NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1997588909|ref|NP_001380641|]
View 

AP-1 complex subunit gamma-1 isoform 1 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 550.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGVFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 1997588909 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 4.84e-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: 4.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 1997588909  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 ...
593-705 2.35e-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: 47.99  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 593 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 667
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1997588909 668 LTGAPAAAPTPASVPQITQPPFLLDGLSSQPLFNDIAP 705
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, ...
23-577 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: 550.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGVFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 1997588909 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 4.84e-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: 4.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 1997588909  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 4.50e-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: 126.28  E-value: 4.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 708 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKV 787
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1997588909 788 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 820
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-573 1.72e-09

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


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 61.28  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096    61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKNEKLVPQLvrilkn 228
Cdd:COG5096   141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLEVILRIPQL------ 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 229 limsgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL------- 297
Cdd:COG5096   213 ----------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlf 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 298 --------TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKD 359
Cdd:COG5096   283 lisspplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQN 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 360 LDVSIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgVFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR-- 437
Cdd:COG5096   353 LSQILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRis 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 438 DDAVPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDI 511
Cdd:COG5096   430 VLVLRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 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 ...
593-705 2.35e-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: 47.99  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 593 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 667
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1997588909 668 LTGAPAAAPTPASVPQITQPPFLLDGLSSQPLFNDIAP 705
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, ...
23-577 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: 550.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  23 EREMIQKECAAIRSSFREEDNtYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLL 102
Cdd:pfam01602   1 EEKRIQQELARILNSFRDDPR-KKKNAVKKLLYLIMLGEDISFLFFEVVKLVASKDFTLKRLGYLYLMLLAEESPDLAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 103 MTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNL 182
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVPELARDLAPDIKKLLVDRSPYVRKKAALAILKLYRKSPDLVRDFVPELKEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 183 LNEKNHGVLHTSVVLLTEMCeRSPDMLAhfrkneKLVPQLVRILKNLImsgyspehdvsGISDPFLQVRILRLLRILGRN 262
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEIC-KNDRLYL------KLLPLLFRRLCNLL-----------GVLNPWLQVKILRLLTRLAPL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 263 D-DDSSEAMNDILAQVAtntetskNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQT 341
Cdd:pfam01602 222 DpLLPKELLEDLLNLLQ-------NSNNAVLYETANTIVHLAPAPELIVLAVNALGRLLSSPDENLRYVALRNLNKIVMK 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 342 DHNAVQrHRSTIVDCLK-DLDVSIKRRAMELSFALVNGNNIRGMMKELLYFL-DSCEPEFKADCASGVFLAAEKYAPSKR 419
Cdd:pfam01602 295 EPKAVQ-HLDLIIFCLKtDDDISIRLRALDLLYALVNESNVKEIVKELLKYVhEIADPDFKIELVRAIGRLAEKFPTDAE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 420 WHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILgDYSQQPLVQVAAWCIGEYGDLLVSGQCeeee 499
Cdd:pfam01602 374 WYLDVLLDLLSLAGSYVVDEIVEVIRDIIQNVPELREYILEHLCELLE-DIESPEALAAALWILGEYGELIPNGSS---- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 500 piqvtedeVLDILESVLISNMSTSV-TRGYALTAIMKLSTRFTC--TVNRIKKVVSIYG--SSIDVELQQRAVEYNALFK 574
Cdd:pfam01602 449 --------PPDLLRSILEVFVLESAkVRAAALTALAKLGLTSPEetTQNLIIQLLLTLAtqDSLDLEVRDRAVEYLRLLS 520

                  ...
gi 1997588909 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 4.84e-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: 4.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  712 AYSKNGLKIEFTFERsntNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFntGTITQVIKVLNPQ 791
Cdd:smart00809   1 AYEKNGLQIGFKFER---RPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPG--GQITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
gi 1997588909  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 4.50e-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: 126.28  E-value: 4.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 708 PSITAYSKNGLKIEFTFERsNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKV 787
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFER-SRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1997588909 788 LNPQKQQLRMRIKLTYNhKGSAMQDLAEVNNFP 820
Cdd:pfam02883  80 ENPGKKPLRMRLKISYL-NGGAVQEQGDVLKFP 111
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
71-573 1.72e-09

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


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 61.28  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909  71 LKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSN 150
Cdd:COG5096    61 IKNVATRDVELKRLLYLYLERYAKLKPELALLAVNTIQKDLQDPNEEIRGFALRTLSLLRVKELLGNIIDPIKKLLTDPH 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 151 SYLRKKAALCAVHVIRKVPELM--EMFLPATKNLLNEKNHGVLHTSVVLLTEMCERspDMLAHFRKNEKLVPQLvrilkn 228
Cdd:COG5096   141 AYVRKTAALAVAKLYRLDKDLYheLGLIDILKELVADSDPIVIANALASLAEIDPE--LAHGYSLEVILRIPQL------ 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 229 limsgyspehDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVAT----NTETSKNVGNAILYETVL------- 297
Cdd:COG5096   213 ----------DLLSLSVSTEWLLLIILEVLTERVPTTPDSAEDFEERLSPPlqhnNAEVLLIAVKVILRLLVFlpsnnlf 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 298 --------TIMDIKSESGLRVLAINILGRF-----LLNNDKNIRYVA----LTSLL-KTVQTDHNAvqrhrstivdCLKD 359
Cdd:COG5096   283 lisspplvTLLAKPESLIQYVLRRNIQIDLevcskLLDKVKKLFLIEynddIYIKLeKLDQLTRLA----------DDQN 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 360 LDVSIKRRAMELSFALVNGNNIRGMMKElLYFLDSCEPEFKADCASgVFLAAEKYAPSKRWHIDTIMRVLTTAgSYVR-- 437
Cdd:COG5096   353 LSQILLELIYYIAENHIDAEMVSEAIKA-LGDLASKAESSVNDCIS-ELLELLEGVWIRGSYIVQEVRIVDCI-SVIRis 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 438 DDAVPNLIQlitNSVEMHAYTVQRLYKAiLGDYSQQPLV------QVAAWCIGEYGDLlvsgqceeeepIQVTEDEVLDI 511
Cdd:COG5096   430 VLVLRILPN---EYPKILLRGLYALEET-LELQSREPRAksvtdkYLGAWLLGEFSDI-----------IPRLEPELLRI 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 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 ...
593-705 2.35e-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: 47.99  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 593 VTTNGPSEIVQTNGETEPAPLETKPPPSGPQPT-----SQANDLLDLLGGNDITPVIptapTSKPASAGGELLDLLGDIT 667
Cdd:pfam05109 562 VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgetsPQANTTNHTLGGTSSTPVV----TSPPKNATSAVTTGQHNIT 637
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1997588909 668 LTGAPAAAPTPASVPQITQPPFLLDGLSSQPLFNDIAP 705
Cdd:pfam05109 638 SSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHP 675
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
118-209 5.44e-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: 38.60  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997588909 118 VQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRkvPELMEM--FLPATKNLLNEKNHGVLHTSV 195
Cdd:pfam12717   2 IRALAIRTMGCIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLIL--PDMVKVkgFISELAKLLEDPNPMVVANAL 79
                          90
                  ....*....|....
gi 1997588909 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH