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Conserved domains on  [gi|2031939749|ref|XP_041090503|]
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heterogeneous nuclear ribonucleoprotein U-like protein 1 isoform X1 [Polyodon spathula]

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, ...
 217-394 1.26e-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: 355.36  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 217 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARVSYGVSKGKVCFEMKINEEISVKHLPSSEPDPHVVRVGWSLDS 296
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 297 CSTQLGEEEFSYGYGGTGKKSTNCKFEDFGEKFRENDVIGCFIDFEaGEEVEMAYSKNGEWLGVGFRVSKEELADRALFP 376
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 2031939749 377 HVLVKNCAIEFNFGQKEE 394
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 ...
 430-574 6.92e-34

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: 126.66  E-value: 6.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 430 LMMVGLPASGKTTWAEKHAAENPTkkfNILGTNAIMEKMKVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 509
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGA---VRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031939749 510 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKRTDEEGK--DVPDHAVLEMKANFALP 574
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 2.57e-08

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 50.18  E-value: 2.57e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2031939749    6 VRKLKVHELKEELQARGLEARGLKADLAERLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PLN03124 super family cl33640
poly [ADP-ribose] polymerase; Provisional
 1-113 3.68e-04

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03124:

Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.06  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749   1 MSAvdvrKLKVHELKEELQARGLEARGLKADLAERLQAALDSEALGVAVAAPPPPPGVVLGEGYAGEGDAE---DDEKEQ 77
Cdd:PLN03124    1 MAN----KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQDDGDDEpvsPKRIAI 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2031939749  78 DQVLGMEAGDSLAdqdqgfsELSADGLDDTSVKEEI 113
Cdd:PLN03124   77 DEVKGMTVRELRE-------AASERGLATTGRKKDL 105
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 217-394 1.26e-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: 355.36  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 217 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARVSYGVSKGKVCFEMKINEEISVKHLPSSEPDPHVVRVGWSLDS 296
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 297 CSTQLGEEEFSYGYGGTGKKSTNCKFEDFGEKFRENDVIGCFIDFEaGEEVEMAYSKNGEWLGVGFRVSKEELADRALFP 376
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 2031939749 377 HVLVKNCAIEFNFGQKEE 394
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 ...
 430-574 6.92e-34

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: 126.66  E-value: 6.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 430 LMMVGLPASGKTTWAEKHAAENPTkkfNILGTNAIMEKMKVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 509
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGA---VRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031939749 510 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKRTDEEGK--DVPDHAVLEMKANFALP 574
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 260-391 2.51e-24

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 98.52  E-value: 2.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749  260 KGKVCFEMKINeeisvkhlpssepDPHVVRVGWSLDSCS----TQLGEEEFSYGYGGT-GKKSTNCKFEDFGEKFRE-ND 333
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749  334 VIGCFIDFEAGeevEMAYSKNGEWL-GVGFRVSKeelADRALFPHVLVKN-CAIEFNFGQ 391
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKYLhGLAFFDVK---FSGPLYPAFSLGSgNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 282-391 5.12e-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: 94.72  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 282 EPDPHVVRVGWSLDSCSTQ----LGEEEFSYGYGG-TGKKSTNCKFEDFGE-KFRENDVIGCFIDFEAGeevEMAYSKNG 355
Cdd:pfam00622  10 GQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2031939749 356 EWLGVGFRVSKeelADRALFPHV-LVKNCAIEFNFGQ 391
Cdd:pfam00622  87 KSLGYAFRDVP---FAGPLFPAVsLGAGEGLKFNFGL 120
COG4639 COG4639
Predicted kinase [General function prediction only];
426-583 1.52e-10

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 59.84  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 426 ECEILMMVGLPASGKTTWAEKHAAENPtkkfnILGTNAIMEKMKVmGLRRQRNYAGRWDVLIQQATQCLnrliqiaaRKK 505
Cdd:COG4639     1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVSSDDIRALLGG-DENDQSAWGDVFQLAHEIARARL--------RAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 506 RNYILDQTNVygsaQRRKMRPFEGFQRK------AIVICPTDEDLKERTLKRTdeegKDVPDHAVLEMKANF-ALPECGE 578
Cdd:COG4639    67 RLTVVDATNL----QREARRRLLALARAygalvvAVVLDVPLEVCLARNAARD----RQVPEEVIRRMLRRLrRPPLPEE 138


