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Conserved domains on  [gi|224014212|ref|XP_002296769|]
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predicted protein [Thalassiosira pseudonana CCMP1335]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 101-153 8.14e-12

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16655:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 55  Bit Score: 60.98  E-value: 8.14e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224014212  101 HLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYN 153
Cdd:cd16655     3 EFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVPN 55
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
 198-404 5.78e-07

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.90  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  198 IIKHQSLIPRRTATAKSLPLRKSKAKRSKDKVASKMQDELLVVKSNRLLMQMQEELEMLEKQHENEVRMHTVSLEE---- 273
Cdd:PTZ00108 1152 IAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDdeeq 1231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  274 --APKTQQKPRLEEPKKKRQVSSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSR-FPSHPHQPSPQQSCSPT-P 349
Cdd:PTZ00108 1232 ktKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpDGESNGGSKPSSPTKKKvK 1311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 224014212  350 KRVVKSHAIKPSSKSSTRATTSSNTS-SRVSKASPHSETKAPVTTDKLDSKSNINN 404
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSkTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-561 1.85e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   293 SSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSRFPSH-PHQPSPQQSC-SPTPKRVVKSHAI-KPSSKSSTRAT 369
Cdd:pfam05109  460 APASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKaPDMTSPTSAVtTPTPNATSPTPAVtTPTPNATSPTL 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   370 TSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRS----------SRSLEEACSHFPPPRHPSSSPVSAKMSV 439
Cdd:pfam05109  540 GKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSavttptpnatSPTVGETSPQANTTNHTLGGTSSTPVVT 619

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   440 ALPLATSRASSS-----TVPTTPRCSRSPSTRNQVLPSSQANLNNVHHVHCHAKLPRSSRSLEEACSHFAPSRHPS-SSP 513
Cdd:pfam05109  620 SPPKNATSAVTTgqhniTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVStSSP 699

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 224014212   514 VSAKKSVALPLATFRASSSSAPTTPRCSRSPSTRNQVLPSSQANLNNA 561
Cdd:pfam05109  700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTA 747
 
Name Accession Description Interval E-value
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 101-153 8.14e-12

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 60.98  E-value: 8.14e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224014212  101 HLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYN 153
Cdd:cd16655     3 EFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVPN 55
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 198-404 5.78e-07

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.90  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  198 IIKHQSLIPRRTATAKSLPLRKSKAKRSKDKVASKMQDELLVVKSNRLLMQMQEELEMLEKQHENEVRMHTVSLEE---- 273
Cdd:PTZ00108 1152 IAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDdeeq 1231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  274 --APKTQQKPRLEEPKKKRQVSSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSR-FPSHPHQPSPQQSCSPT-P 349
Cdd:PTZ00108 1232 ktKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpDGESNGGSKPSSPTKKKvK 1311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 224014212  350 KRVVKSHAIKPSSKSSTRATTSSNTS-SRVSKASPHSETKAPVTTDKLDSKSNINN 404
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSkTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 101-158 5.38e-06

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 44.92  E-value: 5.38e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 224014212    101 HLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYNPRVKE 158
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKS 58
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 232-291 3.21e-05

Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197399 [Multi-domain]  Cd Length: 90  Bit Score: 43.59  E-value: 3.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  232 KMQDELLVVKSNRllmQMQEELEMLE--KQHENEVRMHTVSLEEAPK--------TQQKPRLEEPKKKRQ 291
Cdd:cd10163     8 QLQQELLLIQQQQ---QIQKQLLIAEfqKQHENLTRQHQAQLQEHLKlqqellamKQQQELLEKEQKLEQ 74
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-561 1.85e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   293 SSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSRFPSH-PHQPSPQQSC-SPTPKRVVKSHAI-KPSSKSSTRAT 369
Cdd:pfam05109  460 APASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKaPDMTSPTSAVtTPTPNATSPTPAVtTPTPNATSPTL 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   370 TSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRS----------SRSLEEACSHFPPPRHPSSSPVSAKMSV 439
Cdd:pfam05109  540 GKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSavttptpnatSPTVGETSPQANTTNHTLGGTSSTPVVT 619

