEMKANFSLP 593
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAarARAGGDPSDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
7-40 2.98e-12

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 61.35  E-value: 2.98e-12
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1397715756    7 DKLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:smart00513   2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 8-40 4.68e-12

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: 60.88  E-value: 4.68e-12
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1397715756   8 KLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:pfam02037   3 KLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 301-411 1.84e-10

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: 58.89  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 301 DETNPHVLRVGWSVDDTSLQ----LGEEPLSYGYGG-TGKASTDCKFTDFGQ-TFTAGDIITAYLDMDSDpvTMSYSKNG 374
Cdd:pfam00622   9 FGQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG--TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1397715756 375 EDLGVCFEVEKeklEDKALFPH-LLTKNTEFECNFGQR 411
Cdd:pfam00622  87 KSLGYAFRDVP---FAGPLFPAvSLGAGEGLKFNFGLR 121
COG4639 COG4639
Predicted kinase [General function prediction only];
446-541 1.68e-07

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 51.37  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 446 CEIIMMVGLPGAGKTYWAEKHAgankeKRYFVLGTNNIIDKMKvmGLPRKKNYSGR-WDVLIDKATKCLnrmieiaaRKK 524
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFARRLF-----APTEVVSSDDIRALLG--GDENDQSAWGDvFQLAHEIARARL--------RAG 66

                          90
                  ....*....|....*..
gi 1397715756 525 RNYILDQTNVYASARRR 541
Cdd:COG4639    67 RLTVVDATNLQREARRR 83
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 8-40 7.99e-05

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 46.37  E-value: 7.99e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1397715756   8 KLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:PLN03124    4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAI 36
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 239-413 3.82e-104

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: 318.76  E-value: 3.82e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 239 LDRYNCDLNLRIQDDGLKACPLTVEGFAFMWAGARSMYGVRSGKVAYEAKLLENLNVDHLPKDETNPHVLRVGWSVDDTS 318
Cdd:cd12884     3 LDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDSSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 319 LQLGEEPLSYGYGGTGKASTDCKFTDFGQTFTAGDIITAYLDMDSDPVTMSYSKNGEDLGVCFEVEKEKLEDKALFPHLL 398
Cdd:cd12884    83 LQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPHVL 162

                         170
                  ....*....|....*
gi 1397715756 399 TKNTEFECNFGQREE 413
Cdd:cd12884   163 TKNCAVEVNFGQKEE 177
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 239-410 5.73e-36

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: 133.08  E-value: 5.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 239 LDRYNCDLNLRIQDDGLKACPLTvegfAFMWAGARSMYGVR-SGKVAYEAKLLEnlnvdhlpkdetnPHVLRVGWSVDDT 317
Cdd:cd12873     1 MNPYDRDAALAISPDGLLCQSRE----EKGWQGCRATKGVKgKGKYYYEVTVTD-------------EGLCRVGWSTEDA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 318 SLQLGEEPLSYGYGGTGKASTDCKFTDFGQTFTAGDIITAYLDMDSDpvTMSYSKNGEDLGVCFEVEKeKLEDKALFPHL 397
Cdd:cd12873    64 SLDLGTDKFGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLDLDNG--TISFSKNGKDLGKAFDIPP-HLRNSALFPAV 140

                         170
                  ....*....|...
gi 1397715756 398 LTKNTEFECNFGQ 410
Cdd:cd12873   141 CLKNAEVEFNFGD 153
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 449-593 5.40e-30

