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Conserved domains on  [gi|1042354685|ref|XP_017321165|]
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heterogeneous nuclear ribonucleoprotein U-like protein 1 [Ictalurus punctatus]

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, ...
 213-390 1.32e-118

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: 354.97  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 213 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARASYGVNKGRVCYEMRITEEISVKHLPSSEPDPHVVRVGWSLDS 292
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 293 CSTQLGEEPFSYGYGGTGKKSSSCKFEDYGQKFGENDVVGCYIDFDSShEVEISFSKNGKWLDVAFRVRKEELSGRALFP 372
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESE-PVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1042354685 373 HILVKNCAVEFNFGQKEE 390
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 426-570 1.86e-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: 117.03  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 426 LMMVGLPACGKTTWAAKHAETNPekkYNILGTNAIMEKMKVMGLRRQRNYAGRWDIliqqATQCLNRLIQIAARKKRNYI 505
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1042354685 506 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKQTDVEGK--DVPDHAVLEMKANFVLP 570
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
5-39 7.29e-11

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 57.50  E-value: 7.29e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1042354685    5 VKRLKVNELKEELQKRGLDIRGLKADLVDRLKAAL 39
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PLN03124 super family cl33640
poly [ADP-ribose] polymerase; Provisional
 7-145 6.14e-07

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03124:

Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 52.92  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685   7 RLKVNELKEELQKRGLDIRGLKADLVDRLKAALDSEAAAQDAQEVTPGDG---QQTEAVAGDEEPGYEDVSHQGRQEDEG 83
Cdd:PLN03124    4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGrkkRRERQDDGDDEPVSPKRIAIDEVKGMT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042354685  84 IQIKDETKVVPDVDHDVNRAEIVEEHLVKPETEMlPVFTEEQNALPGEVKEEDDVKPEQQQD 145
Cdd:PLN03124   84 VRELREAASERGLATTGRKKDLLERLCAALESDV-KVGSANGTGEDEKEKGGDEEREKEEKI 144
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 668-747 2.18e-04

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member PTZ00110:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 545  Bit Score: 44.76  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 668 DNSSRGGY-NRNQSYGGSYNSNHQGSYSkdGYNQSYNqgynqdyNQSNYNQGNYNQGSYNYGNYSQ-YPGYGQGYSDNQA 745
Cdd:PTZ00110    1 MRSTDGSSsNGSVSSGPSNNYNSYGPYP--DSSNPYG-------NYQANHQDNYGGFRPGYGNYSGgYGGFGMNSYGSST 71


                  ..
gi 1042354685 746 SG 747
Cdd:PTZ00110   72 LG 73
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 213-390 1.32e-118

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: 354.97  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 213 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARASYGVNKGRVCYEMRITEEISVKHLPSSEPDPHVVRVGWSLDS 292
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 293 CSTQLGEEPFSYGYGGTGKKSSSCKFEDYGQKFGENDVVGCYIDFDSShEVEISFSKNGKWLDVAFRVRKEELSGRALFP 372
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESE-PVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1042354685 373 HILVKNCAVEFNFGQKEE 390
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 426-570 1.86e-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: 117.03  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 426 LMMVGLPACGKTTWAAKHAETNPekkYNILGTNAIMEKMKVMGLRRQRNYAGRWDIliqqATQCLNRLIQIAARKKRNYI 505
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1042354685 506 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKQTDVEGK--DVPDHAVLEMKANFVLP 570
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 278-387 6.85e-23

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: 94.33  E-value: 6.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 278 EPDPHVVRVGWSLDSCSTQ----LGEEPFSYGYGG-TGKKSSSCKFEDYGQ-KFGENDVVGCYIDFDSShevEISFSKNG 351
Cdd:pfam00622  10 GQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1042354685 352 KWLDVAFrvRKEELSGrALFPHI-LVKNCAVEFNFGQ 387
Cdd:pfam00622  87 KSLGYAF--RDVPFAG-PLFPAVsLGAGEGLKFNFGL 120
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 256-387 7.29e-23

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: 94.28  E-value: 7.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685  256 KGRVCYEMRITeeisvkhlpssepDPHVVRVGWSLDSCS----TQLGEEPFSYGYGGT-GKKSSSCKFEDYGQKFGE-ND 329
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685  330 VVGCYIDFDSShevEISFSKNGKWLD-VAFRVRKeelSGRALFPHILVKN-CAVEFNFGQ 387
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKYLHgLAFFDVK---FSGPLYPAFSLGSgNSVRLNFGP 121
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
5-39 7.29e-11

