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Conserved domains on  [gi|118601081|ref|NP_001073027|]
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heterogeneous nuclear ribonucleoprotein U-like protein 2 [Homo sapiens]

Protein Classification

SPRY_hnRNP and AAA_33 domain-containing protein( domain architecture ID 13917707)

protein containing domains SAP, PRK12678, 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, ...
 246-417 8.59e-101

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: 307.59  E-value: 8.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 246 VNLDTYTSDLHFQVSKDRYGGQPLFSEKFPTLWSGARSTYGVTKGKVCFEAKVTQNLPMK---EGCTEVSLLRVGWSVDF 322
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKhlpTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 323 SRPQLGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVELSFSKNGEDLGVAFWISKDSLADRALLPH 402
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*
gi 118601081 403 VLCKNCVVELNFGQK 417
Cdd:cd12884  161 VLTKNCAVEVNFGQK 175
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 454-599 1.53e-25

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: 102.77  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  454 VILMVGLPGSGKTQWALKYAKENPekrYNVLGAETVLNQMRMKGLEEPEMDPKSRDLLVqqasQCLSKLVQIASRTKRNF 533
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTY----ERLHELARIALRAGRPV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  534 ILDQCNVYNSGQRRKLLLFKT--FSRKVVVVVPNEEDWKKRLELRKEVEGD--DVPESIMLEMKANFSLP 599
Cdd:pfam13671  74 ILDATNLRRDERARLLALAREygVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
3-37 7.86e-09

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 51.72  E-value: 7.86e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 118601081     3 VKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEAL 37
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 6-212 1.30e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081   6 LKVTELR---SELQRRGLdSRGLKVDLAQRLQEALDAEMLEDEAGGGGAGPGGACKAEPRPVAASGGGPGGDEEEDEEEE 82
Cdd:PRK12678  26 MKLPELRalaKQLGIKGT-SGMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  83 EEDEEALLEDEDEEPPPAQAlGQAAQPPPEPPEAAAMEAAAEPDASEKPAEATAGSGGVNGGEEqglgKREEDEPEERSG 162
Cdd:PRK12678 105 APAARAAAAAAAEAASAPEA-AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE----ERDERRRRGDRE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 118601081 163 DETPGSEVPGDKAAEEQGDDQDSEKSKPAGSDGERRGVKRQRDEKDEHGR 212
Cdd:PRK12678 180 DRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGR 229
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 246-417 8.59e-101

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: 307.59  E-value: 8.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 246 VNLDTYTSDLHFQVSKDRYGGQPLFSEKFPTLWSGARSTYGVTKGKVCFEAKVTQNLPMK---EGCTEVSLLRVGWSVDF 322
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKhlpTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 323 SRPQLGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVELSFSKNGEDLGVAFWISKDSLADRALLPH 402
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*
gi 118601081 403 VLCKNCVVELNFGQK 417
Cdd:cd12884  161 VLTKNCAVEVNFGQK 175
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 454-599 1.53e-25

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: 102.77  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  454 VILMVGLPGSGKTQWALKYAKENPekrYNVLGAETVLNQMRMKGLEEPEMDPKSRDLLVqqasQCLSKLVQIASRTKRNF 533
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTY----ERLHELARIALRAGRPV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  534 ILDQCNVYNSGQRRKLLLFKT--FSRKVVVVVPNEEDWKKRLELRKEVEGD--DVPESIMLEMKANFSLP 599
Cdd:pfam13671  74 ILDATNLRRDERARLLALAREygVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 289-416 8.24e-22

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: 91.20  E-value: 8.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081   289 KGKVCFEAKVTQNlpmkegctevSLLRVGWSVDFSRP----QLGEDEFSYGFDGR-GLKAENGQFEEFGQTFGE-NDVIG 362
Cdd:smart00449   1 SGRHYFEVEIGDG----------GHWRVGVATKSVPRgyfaLLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGDVIG 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 118601081   363 CFANFETEEVelSFSKNGEDL-GVAFwisKDSLADRALLPHVLCKN-CVVELNFGQ 416
Cdd:smart00449  71 CFLDLEAGTI--SFYKNGKYLhGLAF---FDVKFSGPLYPAFSLGSgNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 294-416 9.18e-16