                  ....*
gi 2031939749 579 VLDSV 583
Cdd:COG4639   139 GFRVV 143
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 2.57e-08

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 50.18  E-value: 2.57e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2031939749    6 VRKLKVHELKEELQARGLEARGLKADLAERLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 8-40 7.55e-08

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: 48.94  E-value: 7.55e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2031939749   8 KLKVHELKEELQARGLEARGLKADLAERLQAAL 40
Cdd:pfam02037   3 KLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
pseT PHA02530
polynucleotide kinase; Provisional
 426-576 5.38e-05

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 45.78  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 426 ECEILMMVGLPASGKTTWAEKHAAENPtKKFNIlgtNAIMEKMKVMGLRRQRNYAGRWDVliQQATQCLNRLIQIAA-RK 504
Cdd:PHA02530    1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV---NRDDLRQSLFGHGEWGEYKFTKEK--EDLVTKAQEAAALAAlKS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 505 KRNYILDQTNVyGSAQRRKMRPF---EGFQRKAIVICPTDEDLKERTLKRTDeegKDVPDHAVLEM-------------- 567
Cdd:PHA02530   75 GKSVIISDTNL-NPERRRKWKELakeLGAEFEEKVFDVPVEELVKRNRKRGE---RAVPEDVLRSMfkqmkeyrglvwpv 150

                         170
                  ....*....|
gi 2031939749 568 -KANFALPEC 576
Cdd:PHA02530  151 yTADPGLPKA 160
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 1-113 3.68e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.06  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749   1 MSAvdvrKLKVHELKEELQARGLEARGLKADLAERLQAALDSEALGVAVAAPPPPPGVVLGEGYAGEGDAE---DDEKEQ 77
Cdd:PLN03124    1 MAN----KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQDDGDDEpvsPKRIAI 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2031939749  78 DQVLGMEAGDSLAdqdqgfsELSADGLDDTSVKEEI 113
Cdd:PLN03124   77 DEVKGMTVRELRE-------AASERGLATTGRKKDL 105
dnaE PRK06826
DNA polymerase III DnaE; Reviewed
 365-404 3.83e-03

DNA polymerase III DnaE; Reviewed


Pssm-ID: 235868 [Multi-domain]  Cd Length: 1151  Bit Score: 41.03  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2031939749  365 SKEELADraLFPHVL--VKN-------CAIEFNFGQKEEPYFPVPEGYT 404
Cdd:PRK06826   248 SPEEMYE--LFSYVPeaLENtvkiaerCNVEFEFGKSKLPKFPLPEGYD 294
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 421-487 5.28e-03

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 38.53  E-value: 5.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031939749 421 PASKAECEILMMvGLPASGKTTWAEKHAAEN-----PTKKFNILGTNAIMEKMKV--MGLRRQ-----RNYAGRWDVLI 487
Cdd:cd04155    10 PSSRQEVRILLL-GLDNAGKTTILKQLASEDishitPTQGFNIKNVQADGFKLNVwdIGGQRKirpywRNYFENTDVLI 87
 
Name Accession Description Interval E-value
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 217-394 1.26e-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: 355.36  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 217 VAIDTYNCDLHFKVARDRYSGYPLTIEGFAYLWSGARVSYGVSKGKVCFEMKINEEISVKHLPSSEPDPHVVRVGWSLDS 296
Cdd:cd12884     1 VCLDTYNSDLHLKISKDRYSASPLTDEGFAYLWAGARATYGVTKGKVCFEVKVTENLPVKHLPTEETDPHVVRVGWSVDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 297 CSTQLGEEEFSYGYGGTGKKSTNCKFEDFGEKFRENDVIGCFIDFEaGEEVEMAYSKNGEWLGVGFRVSKEELADRALFP 376
Cdd:cd12884    81 SSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEPFGENDVIGCYLDFE-SEPVEISFSKNGKDLGVAFKISKEELGGKALFP 159

                         170
                  ....*....|....*...
gi 2031939749 377 HVLVKNCAIEFNFGQKEE 394
Cdd:cd12884   160 HVLTKNCAVEVNFGQKEE 177
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 249-392 3.13e-42