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: 115.87  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 449 IMMVGLPGAGKTYWAEKHAGANKekrYFVLGTNNIIDKMKVMGLPRKKNYSGRWDVLIDkatkCLNRMIEIAARKKRNYI 528
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTYE----RLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397715756 529 LDQTNVYASARRRKMQPFE--GFQRKAVVVVPTDEEFKVRVE--KREKEEGKEIPEKAVLEMKANFSLP 593
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAarARAGGDPSDVPEEVLDRQKARFEPP 143
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 281-395 8.38e-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: 68.61  E-value: 8.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 281 GKVAYEAKLlenlnvdhlpkDETNPHVLRVGWSVDDTSLQ----LGEEPLSYGYGGTGKAS-TDCKFTDFGQTFTAGDII 355
Cdd:cd11709     1 GKWYWEVRV-----------DSGNGGLIQVGWATKSFSLDgeggVGDDEESWGYDGSRLRKgHGGSSGPGGRPWKSGDVV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1397715756 356 TAYLDMDSdpVTMSYSKNGEDLGVCFEVEKEKleDKALFP 395
Cdd:cd11709    70 GCLLDLDE--GTLSFSLNGKDLGVAFTNLFLK--GGGLYP 105
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
7-40 2.98e-12

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 61.35  E-value: 2.98e-12
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1397715756    7 DKLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:smart00513   2 AKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 8-40 4.68e-12

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: 60.88  E-value: 4.68e-12
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1397715756   8 KLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:pfam02037   3 KLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 301-411 1.84e-10

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: 58.89  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 301 DETNPHVLRVGWSVDDTSLQ----LGEEPLSYGYGG-TGKASTDCKFTDFGQ-TFTAGDIITAYLDMDSDpvTMSYSKNG 374
Cdd:pfam00622   9 FGQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG--TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1397715756 375 EDLGVCFEVEKeklEDKALFPH-LLTKNTEFECNFGQR 411
Cdd:pfam00622  87 KSLGYAFRDVP---FAGPLFPAvSLGAGEGLKFNFGLR 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 269-382 1.14e-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: 57.53  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 269 WAGARSMYGVRSGKVAYEAKllenlnVDHLPKDETnPHVlRVGWSVDDTSLQ--LGEEPLSYGYGG-TGKASTDCKFTDF 345
Cdd:cd12872    16 YRMARANHGVREGKWYFEVK------ILEGGGTET-GHV-RVGWSRREASLQapVGYDKYSYAIRDkDGSKFHQSRGKPY 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1397715756 346 G-QTFTAGDIITAYLDMDSdpvtMSYSKNGEDLGVCFE 382
Cdd:cd12872    88 GePGFKEGDVIGFLITLPK----IEFFKNGKSQGVAFE 121
COG4639 COG4639
Predicted kinase [General function prediction only];
446-541 1.68e-07

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 51.37  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 446 CEIIMMVGLPGAGKTYWAEKHAgankeKRYFVLGTNNIIDKMKvmGLPRKKNYSGR-WDVLIDKATKCLnrmieiaaRKK 524
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFARRLF-----APTEVVSSDDIRALLG--GDENDQSAWGDvFQLAHEIARARL--------RAG 66

                          90
                  ....*....|....*..
gi 1397715756 525 RNYILDQTNVYASARRR 541
Cdd:COG4639    67 RLTVVDATNLQREARRR 83
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 322-410 5.62e-07

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: 49.83  E-value: 5.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 322 GEEPLSYGY----------GGTGKAstdckftdFGQTFTAGDIITAYLDMdsdpVTMS--YSKNGEDLGVCFevekEKLE 389
Cdd:cd12909    58 GWEPHSWGYhgddghsfcsSGTGKP--------YGPTFTTGDVIGCGINF----RDNTafYTKNGVNLGIAF----RDIK 121

                          90       100
                  ....*....|....*....|...
gi 1397715756 390 DKALFPH--LLTKNTEFECNFGQ 410
Cdd:cd12909   122 KGNLYPTvgLRTPGEHVEANFGQ 144
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
 243-395 1.41e-06

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: 48.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 243 NCDLNLRIQDDGLKACPLTVegfAFMWAGARSMYGVRSGKVAYEAKLlenlnvdhlPKDETNPHVLrVGWSVDDTSLQ-- 320
Cdd:cd12875     7 DCSKNIYIKEDGLTFHRRPV---AQSTDAIRGKKGYTRGLHAWEVKW---------ISRPRGSHAV-VGVATKDAPLQcd 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 321 -----LGEEPLSYGYG-GTGKASTDCK-----FTDFGQTFTAGDIITAYLDMDSDpvTMSYSKNGEDLGVCFevekEKLE 389
Cdd:cd12875    74 gyvtlLGSNSESWGWDlGDNKLYHNGKkvigsYPAKSENYQVPDRILVILDMEDG--TLAFEANGEYLGVAF----RGLP 147


