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Conserved domains on  [gi|71773010|ref|NP_001025178|]
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AP-1 complex subunit gamma-1 isoform a [Homo sapiens]

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, ...
23-577 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: 551.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 71773010   575 KYD 577
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
712-820 1.01e-35

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: 130.44  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 71773010    792 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 820
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
593-654 3.15e-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: 44.52  E-value: 3.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71773010   593 VTTNGPTEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIPTAPTSKPSS 654
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVVTSPPKNATSA 628
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
23-577 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: 551.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 71773010   575 KYD 577
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
712-820 1.01e-35

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: 130.44  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 71773010    792 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 820
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
708-820 6.97e-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: 125.51  E-value: 6.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   708 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKV 787
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 71773010   788 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 820
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-573 1.31e-09

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


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 61.67  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096  61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKNEKLVPQLvrilkn 228
Cdd:COG5096 141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLEVILRIPQL------ 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 229 limsgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL------- 297
Cdd:COG5096 213 ----------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlf 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 298 --------TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKD 359
Cdd:COG5096 283 lisspplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQN 352
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 360 LDVSIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgIFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR-- 437
Cdd:COG5096 353 LSQILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRis 429
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 438 DDAVPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDI 511
Cdd:COG5096 430 VLVLRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI 494
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 512 lesvLISNM--STSVTRGYALTAIMKLS----TRFTCTVNRIKKVVSIY--GSSIDVELQQRAVEYNALF 573
Cdd:COG5096 495 ----AISNFvdETLEVQYTILMSSVKLIansiRKAKQCNSELDQDVLRRcfDYVLVPDLRDRARMYSRLL 560
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
593-654 3.15e-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: 44.52  E-value: 3.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71773010   593 VTTNGPTEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIPTAPTSKPSS 654
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVVTSPPKNATSA 628
 
Name Accession Description Interval E-value
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
23-577 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: 551.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGIFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 71773010   575 KYD 577
Cdd:pfam01602 521 LAD 523
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
712-820 1.01e-35

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: 130.44  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010    712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 71773010    792 KQQLRMRIKLTYNHKGSAMQDLAEVNNFP 820
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
708-820 6.97e-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: 125.51  E-value: 6.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   708 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKV 787
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 71773010   788 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 820
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-573 1.31e-09

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


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 61.67  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096  61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKNEKLVPQLvrilkn 228
Cdd:COG5096 141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLEVILRIPQL------ 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 229 limsgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL------- 297
Cdd:COG5096 213 ----------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlf 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 298 --------TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKD 359
Cdd:COG5096 283 lisspplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQN 352
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 360 LDVSIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgIFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR-- 437
Cdd:COG5096 353 LSQILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRis 429
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 438 DDAVPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDI 511
Cdd:COG5096 430 VLVLRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI 494
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010 512 lesvLISNM--STSVTRGYALTAIMKLS----TRFTCTVNRIKKVVSIY--GSSIDVELQQRAVEYNALF 573
Cdd:COG5096 495 ----AISNFvdETLEVQYTILMSSVKLIansiRKAKQCNSELDQDVLRRcfDYVLVPDLRDRARMYSRLL 560
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
593-654 3.15e-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: 44.52  E-value: 3.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71773010   593 VTTNGPTEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIPTAPTSKPSS 654
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVVTSPPKNATSA 628
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
118-209 5.92e-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: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71773010   118 VQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRkvPELMEM--FLPATKNLLNEKNHGVLHTSV 195
Cdd:pfam12717   2 IRALAIRTMGCIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLIL--PDMVKVkgFISELAKLLEDPNPMVVANAL 79
                          90
                  ....*....|....
gi 71773010   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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