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 57.50  E-value: 7.29e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1042354685    5 VKRLKVNELKEELQKRGLDIRGLKADLVDRLKAAL 39
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 ...
 5-39 2.00e-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: 2.00e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1042354685   5 VKRLKVNELKEELQKRGLDIRGLKADLVDRLKAAL 39
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
COG4639 COG4639
Predicted kinase [General function prediction only];
423-521 1.70e-07

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 50.98  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 423 CEILMMVGLPACGKTTWAAKHAETNPekkynILGTNAIMEKMKVmGLRRQRNYAGRWDILIQQATQCLnrliqiaaRKKR 502
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFARRLFAPTE-----VVSSDDIRALLGG-DENDQSAWGDVFQLAHEIARARL--------RAGR 67

                          90
                  ....*....|....*....
gi 1042354685 503 NYILDQTNVygsaqRRKMR 521
Cdd:COG4639    68 LTVVDATNL-----QREAR 81
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 7-145 6.14e-07

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 52.92  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685   7 RLKVNELKEELQKRGLDIRGLKADLVDRLKAALDSEAAAQDAQEVTPGDG---QQTEAVAGDEEPGYEDVSHQGRQEDEG 83
Cdd:PLN03124    4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGrkkRRERQDDGDDEPVSPKRIAIDEVKGMT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042354685  84 IQIKDETKVVPDVDHDVNRAEIVEEHLVKPETEMlPVFTEEQNALPGEVKEEDDVKPEQQQD 145
Cdd:PLN03124   84 VRELREAASERGLATTGRKKDLLERLCAALESDV-KVGSANGTGEDEKEKGGDEEREKEEKI 144
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 4-67 2.03e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.83  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1042354685   4 DVKRLKVNELKEELQKRGLDIRGLKADLVDRLKAALDSEAAAQDAQevtpGDGQQTEAVAGDEE 67
Cdd:PLN03124   78 EVKGMTVRELREAASERGLATTGRKKDLLERLCAALESDVKVGSAN----GTGEDEKEKGGDEE 137
PTZ00110 PTZ00110
helicase; Provisional
 668-747 2.18e-04

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 44.76  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 668 DNSSRGGY-NRNQSYGGSYNSNHQGSYSkdGYNQSYNqgynqdyNQSNYNQGNYNQGSYNYGNYSQ-YPGYGQGYSDNQA 745
Cdd:PTZ00110    1 MRSTDGSSsNGSVSSGPSNNYNSYGPYP--DSSNPYG-------NYQANHQDNYGGFRPGYGNYSGgYGGFGMNSYGSST 71


                  ..
gi 1042354685 746 SG 747
Cdd:PTZ00110   72 LG 73
Usher pfam00577
Outer membrane usher protein; In Gram-negative bacteria the biogenesis of fimbriae (or pili) ...
 662-739 1.89e-03

Outer membrane usher protein; In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two- component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher'. The usher protein is rather large (from 86 to 100 Kd) and seems to be mainly composed of membrane-spanning beta-sheets, a structure reminiscent of porins. Although the degree of sequence similarity of these proteins is not very high they share a number of characteriztics. One of these is the presence of two pairs of cysteines, the first one located in the N-terminal part and the second at the C-terminal extremity that are probably involved in disulphide bonds. The best conserved region is located in the central part of these proteins.


Pssm-ID: 425762 [Multi-domain]  Cd Length: 549  Bit Score: 41.52  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 662 WGGNYRDNSSRGGYNRNQSYGGSYNSNHQGSYSKDGYNQSYNQGYNQDYNQSNYNQGNYN------QGSYNYG-NYSQYP 734
Cdd:pfam00577 374 FGRGLSRANSSYSMTRNNSGRTTSNTGVYGTLLDDNLSYSVNAGRASDGRHTGSGNLSYQgsygtvSGSYSYGrDYRQLN 453


                  ....*
gi 1042354685 735 GYGQG 739
Cdd:pfam00577 454 YSVSG 458
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 213-390 1.32e-118

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: 354.97  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 213 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARASYGVNKGRVCYEMRITEEISVKHLPSSEPDPHVVRVGWSLDS 292
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 293 CSTQLGEEPFSYGYGGTGKKSSSCKFEDYGQKFGENDVVGCYIDFDSShEVEISFSKNGKWLDVAFRVRKEELSGRALFP 372
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESE-PVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 1042354685 373 HILVKNCAVEFNFGQKEE 390
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 245-388 5.22e-45