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   440 ALPLATSRASSS-----TVPTTPRCSRSPSTRNQVLPSSQANLNNVHHVHCHAKLPRSSRSLEEACSHFAPSRHPS-SSP 513
Cdd:pfam05109  620 SPPKNATSAVTTgqhniTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVStSSP 699

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 224014212   514 VSAKKSVALPLATFRASSSSAPTTPRCSRSPSTRNQVLPSSQANLNNA 561
Cdd:pfam05109  700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTA 747
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 304-539 2.39e-04

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 45.27  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  304 VEVKTPT-PPTKTCSSREITETTKPRSSRFP---------SHP--------HQPSPQQSCSPT-PKRVVKSHAIKpSSKS 364
Cdd:COG5422    19 APRKSDAfVSKQLLPPRRLQRKLNPISIRNGadndiinseSKEsfgkyalgHQIFSSFSSSPKlFQRRNSAGPIT-HSPS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  365 STRATTSSNTSSRvSKASPHSETKAPVTTDKLDSKSNiNNAKASPRSSRS---LEEACSHFPPPRHPSSSPVSAKMSVal 441
Cdd:COG5422    98 ATSSTSSLNSNDG-DQFSPASDSLSFNPSSTQSRKDS-GPGDGSPVQKRKnplLPSSSTHGTHPPIVFTDNNGSHAGA-- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  442 PLATSRASSSTVPTTPRCSRSPSTRNQVLPSSQANLNNV-HHVHCHAKLPRSSRSLEEACSHFAPSRHPSSSPVSAKKSV 520
Cdd:COG5422   174 PNARSRKEIPSLGSQSMQLPSPHFRQKFSSSDTSNGFSYpSIRKNSRHSSNSMPSFPHSSTAVLLKRHSGSSGASLISSN 253

                         250
                  ....*....|....*....
gi 224014212  521 ALPLATFRASSSSAPTTPR 539
Cdd:COG5422   254 ITPSSSNSEAMSTSSKRPY 272
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 281-548 1.84e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  281 PRLEEPKKKRQVSSantkSRSCHVEVKTPTPPTKTCSSreiteTTKPRSSRF-----PSHPHQPSPQQSCSP--TPKRVV 353
Cdd:PHA03307  132 PDLSEMLRPVGSPG----PPPAASPPAAGASPAAVASD-----AASSRQAALplsspEETARAPSSPPAEPPpsTPPAAA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  354 KSHAIKPSSKSSTRATTSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRSSRSLEEACShfpPPRHPSSSPV 433
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRI---WEASGWNGPS 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  434 SAKMSVALPLATSRASSSTVPTTPRCSRSPSTRNQVL---PSSQANLnnvhhvhchAKLPRSSRSLEEACSHFAPS--RH 508
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSsssSSRESSS---------SSTSSSSESSRGAAVSPGPSpsRS 350

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 224014212  509 PSSSPVSA--------KKSVALPLATFRASSSSAPTTPRCSRSPSTRN 548
Cdd:PHA03307  351 PSPSRPPPpadpssprKRPRPSRAPSSPAASAGRPTRRRARAAVAGRA 398
 
Name Accession Description Interval E-value
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 101-153 8.14e-12

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 60.98  E-value: 8.14e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224014212  101 HLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYN 153
Cdd:cd16655     3 EFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVPN 55
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 198-404 5.78e-07

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.90  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  198 IIKHQSLIPRRTATAKSLPLRKSKAKRSKDKVASKMQDELLVVKSNRLLMQMQEELEMLEKQHENEVRMHTVSLEE---- 273
Cdd:PTZ00108 1152 IAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDdeeq 1231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  274 --APKTQQKPRLEEPKKKRQVSSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSR-FPSHPHQPSPQQSCSPT-P 349
Cdd:PTZ00108 1232 ktKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpDGESNGGSKPSSPTKKKvK 1311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 224014212  350 KRVVKSHAIKPSSKSSTRATTSSNTS-SRVSKASPHSETKAPVTTDKLDSKSNINN 404
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSkTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 101-158 5.38e-06