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: 150.80  E-value: 3.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 249 WSGARVSYGVS-KGKVCFEMKINEEisvkhlpssepdpHVVRVGWSLDSCSTQLGEEEFSYGYGGTGKKSTNCKFEDFGE 327
Cdd:cd12873    27 WQGCRATKGVKgKGKYYYEVTVTDE-------------GLCRVGWSTEDASLDLGTDKFGFGYGGTGKKSHGRQFDDYGE 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2031939749 328 KFRENDVIGCFIDFEAGeevEMAYSKNGEWLGVGFRVsKEELADRALFPHVLVKNCAIEFNFGQK 392
Cdd:cd12873    94 PFGLGDVIGCYLDLDNG---TISFSKNGKDLGKAFDI-PPHLRNSALFPAVCLKNAEVEFNFGDK 154
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 430-574 6.92e-34

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: 126.66  E-value: 6.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 430 LMMVGLPASGKTTWAEKHAAENPTkkfNILGTNAIMEKMKVMGLRRQRNYAGRWDVliqqATQCLNRLIQIAARKKRNYI 509
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGA---VRLSSDDERKRLFGEGRPSISYYTDATDR----TYERLHELARIALRAGRPVI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031939749 510 LDQTNVYGSAQRRKMRPFE--GFQRKAIVICPTDEDLKERTLKRTDEEGK--DVPDHAVLEMKANFALP 574
Cdd:pfam13671  75 LDATNLRRDERARLLALAReyGVPVRIVVFEAPEEVLRERLAARARAGGDpsDVPEEVLDRQKARFEPP 143
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 260-391 2.51e-24

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 98.52  E-value: 2.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749  260 KGKVCFEMKINeeisvkhlpssepDPHVVRVGWSLDSCS----TQLGEEEFSYGYGGT-GKKSTNCKFEDFGEKFRE-ND 333
Cdd:smart00449   1 SGRHYFEVEIG-------------DGGHWRVGVATKSVPrgyfALLGEDKGSWGYDGDgGKKYHNSTGPEYGLPLQEpGD 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749  334 VIGCFIDFEAGeevEMAYSKNGEWL-GVGFRVSKeelADRALFPHVLVKN-CAIEFNFGQ 391
Cdd:smart00449  68 VIGCFLDLEAG---TISFYKNGKYLhGLAFFDVK---FSGPLYPAFSLGSgNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 282-391 5.12e-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: 94.72  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 282 EPDPHVVRVGWSLDSCSTQ----LGEEEFSYGYGG-TGKKSTNCKFEDFGE-KFRENDVIGCFIDFEAGeevEMAYSKNG 355
Cdd:pfam00622  10 GQDGGGWRVGWATKSVPRKgerfLGDESGSWGYDGwTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAG---TISFTKNG 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2031939749 356 EWLGVGFRVSKeelADRALFPHV-LVKNCAIEFNFGQ 391
Cdd:pfam00622  87 KSLGYAFRDVP---FAGPLFPAVsLGAGEGLKFNFGL 120
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 249-397 7.81e-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: 89.50  E-value: 7.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 249 WSGARVSYGVSKGKVCFEMKINEeisvkhlPSSEPDPHvVRVGWSLDSCSTQ--LGEEEFSYGYGG-TGKKSTNCKFEDF 325
Cdd:cd12872    16 YRMARANHGVREGKWYFEVKILE-------GGGTETGH-VRVGWSRREASLQapVGYDKYSYAIRDkDGSKFHQSRGKPY 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031939749 326 GEK-FRENDVIGCFIDFEageevEMAYSKNGEWLGVGFRVSKEELadrALFPHV-LVKNCAIEFNFGqkeePYF 397
Cdd:cd12872    88 GEPgFKEGDVIGFLITLP-----KIEFFKNGKSQGVAFEDIYGTG---GYYPAVsLYKGATVTINFG----PDF 149
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 261-388 1.69e-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: 84.79  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 261 GKVCFEMKINEEISvkhlpssepdpHVVRVGWSLDSCSTQ----LGEEEFSYGYGGTGKKS-TNCKFEDFGEKFRENDVI 335
Cdd:cd11709     1 GKWYWEVRVDSGNG-----------GLIQVGWATKSFSLDgeggVGDDEESWGYDGSRLRKgHGGSSGPGGRPWKSGDVV 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2031939749 336 GCFIDFEAGeevEMAYSKNGEWLGVGFRVSKeeLADRALFPHV-LVKNCAIEFN 388
Cdd:cd11709    70 GCLLDLDEG---TLSFSLNGKDLGVAFTNLF--LKGGGLYPAVsLGSGQGVTIN 118
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 265-390 5.66e-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: 72.31  E-value: 5.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 265 FEMKINeeisvkhlpsSEPDPHVVRVGWSLDSCST--QLGEEEFSYGY-GGTGKKSTNCKF-EDFGEKFRENDVIGCFID 340
Cdd:cd12885    18 FEVTIL----------DLGEKGIVSIGFCTSGFPLnrMPGWEDGSYGYhGDDGRVYLGGGEgENYGPPFGTGDVVGCGIN 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2031939749 341 FEAGeevEMAYSKNGEWLGVGFrvskEELADRALFP--HVLVKNCAIEFNFG 390
Cdd:cd12885    88 FKTG---EVFFTKNGELLGTAF----ENVVKGRLYPtvGLGSPGVKVRVNFG 132
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 287-390 6.31e-11