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: 158.51  E-value: 5.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 245 WSGARASYGV-NKGRVCYEMRITEEisvkhlpssepdpHVVRVGWSLDSCSTQLGEEPFSYGYGGTGKKSSSCKFEDYGQ 323
Cdd:cd12873    27 WQGCRATKGVkGKGKYYYEVTVTDE-------------GLCRVGWSTEDASLDLGTDKFGFGYGGTGKKSHGRQFDDYGE 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042354685 324 KFGENDVVGCYIDFDSShevEISFSKNGKWLDVAFRvRKEELSGRALFPHILVKNCAVEFNFGQK 388
Cdd:cd12873    94 PFGLGDVIGCYLDLDNG---TISFSKNGKDLGKAFD-IPPHLRNSALFPAVCLKNAEVEFNFGDK 154
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 426-570 1.86e-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: 117.03  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 426 LMMVGLPACGKTTWAAKHAETNPekkYNILGTNAIMEKMKVMGLRRQRNYAGRWDIliqqATQCLNRLIQIAARKKRNYI 505
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1042354685 506 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKQTDVEGK--DVPDHAVLEMKANFVLP 570
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 278-387 6.85e-23

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: 94.33  E-value: 6.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 278 EPDPHVVRVGWSLDSCSTQ----LGEEPFSYGYGG-TGKKSSSCKFEDYGQ-KFGENDVVGCYIDFDSShevEISFSKNG 351
Cdd:pfam00622  10 GQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1042354685 352 KWLDVAFrvRKEELSGrALFPHI-LVKNCAVEFNFGQ 387
Cdd:pfam00622  87 KSLGYAF--RDVPFAG-PLFPAVsLGAGEGLKFNFGL 120
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 256-387 7.29e-23

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: 94.28  E-value: 7.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685  256 KGRVCYEMRITeeisvkhlpssepDPHVVRVGWSLDSCS----TQLGEEPFSYGYGGT-GKKSSSCKFEDYGQKFGE-ND 329
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685  330 VVGCYIDFDSShevEISFSKNGKWLD-VAFRVRKeelSGRALFPHILVKN-CAVEFNFGQ 387
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKYLHgLAFFDVK---FSGPLYPAFSLGSgNSVRLNFGP 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 245-393 5.25e-21

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: 90.27  E-value: 5.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 245 WSGARASYGVNKGRVCYEMRITEeisvkhlPSSEPDPHvVRVGWSLDSCSTQ--LGEEPFSYGYGG-TGKKSSSCKFEDY 321
Cdd:cd12872    16 YRMARANHGVREGKWYFEVKILE-------GGGTETGH-VRVGWSRREASLQapVGYDKYSYAIRDkDGSKFHQSRGKPY 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042354685 322 GQK-FGENDVVGCYIDFDsshevEISFSKNGKWLDVAFrvrkEELSGR-ALFPHI-LVKNCAVEFNFGqkeePFF 393
Cdd:cd12872    88 GEPgFKEGDVIGFLITLP-----KIEFFKNGKSQGVAF----EDIYGTgGYYPAVsLYKGATVTINFG----PDF 149
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 257-384 7.41e-19

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: 82.86  E-value: 7.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 257 GRVCYEMRITEEISvkhlpssepdpHVVRVGWSLDSCSTQ----LGEEPFSYGYGGTGKKS-SSCKFEDYGQKFGENDVV 331
Cdd:cd11709     1 GKWYWEVRVDSGNG-----------GLIQVGWATKSFSLDgeggVGDDEESWGYDGSRLRKgHGGSSGPGGRPWKSGDVV 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1042354685 332 GCYIDFDsshEVEISFSKNGKWLDVAFRVRKEElsGRALFPHI-LVKNCAVEFN 384
Cdd:cd11709    70 GCLLDLD---EGTLSFSLNGKDLGVAFTNLFLK--GGGLYPAVsLGSGQGVTIN 118
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 268-386 1.17e-15

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: 74.24  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 268 EISVKHLPSSepdpHVVRVGWSLDSCST--QLGEEPFSYGY-GGTGKKSSSCKF-EDYGQKFGENDVVGCYIDFDSShev 343
Cdd:cd12885    19 EVTILDLGEK----GIVSIGFCTSGFPLnrMPGWEDGSYGYhGDDGRVYLGGGEgENYGPPFGTGDVVGCGINFKTG--- 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1042354685 344 EISFSKNGKWLDVAFRVRkeeLSGRaLFP--HILVKNCAVEFNFG 386
Cdd:cd12885    92 EVFFTKNGELLGTAFENV---VKGR-LYPtvGLGSPGVKVRVNFG 132
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 248-386 1.59e-13