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 44.92  E-value: 5.38e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 224014212    101 HLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYNPRVKE 158
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKS 58
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 100-150 2.66e-05

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 42.55  E-value: 2.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 224014212  100 KHLICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVS-PVTGNSLNVSDL 150
Cdd:cd16664     2 EEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTcPITGQPLTHTDL 53
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 102-142 2.89e-05

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 42.16  E-value: 2.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 224014212  102 LICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTG 142
Cdd:cd16453     1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDNTDPFTR 41
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 102-162 3.02e-05

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 43.02  E-value: 3.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224014212  102 LICPLTKAPICHLVSDSE-GNSYEQKAILRWLDLEGVS---PVTG--NSLNVSDLKYNPRVKEGVEQ 162
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSRKKKakcPVAGcrNTVSKSDLVPDPELKRRIER 67
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 232-291 3.21e-05

Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197399 [Multi-domain]  Cd Length: 90  Bit Score: 43.59  E-value: 3.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  232 KMQDELLVVKSNRllmQMQEELEMLE--KQHENEVRMHTVSLEEAPK--------TQQKPRLEEPKKKRQ 291
Cdd:cd10163     8 QLQQELLLIQQQQ---QIQKQLLIAEfqKQHENLTRQHQAQLQEHLKlqqellamKQQQELLEKEQKLEQ 74
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-561 1.85e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   293 SSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSRFPSH-PHQPSPQQSC-SPTPKRVVKSHAI-KPSSKSSTRAT 369
Cdd:pfam05109  460 APASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKaPDMTSPTSAVtTPTPNATSPTPAVtTPTPNATSPTL 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   370 TSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRS----------SRSLEEACSHFPPPRHPSSSPVSAKMSV 439
Cdd:pfam05109  540 GKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSavttptpnatSPTVGETSPQANTTNHTLGGTSSTPVVT 619

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   440 ALPLATSRASSS-----TVPTTPRCSRSPSTRNQVLPSSQANLNNVHHVHCHAKLPRSSRSLEEACSHFAPSRHPS-SSP 513
Cdd:pfam05109  620 SPPKNATSAVTTgqhniTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVStSSP 699

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 224014212   514 VSAKKSVALPLATFRASSSSAPTTPRCSRSPSTRNQVLPSSQANLNNA 561
Cdd:pfam05109  700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTA 747
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 304-539 2.39e-04

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 45.27  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  304 VEVKTPT-PPTKTCSSREITETTKPRSSRFP---------SHP--------HQPSPQQSCSPT-PKRVVKSHAIKpSSKS 364
Cdd:COG5422    19 APRKSDAfVSKQLLPPRRLQRKLNPISIRNGadndiinseSKEsfgkyalgHQIFSSFSSSPKlFQRRNSAGPIT-HSPS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  365 STRATTSSNTSSRvSKASPHSETKAPVTTDKLDSKSNiNNAKASPRSSRS---LEEACSHFPPPRHPSSSPVSAKMSVal 441
Cdd:COG5422    98 ATSSTSSLNSNDG-DQFSPASDSLSFNPSSTQSRKDS-GPGDGSPVQKRKnplLPSSSTHGTHPPIVFTDNNGSHAGA-- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  442 PLATSRASSSTVPTTPRCSRSPSTRNQVLPSSQANLNNV-HHVHCHAKLPRSSRSLEEACSHFAPSRHPSSSPVSAKKSV 520
Cdd:COG5422   174 PNARSRKEIPSLGSQSMQLPSPHFRQKFSSSDTSNGFSYpSIRKNSRHSSNSMPSFPHSSTAVLLKRHSGSSGASLISSN 253

                         250
                  ....*....|....*....
gi 224014212  521 ALPLATFRASSSSAPTTPR 539
Cdd:COG5422   254 ITPSSSNSEAMSTSSKRPY 272
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 232-291 2.61e-04

Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197397 [Multi-domain]  Cd Length: 90  Bit Score: 40.83  E-value: 2.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224014212  232 KMQDELLVVKSNRllmQMQEELEMLE--KQHENEVRMHTVSLEEAPKTQQ-------KPRLEEPKKKRQ 291
Cdd:cd10149     8 QLQQELLALKQQQ---QIQKQLLIAEfqKQHENLTRQHEAQLQEHIKQQQemlaikqQQELLEKQRKLE 73
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 281-548 1.84e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  281 PRLEEPKKKRQVSSantkSRSCHVEVKTPTPPTKTCSSreiteTTKPRSSRF-----PSHPHQPSPQQSCSP--TPKRVV 353
Cdd:PHA03307  132 PDLSEMLRPVGSPG----PPPAASPPAAGASPAAVASD-----AASSRQAALplsspEETARAPSSPPAEPPpsTPPAAA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  354 KSHAIKPSSKSSTRATTSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRSSRSLEEACShfpPPRHPSSSPV 433
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRI---WEASGWNGPS 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  434 SAKMSVALPLATSRASSSTVPTTPRCSRSPSTRNQVL---PSSQANLnnvhhvhchAKLPRSSRSLEEACSHFAPS--RH 508
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSsssSSRESSS---------SSTSSSSESSRGAAVSPGPSpsRS 350

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 224014212  509 PSSSPVSA--------KKSVALPLATFRASSSSAPTTPRCSRSPSTRN 548
Cdd:PHA03307  351 PSPSRPPPpadpssprKRPRPSRAPSSPAASAGRPTRRRARAAVAGRA 398
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 102-154 1.84e-03

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 37.46  E-value: 1.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224014212  102 LICPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDLKYNP 154
Cdd:cd23149     1 FTCPITSGFMEDPVITPSGFSYERSAIERWLETKPEDPQTREPLTAKDLQPNR 53
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 273-594 3.31e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  273 EAPKTQQKPR--LEEPKKKRQVSSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSRFPSHPHQPspqqscsPTPK 350
Cdd:PTZ00449  541 DEPKEGGKPGetKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRP-------KSPK 613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  351 RvvkshaikpsSKSSTRATTSSNTSSRVSKASPHSETKaPVTTDKLDSKSNINNAKaSPRSSR-----SLEEacSHFPPP 425
Cdd:PTZ00449  614 L----------PELLDIPKSPKRPESPKSPKRPPPPQR-PSSPERPEGPKIIKSPK-PPKSPKppfdpKFKE--KFYDDY 679

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  426 RHPSSSPVSAKMSVALPLATSRASSSTVPTTPrcsRSPSTRNQVLPssqanlnnvhhvhchAKLPRSSRsleeacSHFAP 505
Cdd:PTZ00449  680 LDAAAKSKETKTTVVLDESFESILKETLPETP---GTPFTTPRPLP---------------PKLPRDEE------FPFEP 735

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  506 SRHPSSSPVSAKKSVALPLATFRASSSSAPTTPrcsrspstrnqvLPSSQANLNNAHHVHCHANLPPPPKRREDPLVKTE 585
Cdd:PTZ00449  736 IGDPDAEQPDDIEFFTPPEEERTFFHETPADTP------------LPDILAEEFKEEDIHAETGEPDEAMKRPDSPSEHE 803

                         330
                  ....*....|.
gi 224014212  586 PMS--NTASLP 594
Cdd:PTZ00449  804 DKPpgDHPSLP 814
PHA03247 PHA03247
large tegument protein UL36; Provisional
 264-601 3.62e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  264 VRMH--TVSLEEAPKTQQKPRLEEPKKKRQVSSANTKSRSCHVEVKTPTP-PTKTCSSREITETTKPRSSRFPSHPHQPS 340
Cdd:PHA03247 2661 VSRPrrARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPaPHALVSATPLPPGPAAARQASPALPAAPA 2740

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  341 PQqscsPTPKRVVKSHAIKPSSKSSTRATTSSNTSSRVSKASPHSETKAPVTTdkldSKSNINNAKASPRSSRSLEEACS 420
Cdd:PHA03247 2741 PP----AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA----SLSESRESLPSPWDPADPPAAVL 2812