                  ....*.
gi 1397715756 390 DKALFP 395
Cdd:cd12875   148 GKLLYP 153
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 300-409 1.73e-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: 48.04  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 300 KDETNPHVLRVGWSVDDTSL--QLGEEPLSYGY-GGTGKASTDCKF-TDFGQTFTAGDIITAYLDMDSDpvTMSYSKNGE 375
Cdd:cd12885    23 LDLGEKGIVSIGFCTSGFPLnrMPGWEDGSYGYhGDDGRVYLGGGEgENYGPPFGTGDVVGCGINFKTG--EVFFTKNGE 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1397715756 376 DLGVCFE-VEKEKledkaLFP--HLLTKNTEFECNFG 409
Cdd:cd12885   101 LLGTAFEnVVKGR-----LYPtvGLGSPGVKVRVNFG 132
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 322-409 2.27e-06

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: 47.71  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 322 GEEPLSYGYGGTGKASTDCKFTDFGQTFTAGDIITAYLDMDSDpvTMSYSKNGEDLGVCFEvEKEKLEDKALFPHL-LTK 400
Cdd:cd12882    43 GDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKG--TISFYRNGRSLGVAFD-NVRRGPGLAYFPAVsLSF 119


                  ....*....
gi 1397715756 401 NTEFECNFG 409
Cdd:cd12882   120 GERLELNFG 128
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 272-375 1.28e-05

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: 45.37  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 272 ARSMYGVRSGKVAYEAKLLenlnvdhlpkdetNPHVLRVGWSVDDT--SLQLGEEPLSYGYGGTGKASTDCKFTDFGQTF 349
Cdd:cd12878     5 AEKTYAVTSGKWYFEFEVL-------------TSGYMRVGWARPGFrpDLELGSDDLSYAFDGFLARKWHQGSESFGKQW 71

                          90       100
                  ....*....|....*....|....*.
gi 1397715756 350 TAGDIITAYLDMDSDpvTMSYSKNGE 375
Cdd:cd12878    72 QPGDVVGCMLDLVDR--TISFTLNGE 95
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 347-382 4.24e-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: 44.65  E-value: 4.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1397715756 347 QTFTAGDIITAYLDMDSDpvTMSYSKNGEDLGVCFE 382
Cdd:cd12881   102 SKFHQGDYITVVLDMEEG--TLSFGKNGEEPGVAFE 135
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 8-40 7.99e-05

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 46.37  E-value: 7.99e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1397715756   8 KLKVTELRDELKARGLDTKGVKAVLVERLKQAL 40
Cdd:PLN03124    4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAI 36
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 321-382 6.22e-04

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: 41.76  E-value: 6.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397715756 321 LGEEPLSYGYGGTGKASTDCKFTDFGQTF-TAGDIITAYLDMDSDpvTMSYSKNGEDLGVCFE 382
Cdd:cd12876    83 LGEDEESWGLSYKGLLWHDGQSRPYTSPFgNQGTIIGVHLDMWRG--TLTFYKNGKPLGVAFT 143
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 327-409 1.55e-03

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: 39.41  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397715756 327 SYGYGGT----GKASTDCKFTDFGQTFTAGDIITAYLDMDSDpvTMSYSKNGE--DLGVCFEVEKEKLEDKALFPHLLTK 400
Cdd:cd12886    40 SIGYSLGvysgNKLSNGSSVATYGAGFTAGDVIGVALDLDAG--KIWFYKNGVwqGGGDPAPGTNPAFAGTAMYPAVTGG 117

                          90
                  ....*....|..
gi 1397715756 401 NT---EFECNFG 409
Cdd:cd12886   118 SStggSFTANFG 129
 
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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