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


Pssm-ID: 293940  Cd Length: 128  Bit Score: 68.12  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 248 ARASYGVNKGRVCYEMRIteeisvkhlpSSEPdphVVRVGWSLDSC----STQLGEEPFSYGYGGTGKKSSSCKFEDYGQ 323
Cdd:cd12882     2 IRANACVYKGKWMYEVTL----------GTKG---IMQIGWATISCrftqEEGVGDTRDSYAYDGNRVRKWNVSTQKYGE 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042354685 324 KFGENDVVGCYIDFDSShevEISFSKNGKWLDVAF-RVRKeeLSGRALFPHI-LVKNCAVEFNFG 386
Cdd:cd12882    69 PWVAGDVIGCCIDLDKG---TISFYRNGRSLGVAFdNVRR--GPGLAYFPAVsLSFGERLELNFG 128
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
5-39 7.29e-11

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 57.50  E-value: 7.29e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1042354685    5 VKRLKVNELKEELQKRGLDIRGLKADLVDRLKAAL 39
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 ...
 5-39 2.00e-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: 2.00e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1042354685   5 VKRLKVNELKEELQKRGLDIRGLKADLVDRLKAAL 39
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 254-387 2.55e-10

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: 59.07  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 254 VNKGRVCYeMRI---TEEISVKHLPssepdphvvrvGWsldscstqlgeEPFSYGY----------GGTGKKsssckfed 320
Cdd:cd12909    34 ISKGRDGY-IGIgfsTKDVNLNRLP-----------GW-----------EPHSWGYhgddghsfcsSGTGKP-------- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 321 YGQKFGENDVVGCYIDF-DSSheveISFSKNGKWLDVAFRvrkeELSGRALFPHILVK--NCAVEFNFGQ 387
Cdd:cd12909    83 YGPTFTTGDVIGCGINFrDNT----AFYTKNGVNLGIAFR----DIKKGNLYPTVGLRtpGEHVEANFGQ 144
COG4639 COG4639
Predicted kinase [General function prediction only];
423-521 1.70e-07

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 50.98  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 423 CEILMMVGLPACGKTTWAAKHAETNPekkynILGTNAIMEKMKVmGLRRQRNYAGRWDILIQQATQCLnrliqiaaRKKR 502
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFARRLFAPTE-----VVSSDDIRALLGG-DENDQSAWGDVFQLAHEIARARL--------RAGR 67

                          90
                  ....*....|....*....
gi 1042354685 503 NYILDQTNVygsaqRRKMR 521
Cdd:COG4639    68 LTVVDATNL-----QREAR 81
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 7-145 6.14e-07

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 52.92  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685   7 RLKVNELKEELQKRGLDIRGLKADLVDRLKAALDSEAAAQDAQEVTPGDG---QQTEAVAGDEEPGYEDVSHQGRQEDEG 83
Cdd:PLN03124    4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGrkkRRERQDDGDDEPVSPKRIAIDEVKGMT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042354685  84 IQIKDETKVVPDVDHDVNRAEIVEEHLVKPETEMlPVFTEEQNALPGEVKEEDDVKPEQQQD 145
Cdd:PLN03124   84 VRELREAASERGLATTGRKKDLLERLCAALESDV-KVGSANGTGEDEKEKGGDEEREKEEKI 144
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 248-359 9.00e-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: 48.84  E-value: 9.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 248 ARASYGVNKGRVCYEMRITeeisvkhlpssepDPHVVRVGWSLDSC--STQLGEEPFSYGYGGTGKKSSSCKFEDYGQKF 325
Cdd:cd12878     5 AEKTYAVTSGKWYFEFEVL-------------TSGYMRVGWARPGFrpDLELGSDDLSYAFDGFLARKWHQGSESFGKQW 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1042354685 326 GENDVVGCYIDFDSSHeveISFSKNGKWL------DVAFR 359
Cdd:cd12878    72 QPGDVVGCMLDLVDRT---ISFTLNGELLidssgsEVAFK 108
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 4-67 2.03e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.83  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1042354685   4 DVKRLKVNELKEELQKRGLDIRGLKADLVDRLKAALDSEAAAQDAQevtpGDGQQTEAVAGDEE 67
Cdd:PLN03124   78 EVKGMTVRELREAASERGLATTGRKKDLLERLCAALESDVKVGSAN----GTGEDEKEKGGDEE 137
PTZ00110 PTZ00110
helicase; Provisional
 668-747 2.18e-04