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: 60.42  E-value: 6.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 287 VVRVGWSLDSC----STQLGEEEFSYGYGGTGKKSTNCKFEDFGEKFRENDVIGCFIDFEAGeevEMAYSKNGEWLGVGF 362
Cdd:cd12882    24 IMQIGWATISCrftqEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKG---TISFYRNGRSLGVAF 100

                          90       100       110
                  ....*....|....*....|....*....|
gi 2031939749 363 -RVSKeeLADRALFPHV-LVKNCAIEFNFG 390
Cdd:cd12882   101 dNVRR--GPGLAYFPAVsLSFGERLELNFG 128
COG4639 COG4639
Predicted kinase [General function prediction only];
426-583 1.52e-10

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 59.84  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 426 ECEILMMVGLPASGKTTWAEKHAAENPtkkfnILGTNAIMEKMKVmGLRRQRNYAGRWDVLIQQATQCLnrliqiaaRKK 505
Cdd:COG4639     1 MLSLVVLIGLPGSGKSTFARRLFAPTE-----VVSSDDIRALLGG-DENDQSAWGDVFQLAHEIARARL--------RAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 506 RNYILDQTNVygsaQRRKMRPFEGFQRK------AIVICPTDEDLKERTLKRTdeegKDVPDHAVLEMKANF-ALPECGE 578
Cdd:COG4639    67 RLTVVDATNL----QREARRRLLALARAygalvvAVVLDVPLEVCLARNAARD----RQVPEEVIRRMLRRLrRPPLPEE 138


                  ....*
gi 2031939749 579 VLDSV 583
Cdd:COG4639   139 GFRVV 143
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 255-358 2.97e-09

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: 55.77  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 255 SYGVSKGKVCFEMKINeeisvkhlpssepDPHVVRVGWSLDSC--STQLGEEEFSYGYGGTGKKSTNCKFEDFGEKFREN 332
Cdd:cd12878     8 TYAVTSGKWYFEFEVL-------------TSGYMRVGWARPGFrpDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPG 74

                          90       100
                  ....*....|....*....|....*.
gi 2031939749 333 DVIGCFIDFEAGeevEMAYSKNGEWL 358
Cdd:cd12878    75 DVVGCMLDLVDR---TISFTLNGELL 97
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 302-391 1.91e-08

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: 53.68  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 302 GEEEFSYGY----------GGTGKKstnckfedFGEKFRENDVIGCFIDFeageeVEMA--YSKNGEWLGVGFRvskeEL 369
Cdd:cd12909    58 GWEPHSWGYhgddghsfcsSGTGKP--------YGPTFTTGDVIGCGINF-----RDNTafYTKNGVNLGIAFR----DI 120

                          90       100
                  ....*....|....*....|....
gi 2031939749 370 ADRALFPHVLVK--NCAIEFNFGQ 391
Cdd:cd12909   121 KKGNLYPTVGLRtpGEHVEANFGQ 144
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
6-40 2.57e-08

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 50.18  E-value: 2.57e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2031939749    6 VRKLKVHELKEELQARGLEARGLKADLAERLQAAL 40
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 8-40 7.55e-08

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: 48.94  E-value: 7.55e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2031939749   8 KLKVHELKEELQARGLEARGLKADLAERLQAAL 40
Cdd:pfam02037   3 KLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
pseT PHA02530
polynucleotide kinase; Provisional
 426-576 5.38e-05