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: 73.92  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  294 FEAKVTQNLPmkegctevSLLRVGWS-VDFSRP---QLGEDEFSYGFDG-RGLKAENGQFEEFGQ-TFGENDVIGCFANF 367
Cdd:pfam00622   4 FEVEIFGQDG--------GGWRVGWAtKSVPRKgerFLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDY 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 118601081  368 ETEEVelSFSKNGEDLGVAFwiSKDSLADrALLPHV-LCKNCVVELNFGQ 416
Cdd:pfam00622  76 EAGTI--SFTKNGKSLGYAF--RDVPFAG-PLFPAVsLGAGEGLKFNFGL 120
COG4639 COG4639
Predicted kinase [General function prediction only];
451-592 2.37e-10

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 59.46  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 451 ECEVILMVGLPGSGKTQWALKYAKENPekrynVLGaetvLNQMR-MKGLEEPEMDPKSR--DLLVQQASQCLsklvqias 527
Cdd:COG4639    1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVS----SDDIRaLLGGDENDQSAWGDvfQLAHEIARARL-------- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601081 528 RTKRNFILDQCNVyNSGQRRKLL-LFKTFSRKVVVVV--PNEEDWKKRLELRKEvegdDVPESIMLEM 592
Cdd:COG4639   64 RAGRLTVVDATNL-QREARRRLLaLARAYGALVVAVVldVPLEVCLARNAARDR----QVPEEVIRRM 126
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
3-37 7.86e-09

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 51.72  E-value: 7.86e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 118601081     3 VKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEAL 37
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 ...
 3-37 2.64e-07

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: 47.40  E-value: 2.64e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 118601081    3 VKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEAL 37
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
pseT PHA02530
polynucleotide kinase; Provisional
 451-483 2.68e-04

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 43.47  E-value: 2.68e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 118601081 451 ECEVILMVGLPGSGKTQWALKYAKENPeKRYNV 483
Cdd:PHA02530   1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV 32
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 6-212 1.30e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081   6 LKVTELR---SELQRRGLdSRGLKVDLAQRLQEALDAEMLEDEAGGGGAGPGGACKAEPRPVAASGGGPGGDEEEDEEEE 82
Cdd:PRK12678  26 MKLPELRalaKQLGIKGT-SGMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  83 EEDEEALLEDEDEEPPPAQAlGQAAQPPPEPPEAAAMEAAAEPDASEKPAEATAGSGGVNGGEEqglgKREEDEPEERSG 162
Cdd:PRK12678 105 APAARAAAAAAAEAASAPEA-AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE----ERDERRRRGDRE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 118601081 163 DETPGSEVPGDKAAEEQGDDQDSEKSKPAGSDGERRGVKRQRDEKDEHGR 212
Cdd:PRK12678 180 DRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGR 229
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 5-40 1.57e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 41.75  E-value: 1.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 118601081   5 RLKVTELRSELQRRGLDSRGLKVDLAQRLQEALDAE 40
Cdd:PLN03124   4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAED 39
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 246-417 8.59e-101

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: 307.59  E-value: 8.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 246 VNLDTYTSDLHFQVSKDRYGGQPLFSEKFPTLWSGARSTYGVTKGKVCFEAKVTQNLPMK---EGCTEVSLLRVGWSVDF 322
Cdd:cd12884    1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKhlpTEETDPHVVRVGWSVDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 323 SRPQLGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVELSFSKNGEDLGVAFWISKDSLADRALLPH 402
Cdd:cd12884   81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFESEPVEISFSKNGKDLGVAFKISKEELGGKALFPH 160

                        170
                 ....*....|....*
gi 118601081 403 VLCKNCVVELNFGQK 417
Cdd:cd12884  161 VLTKNCAVEVNFGQK 175
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 248-417 6.03e-39

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: 141.17  E-value: 6.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 248 LDTYTSDLHFQVSKDRYGGQPlfseKFPTLWSGARSTYGVT-KGKVCFEAKVTQnlpmkEGctevsLLRVGWSVDFSRPQ 326
Cdd:cd12873    1 MNPYDRDAALAISPDGLLCQS----REEKGWQGCRATKGVKgKGKYYYEVTVTD-----EG-----LCRVGWSTEDASLD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 327 LGEDEFSYGFDGRGLKAENGQFEEFGQTFGENDVIGCFANFETEEVelSFSKNGEDLGVAFWIsKDSLADRALLPHVLCK 406
Cdd:cd12873   67 LGTDKFGFGYGGTGKKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTI--SFSKNGKDLGKAFDI-PPHLRNSALFPAVCLK 143