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  421 hfppprhpssspvsaKMSVALPLATSRASSSTVPTTPRCSRSPSTRNQVLPSsqanlnnvhhvhchaklprssrslEEAC 500
Cdd:PHA03247 2813 ---------------APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS------------------------LPLG 2853

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212  501 SHFAPS-----RHPSSSPVSAKKSVALPlatfRASSSSAPTTPRcsrspSTRNQVLPSSQANLnnahhvhchanlPPPPK 575
Cdd:PHA03247 2854 GSVAPGgdvrrRPPSRSPAAKPAAPARP----PVRRLARPAVSR-----STESFALPPDQPER------------PPQPQ 2912

                         330       340
                  ....*....|....*....|....*.
gi 224014212  576 RREDPLVKTEPMSNTASLPPLHVPEQ 601
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPPPPPPR 2938
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 264-546 4.46e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 40.71  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   264 VRMHTVSLEEAPKTQQ--KPRLEEPKKKRQVSSANTKSRSCHVEVKTPTPPTKTCSSREITETTKPRSSRFPSHPHQPSP 341
Cdd:pfam17823  126 AAQSLPAAIAALPSEAfsAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   342 QQSCSPTPKRVVKShaIKPSSKSSTRATTSSNTSSRVSKASPHSETKAPVTTDKLDSKSNINNAK----ASPRSSRSleE 417
Cdd:pfam17823  206 LTPARGISTAATAT--GHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGtinmGDPHARRL--S 281

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   418 ACSHFPPPRHPSSSPVSAKMSVALPLATSRASSSTVPTTPRCSRSPSTR----NQVLPSSQANLNNVHHVHCHAK----- 488
Cdd:pfam17823  282 PAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTtlepNTPKSVASTNLAVVTTTKAQAKepsas 361

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224014212   489 ---LPRSSRSLE-EACShfaPSRHPSSSPVSAKKS-VALPLATFR------ASSSSAPTTPRCSRSPST 546
Cdd:pfam17823  362 pvpVLHTSMIPEvEATS---PTTQPSPLLPTQGAAgPGILLAPEQvateatAGTASAGPTPRSSGDPKT 427
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 104-150 5.16e-03

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 438325  Cd Length: 73  Bit Score: 36.77  E-value: 5.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 224014212  104 CPLTKAPICHLVSDSEGNSYEQKAILRWLDLEGVSPVTGNSLNVSDL 150
Cdd:cd16663     5 CALSLQPFENPVCTPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDL 51
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 308-573 5.90e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   308 TPTPPTKTCSSREITETTK--PRSSRFPSH---PHQPSPQQSC----SPTPKRVVK-SHAIKPS-----SKSSTRATTSS 372
Cdd:pfam05109  428 TTTSPTLNTTGFAAPNTTTglPSSTHVPTNltaPASTGPTVSTadvtSPTPAGTTSgASPVTPSpsprdNGTESKAPDMT 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   373 NTSSRVSKASPHSETKAPVTTDKLDSKSNINNAKASPRSSRSleeacshfppprhpsssPVSAKMSVALPLATSRASSST 452
Cdd:pfam05109  508 SPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVT-----------------TPTPNATSPTPAVTTPTPNAT 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224014212   453 VP----TTPRCSRSPSTRNQVLP-----SSQANLNNvHHVHCHAKLPRSSRSLEEACSHFAPSRHPSSSpvSAKKSVALp 523
Cdd:pfam05109  571 IPtlgkTSPTSAVTTPTPNATSPtvgetSPQANTTN-HTLGGTSSTPVVTSPPKNATSAVTTGQHNITS--SSTSSMSL- 646

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224014212   524 latfRASSSSAPTTPRCSRSPSTRNQVL----PSSQANL-------NNAHHVHCHANLPPP 573
Cdd:pfam05109  647 ----RPSSISETLSPSTSDNSTSHMPLLtsahPTGGENItqvtpasTSTHHVSTSSPAPRP 703
 
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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