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 45.78  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 426 ECEILMMVGLPASGKTTWAEKHAAENPtKKFNIlgtNAIMEKMKVMGLRRQRNYAGRWDVliQQATQCLNRLIQIAA-RK 504
Cdd:PHA02530    1 MMKIILTVGVPGSGKSTWAREFAAKNP-KAVNV---NRDDLRQSLFGHGEWGEYKFTKEK--EDLVTKAQEAAALAAlKS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 505 KRNYILDQTNVyGSAQRRKMRPF---EGFQRKAIVICPTDEDLKERTLKRTDeegKDVPDHAVLEM-------------- 567
Cdd:PHA02530   75 GKSVIISDTNL-NPERRRKWKELakeLGAEFEEKVFDVPVEELVKRNRKRGE---RAVPEDVLRSMfkqmkeyrglvwpv 150

                         170
                  ....*....|
gi 2031939749 568 -KANFALPEC 576
Cdd:PHA02530  151 yTADPGLPKA 160
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 301-363 6.61e-05

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: 44.46  E-value: 6.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031939749 301 LGEEEFSYGYGGTGKKSTNCKFEDFGEKFR-ENDVIGCFIDFEAGEeveMAYSKNGEWLGVGFR 363
Cdd:cd12876    83 LGEDEESWGLSYKGLLWHDGQSRPYTSPFGnQGTIIGVHLDMWRGT---LTFYKNGKPLGVAFT 143
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 285-390 9.67e-05

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: 42.72  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 285 PHVVRVGWSLDSCSTQ------LGEEEFSYGYGGTGK------KSTNCKFEdfgeKFRENDVIGCFIDFEAGeevEMAYS 352
Cdd:cd12883    12 SGVMQIGWATKDSKFLnhegygIGDDEYSCAYDGCRQliwynaKSKPHTHP----RWKPGDVLGCLLDLNKK---QMIFS 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2031939749 353 KNGEWLGVGFRVskEELADRALFPHV-LVKNCAIEFNFG 390
Cdd:cd12883    85 LNGNRLPPERQV--FTSAKSGFFAAAsFMSFQQCEFNFG 121
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 1-113 3.68e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.06  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749   1 MSAvdvrKLKVHELKEELQARGLEARGLKADLAERLQAALDSEALGVAVAAPPPPPGVVLGEGYAGEGDAE---DDEKEQ 77
Cdd:PLN03124    1 MAN----KLKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRERQDDGDDEpvsPKRIAI 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2031939749  78 DQVLGMEAGDSLAdqdqgfsELSADGLDDTSVKEEI 113
Cdd:PLN03124   77 DEVKGMTVRELRE-------AASERGLATTGRKKDL 105
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
429-574 1.02e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 40.67  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031939749 429 ILMMVGLPASGKTTWAEKHAAENPtkkFNILGTNAIMEKMKVMGLRRQRNYAGRWDvliqQATQCLNRLIQIAARKKRNY 508
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLG---AVRLRSDVVRKRLFGAGLAPLERSPEATA----RTYARLLALARELLAAGRSV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031939749 509 ILDQTnvYGSAQRRKMrpFEGFQRKA-----IVICPTDED-LKERTLKRTDEEGKDVPDHAVLEMKANFALP 574
Cdd:COG0645    74 ILDAT--FLRRAQREA--FRALAEEAgapfvLIWLDAPEEvLRERLEARNAEGGDSDATWEVLERQLAFEEP 141
dnaE PRK06826
DNA polymerase III DnaE; Reviewed
 365-404 3.83e-03

DNA polymerase III DnaE; Reviewed


Pssm-ID: 235868 [Multi-domain]  Cd Length: 1151  Bit Score: 41.03  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2031939749  365 SKEELADraLFPHVL--VKN-------CAIEFNFGQKEEPYFPVPEGYT 404
Cdd:PRK06826   248 SPEEMYE--LFSYVPeaLENtvkiaerCNVEFEFGKSKLPKFPLPEGYD 294
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 421-487 5.28e-03

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 38.53  E-value: 5.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2031939749 421 PASKAECEILMMvGLPASGKTTWAEKHAAEN-----PTKKFNILGTNAIMEKMKV--MGLRRQ-----RNYAGRWDVLI 487
Cdd:cd04155    10 PSSRQEVRILLL-GLDNAGKTTILKQLASEDishitPTQGFNIKNVQADGFKLNVwdIGGQRKirpywRNYFENTDVLI 87
 
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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