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 44.76  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 668 DNSSRGGY-NRNQSYGGSYNSNHQGSYSkdGYNQSYNqgynqdyNQSNYNQGNYNQGSYNYGNYSQ-YPGYGQGYSDNQA 745
Cdd:PTZ00110    1 MRSTDGSSsNGSVSSGPSNNYNSYGPYP--DSSNPYG-------NYQANHQDNYGGFRPGYGNYSGgYGGFGMNSYGSST 71


                  ..
gi 1042354685 746 SG 747
Cdd:PTZ00110   72 LG 73
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 281-386 3.05e-04

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


Pssm-ID: 293941  Cd Length: 121  Bit Score: 41.18  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 281 PHVVRVGWSLDSCSTQ------LGEEPFSYGYGGTGK------KSSSCKFEdygqKFGENDVVGCYIDFDsshEVEISFS 348
Cdd:cd12883    12 SGVMQIGWATKDSKFLnhegygIGDDEYSCAYDGCRQliwynaKSKPHTHP----RWKPGDVLGCLLDLN---KKQMIFS 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1042354685 349 KNGKWLDVAFRVRKEELSGraLFPHI-LVKNCAVEFNFG 386
Cdd:cd12883    85 LNGNRLPPERQVFTSAKSG--FFAAAsFMSFQQCEFNFG 121
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 297-359 5.49e-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: 5.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1042354685 297 LGEEPFSYGYGGTGKKSSSCKFEDYGQKFG-ENDVVGCYIDFDSSHeveISFSKNGKWLDVAFR 359
Cdd:cd12876    83 LGEDEESWGLSYKGLLWHDGQSRPYTSPFGnQGTIIGVHLDMWRGT---LTFYKNGKPLGVAFT 143
btuB PRK10641
TonB-dependent vitamin B12 receptor BtuB;
637-741 1.22e-03

TonB-dependent vitamin B12 receptor BtuB;


Pssm-ID: 236730 [Multi-domain]  Cd Length: 614  Bit Score: 42.29  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 637 GYQIRGGSGGGYRPGFKRGGY-NQNGWGG---NYRDNSS---RG-GYNRNQSYGGSYNSNHQGSYSKDGYNQSYNQGYNq 708
Cdd:PRK10641  197 GFDVVAYGNTGTQAQPDRDGFmSKTLWGGlehQFNDQWSgfvRGyGYDNRTDYDAYYSPGSPLIDTRQLYSQSWDAGLR- 275

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1042354685 709 dYNQSNYNQ---GNYNQ-GSYNYGnySQYPGYGQGYS 741
Cdd:PRK10641  276 -YNGGIYSSqliASYSHsKDYNYD--PHYGRYDSSAT 309
Usher pfam00577
Outer membrane usher protein; In Gram-negative bacteria the biogenesis of fimbriae (or pili) ...
 662-739 1.89e-03

Outer membrane usher protein; In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two- component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher'. The usher protein is rather large (from 86 to 100 Kd) and seems to be mainly composed of membrane-spanning beta-sheets, a structure reminiscent of porins. Although the degree of sequence similarity of these proteins is not very high they share a number of characteriztics. One of these is the presence of two pairs of cysteines, the first one located in the N-terminal part and the second at the C-terminal extremity that are probably involved in disulphide bonds. The best conserved region is located in the central part of these proteins.


Pssm-ID: 425762 [Multi-domain]  Cd Length: 549  Bit Score: 41.52  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042354685 662 WGGNYRDNSSRGGYNRNQSYGGSYNSNHQGSYSKDGYNQSYNQGYNQDYNQSNYNQGNYN------QGSYNYG-NYSQYP 734
Cdd:pfam00577 374 FGRGLSRANSSYSMTRNNSGRTTSNTGVYGTLLDDNLSYSVNAGRASDGRHTGSGNLSYQgsygtvSGSYSYGrDYRQLN 453


                  ....*
gi 1042354685 735 GYGQG 739
Cdd:pfam00577 454 YSVSG 458
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 320-387 4.81e-03

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: 38.88  E-value: 4.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1042354685 320 DYGQKFGENDVVGCYIDFDSsheVEISFSKNGKWLD--------VAFRVRKEELSGRA-LFPHILVKN--CAVEFNFGQ 387
Cdd:cd12910   115 DFTPPFREGDTIGIGYRFSS---GTIFFTRNGKRLGgwdlgeelDAEDDGVTGLEGFHdLYAAIGVFGgeCEVHVNPGQ 190
 
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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