                        170
                 ....*....|.
gi 118601081 407 NCVVELNFGQK 417
Cdd:cd12873  144 NAEVEFNFGDK 154
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 454-599 1.53e-25

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: 102.77  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  454 VILMVGLPGSGKTQWALKYAKENPekrYNVLGAETVLNQMRMKGLEEPEMDPKSRDLLVqqasQCLSKLVQIASRTKRNF 533
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEGRPSISYYTDATDRTY----ERLHELARIALRAGRPV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  534 ILDQCNVYNSGQRRKLLLFKT--FSRKVVVVVPNEEDWKKRLELRKEVEGD--DVPESIMLEMKANFSLP 599
Cdd:pfam13671  74 ILDATNLRRDERARLLALAREygVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 289-416 8.24e-22

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: 91.20  E-value: 8.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081   289 KGKVCFEAKVTQNlpmkegctevSLLRVGWSVDFSRP----QLGEDEFSYGFDGR-GLKAENGQFEEFGQTFGE-NDVIG 362
Cdd:smart00449   1 SGRHYFEVEIGDG----------GHWRVGVATKSVPRgyfaLLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGDVIG 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 118601081   363 CFANFETEEVelSFSKNGEDL-GVAFwisKDSLADRALLPHVLCKN-CVVELNFGQ 416
Cdd:smart00449  71 CFLDLEAGTI--SFYKNGKYLhGLAF---FDVKFSGPLYPAFSLGSgNSVRLNFGP 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 290-413 1.43e-18

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: 82.09  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 290 GKVCFEAKVTQNlpmkegctEVSLLRVGWS----VDFSRPQLGEDEFSYGFDG-RGLKAENGQFEEFGQTFGENDVIGCF 364
Cdd:cd11709    1 GKWYWEVRVDSG--------NGGLIQVGWAtksfSLDGEGGVGDDEESWGYDGsRLRKGHGGSSGPGGRPWKSGDVVGCL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 118601081 365 ANFEteEVELSFSKNGEDLGVAFwiSKDSLADRALLPHV-LCKNCVVELN 413
Cdd:cd11709   73 LDLD--EGTLSFSLNGKDLGVAF--TNLFLKGGGLYPAVsLGSGQGVTIN 118
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 278-415 1.59e-17

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: 79.87  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 278 WSGARSTYGVTKGKVCFEAKVTQNLPMKEGCTevsllRVGWSVDFSRPQ--LGEDEFSYGF-DGRGLKAENGQFEEFG-Q 353
Cdd:cd12872   16 YRMARANHGVREGKWYFEVKILEGGGTETGHV-----RVGWSRREASLQapVGYDKYSYAIrDKDGSKFHQSRGKPYGeP 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118601081 354 TFGENDVIGCFANFEteevELSFSKNGEDLGVAFwisKDSLADRALLPHVLC-KNCVVELNFG 415
Cdd:cd12872   91 GFKEGDVIGFLITLP----KIEFFKNGKSQGVAF---EDIYGTGGYYPAVSLyKGATVTINFG 146
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 281-415 7.70e-16

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: 74.64  E-value: 7.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 281 ARSTYGVTKGKVCFEAKVTQNLPMkegctevsllRVGWSVDFSRP--QLGEDEFSYGFDG-RGLKAENGQfEEFGQTFGE 357
Cdd:cd12878    5 AEKTYAVTSGKWYFEFEVLTSGYM----------RVGWARPGFRPdlELGSDDLSYAFDGfLARKWHQGS-ESFGKQWQP 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118601081 358 NDVIGCFANFetEEVELSFSKNGE----DLG--VAFwisKDSLADRALLPHV-LCKNCVVELNFG 415
Cdd:cd12878   74 GDVVGCMLDL--VDRTISFTLNGEllidSSGseVAF---KDIEIGEGFVPACsLGVGQKGRLNLG 133
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 294-416 9.18e-16

