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Conserved domains on  [gi|667751602|ref|NP_001288140|]
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AP-1 complex subunit gamma-1 isoform 2 [Mus musculus]

Protein Classification

AP-1 complex subunit gamma( domain architecture ID 12024706)

AP-1 complex subunit gamma is a subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
23-574 0e+00

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


:

Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 553.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRND-D 261
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL---KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPLDpL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  262 DSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHN 341
Cdd:pfam01602 225 LPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEPK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  342 AVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKRWHI 419
Cdd:pfam01602 298 AVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWYL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  420 DTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeeepiq 499
Cdd:pfam01602 377 DVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS------- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  500 vtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFKKYD 574
Cdd:pfam01602 449 -----PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLSLAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
709-817 4.81e-36

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


:

Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 131.60  E-value: 4.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   709 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 788
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 667751602   789 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 817
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
590-702 3.46e-05

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: 47.60  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  590 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 664
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 667751602  665 LTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAP 702
Cdd:pfam05109 638 SSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHP 675
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
23-574 0e+00

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 553.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRND-D 261
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL---KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPLDpL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  262 DSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHN 341
Cdd:pfam01602 225 LPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEPK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  342 AVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKRWHI 419
Cdd:pfam01602 298 AVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWYL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  420 DTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeeepiq 499
Cdd:pfam01602 377 DVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS------- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  500 vtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFKKYD 574
Cdd:pfam01602 449 -----PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLSLAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
709-817 4.81e-36

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 131.60  E-value: 4.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   709 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 788
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 667751602   789 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 817
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
705-817 4.66e-34

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 125.90  E-value: 4.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  705 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKV 784
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 667751602  785 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 817
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-570 3.51e-08

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 57.05  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096   61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKlvpqLVRILKNLim 228
Cdd:COG5096  141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLE----VILRIPQL-- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 229 sgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL---------- 294
Cdd:COG5096  213 -------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlflis 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 295 -----TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKDLDV 359
Cdd:COG5096  286 spplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQNLSQ 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 360 SIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgIFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR--DDA 437
Cdd:COG5096  356 ILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRisVLV 432
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 438 VPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDIles 511
Cdd:COG5096  433 LRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI--- 494
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667751602 512 vLISNM--STSVTRGYALTAIMKLS----TRFTCTVNRIKKVVSIY--GSSIDVELQQRAVEYNALF 570
Cdd:COG5096  495 -AISNFvdETLEVQYTILMSSVKLIansiRKAKQCNSELDQDVLRRcfDYVLVPDLRDRARMYSRLL 560
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
590-702 3.46e-05

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: 47.60  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  590 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 664
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 667751602  665 LTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAP 702
Cdd:pfam05109 638 SSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHP 675
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
23-574 0e+00

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 553.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRND-D 261
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL---KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPLDpL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  262 DSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHN 341
Cdd:pfam01602 225 LPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMKEPK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  342 AVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKRWHI 419
Cdd:pfam01602 298 AVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAEWYL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  420 DTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeeepiq 499
Cdd:pfam01602 377 DVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS------- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  500 vtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFKKYD 574
Cdd:pfam01602 449 -----PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLSLAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
709-817 4.81e-36

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 131.60  E-value: 4.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602   709 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 788
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 667751602   789 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 817
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
705-817 4.66e-34

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 125.90  E-value: 4.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  705 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKV 784
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 667751602  785 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 817
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-570 3.51e-08

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 57.05  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096   61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKlvpqLVRILKNLim 228
Cdd:COG5096  141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLE----VILRIPQL-- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 229 sgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL---------- 294
Cdd:COG5096  213 -------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlflis 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 295 -----TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKDLDV 359
Cdd:COG5096  286 spplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQNLSQ 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 360 SIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgIFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR--DDA 437
Cdd:COG5096  356 ILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRisVLV 432
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602 438 VPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDIles 511
Cdd:COG5096  433 LRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI--- 494
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667751602 512 vLISNM--STSVTRGYALTAIMKLS----TRFTCTVNRIKKVVSIY--GSSIDVELQQRAVEYNALF 570
Cdd:COG5096  495 -AISNFvdETLEVQYTILMSSVKLIansiRKAKQCNSELDQDVLRRcfDYVLVPDLRDRARMYSRLL 560
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
590-702 3.46e-05

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: 47.60  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  590 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 664
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 667751602  665 LTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAP 702
Cdd:pfam05109 638 SSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHP 675
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
118-209 5.52e-03

non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.


Pssm-ID: 463677 [Multi-domain]  Cd Length: 162  Bit Score: 38.21  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751602  118 VQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRkvPELMEM--FLPATKNLLNEKNHGVLHTSV 195
Cdd:pfam12717   2 IRALAIRTMGCIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLIL--PDMVKVkgFISELAKLLEDPNPMVVANAL 79
                          90
                  ....*....|....
gi 667751602  196 VLLTEMCERSPDML 209
Cdd:pfam12717  80 AALTEISEKDPNAI 93
 
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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