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: 73.92  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  294 FEAKVTQNLPmkegctevSLLRVGWS-VDFSRP---QLGEDEFSYGFDG-RGLKAENGQFEEFGQ-TFGENDVIGCFANF 367
Cdd:pfam00622   4 FEVEIFGQDG--------GGWRVGWAtKSVPRKgerFLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDY 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 118601081  368 ETEEVelSFSKNGEDLGVAFwiSKDSLADrALLPHV-LCKNCVVELNFGQ 416
Cdd:pfam00622  76 EAGTI--SFTKNGKSLGYAF--RDVPFAG-PLFPAVsLGAGEGLKFNFGL 120
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 310-415 2.35e-13

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: 67.69  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 310 EVSLLRVGWSVDFS----------RPQLGEDEFSYGF---DGRgLKAENGQFEEFGQTFGENDVIGCFANFETEEVelSF 376
Cdd:cd12885   19 EVTILDLGEKGIVSigfctsgfplNRMPGWEDGSYGYhgdDGR-VYLGGGEGENYGPPFGTGDVVGCGINFKTGEV--FF 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 118601081 377 SKNGEDLGVAFwiskDSLADRALLP--HVLCKNCVVELNFG 415
Cdd:cd12885   96 TKNGELLGTAF----ENVVKGRLYPtvGLGSPGVKVRVNFG 132
COG4639 COG4639
Predicted kinase [General function prediction only];
451-592 2.37e-10

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 59.46  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 451 ECEVILMVGLPGSGKTQWALKYAKENPekrynVLGaetvLNQMR-MKGLEEPEMDPKSR--DLLVQQASQCLsklvqias 527
Cdd:COG4639    1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVS----SDDIRaLLGGDENDQSAWGDvfQLAHEIARARL-------- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601081 528 RTKRNFILDQCNVyNSGQRRKLL-LFKTFSRKVVVVV--PNEEDWKKRLELRKEvegdDVPESIMLEM 592
Cdd:COG4639   64 RAGRLTVVDATNL-QREARRRLLaLARAYGALVVAVVldVPLEVCLARNAARDR----QVPEEVIRRM 126
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 308-416 6.18e-09

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: 55.22  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 308 CT-EVSLLRV-GWsvdfsrpqlgeDEFSYGF---DGRGLKAEN-GQfeEFGQTFGENDVIGCFANFETEEVelSFSKNGE 381
Cdd:cd12909   47 STkDVNLNRLpGW-----------EPHSWGYhgdDGHSFCSSGtGK--PYGPTFTTGDVIGCGINFRDNTA--FYTKNGV 111

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 118601081 382 DLGVAFwiskDSLADRALLPHVLCK--NCVVELNFGQ 416
Cdd:cd12909  112 NLGIAF----RDIKKGNLYPTVGLRtpGEHVEANFGQ 144
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
3-37 7.86e-09

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 51.72  E-value: 7.86e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 118601081     3 VKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEAL 37
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 281-415 6.19e-08

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: 51.94  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 281 ARSTYGVTKGKVCFEAKVtqnlpmkegCTEvSLLRVGW---SVDFSRPQ-LGEDEFSYGFDGRGLKAENGQFEEFGQTFG 356
Cdd:cd12882    2 IRANACVYKGKWMYEVTL---------GTK-GIMQIGWatiSCRFTQEEgVGDTRDSYAYDGNRVRKWNVSTQKYGEPWV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118601081 357 ENDVIGCFANFETEEVElsFSKNGEDLGVAF-WISKdsLADRALLPHV-LCKNCVVELNFG 415
Cdd:cd12882   72 AGDVIGCCIDLDKGTIS--FYRNGRSLGVAFdNVRR--GPGLAYFPAVsLSFGERLELNFG 128
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 3-37 2.64e-07

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: 47.40  E-value: 2.64e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 118601081    3 VKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEAL 37
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 327-387 9.48e-07

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: 49.85  E-value: 9.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118601081 327 LGEDEFSYGFDGRGLKAENGQFEEFGQTFG-ENDVIGCfaNFETEEVELSFSKNGEDLGVAF 387
Cdd:cd12876   83 LGEDEESWGLSYKGLLWHDGQSRPYTSPFGnQGTIIGV--HLDMWRGTLTFYKNGKPLGVAF 142
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
454-596 1.81e-05

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 45.67  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 454 VILMVGLPGSGKTQWALKYAKEnpekrynvLGA-----ETVLNQMRMKGLEE----PEMDPKSRDLLVQQASQCLsklvq 524
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAER--------LGAvrlrsDVVRKRLFGAGLAPlersPEATARTYARLLALARELL----- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118601081 525 iasRTKRNFILDqcNVYNSGQRRKllLFKTFSRK------VVVVVPNEEDWKKRLELRKEVEGD-DVPESIMLEMKANF 596
Cdd:COG0645   68 ---AAGRSVILD--ATFLRRAQRE--AFRALAEEagapfvLIWLDAPEEVLRERLEARNAEGGDsDATWEVLERQLAFE 139
pseT PHA02530
polynucleotide kinase; Provisional
 451-483 2.68e-04

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 43.47  E-value: 2.68e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 118601081 451 ECEVILMVGLPGSGKTQWALKYAKENPeKRYNV 483
Cdd:PHA02530   1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV 32
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 453-603 8.16e-04

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 40.87  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 453 EVILMVGLPGSGKTQWALKYAKEnPEKRYnvlGAETVLNQMRMKGLEEPEMDPKSRdlLVQQASQCLSKLVQIASRTKRN 532
Cdd:COG4088    5 MLLILTGPPGSGKTTFAKALAQR-LYAEG---IAVALLHSDDFRRFLVNESFPKET--YEEVVEDVRTTTADNALDNGYS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118601081 533 FILDQCNVYNSGQR--RKLLLFKTFSRKVVVVVPNEEDWKKRLElrkevEGDDVPESIMLEMKANFSLPEKCD 603
Cdd:COG4088   79 VIVDGTFYYRSWQRdfRNLAKHKAPIHIIYLKAPLETALRRNRE-----RGEPIPERVIARMYRKFDKPGTKD 146
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 6-212 1.30e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081   6 LKVTELR---SELQRRGLdSRGLKVDLAQRLQEALDAEMLEDEAGGGGAGPGGACKAEPRPVAASGGGPGGDEEEDEEEE 82
Cdd:PRK12678  26 MKLPELRalaKQLGIKGT-SGMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081  83 EEDEEALLEDEDEEPPPAQAlGQAAQPPPEPPEAAAMEAAAEPDASEKPAEATAGSGGVNGGEEqglgKREEDEPEERSG 162
Cdd:PRK12678 105 APAARAAAAAAAEAASAPEA-AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE----ERDERRRRGDRE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 118601081 163 DETPGSEVPGDKAAEEQGDDQDSEKSKPAGSDGERRGVKRQRDEKDEHGR 212
Cdd:PRK12678 180 DRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGR 229
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 5-40 1.57e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 41.75  E-value: 1.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 118601081   5 RLKVTELRSELQRRGLDSRGLKVDLAQRLQEALDAE 40
Cdd:PLN03124   4 KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAED 39
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 310-385 2.52e-03

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: 38.48  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601081 310 EVSLL-----RVGWSVDFSRPQ------LGEDEFSYGFDG-RGLKAENGQFEEFG-QTFGENDVIGCFANFETEEVelSF 376
Cdd:cd12883    6 EVTVLtsgvmQIGWATKDSKFLnhegygIGDDEYSCAYDGcRQLIWYNAKSKPHThPRWKPGDVLGCLLDLNKKQM--IF 83


                 ....*....
gi 118601081 377 SKNGEDLGV 385
Cdd:cd12883   84 SLNGNRLPP 92
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
 353-407 7.57e-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: 37.71  E-value: 7.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118601081 353 QTFGENDVIGCfaNFETEEVELSFSKNGEDLGVAFwiskDSLADRALLPHVLCKN 407
Cdd:cd12881  102 SKFHQGDYITV--VLDMEEGTLSFGKNGEEPGVAF----EDVDATELYPCVMFYS 150
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 2-40 7.70e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 39.82  E-value: 7.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 118601081   2 EVKRLKVTELRSELQRRGLDSRGLKVDLAQRLQEALDAE 40
Cdd:PLN03124  78 EVKGMTVRELREAASERGLATTGRKKDLLERLCAALESD 116
 
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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