NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|330443694|ref|NP_014156|]
View 

Sla2p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 7-269 1.18e-88

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


:

Pssm-ID: 400137  Cd Length: 272  Bit Score: 284.19  E-value: 1.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694    7 DLQKALKKACSVEETAPKRKHVRACIVYTWD-HQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRD 85
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   86 RDWIRSLGRV--HSGGSSYSKLIREYVRYLVLKLDFHAHHRGFnNGTFEYEEYVSLVSVSDPDEGYETiLDLMSLQDSLD 163
Cdd:pfam07651  81 RRRISSLLRIssFSLSWDYGAFIRAYAKYLDERLDFHRKLPRD-PGTFERVEYGSLVAVGDPNERYLT-MSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  164 EFSQIIFASIQ----SERRNTECKISALIPLIAESYGIYKFITSMLRAMHRQLNDA--EGDAALQPLKERYELQHARLFE 237
Cdd:pfam07651 159 KLQKLLFRLLKcrptGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELskPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 330443694  238 FYADCSSVKYLTTLVtIPKLPVDAPDVFLIND 269
Cdd:pfam07651 239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALE 269
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 763-965 4.30e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 266.54  E-value: 4.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   763 HLRVDVPKPLLSLALMIIDAVVALVKAAIQCQNEIAT--TTSIPLNQFYLKNSRWTEGLISAAKAVAGATNVLITTASKL 840
Cdd:smart00307   1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAqgRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   841 ITsednENTSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCSKDVTDACRSLGNHVM-GMIEDdhstSQQQQ 919
Cdd:smart00307  81 VT----GKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKsGMIFD----EEQEE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 330443694   920 PLDFT--SEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYYNQ 965
Cdd:smart00307 153 EEDFSklSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 420-546 1.03e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 420 ALTNQYEKDQALLQQYDQRVQQLESEITTMDS---TASKQLAN--KDEQLTALQDQLdvwerkyESLAKLYSQLRQEHLN 494
Cdd:COG1579   42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNvrNNKEYEALQKEI-------ESLKRRISDLEDEILE 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443694 495 LLPRFKKLQLKVNSAQESIQK-KEQLEHKLKQKDLQMAELVKDRDRARLELER 546
Cdd:COG1579  115 LMERIEELEEELAELEAELAElEAELEEKKAELDEELAELEAELEELEAEREE 167
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 7-269 1.18e-88

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 284.19  E-value: 1.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694    7 DLQKALKKACSVEETAPKRKHVRACIVYTWD-HQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRD 85
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   86 RDWIRSLGRV--HSGGSSYSKLIREYVRYLVLKLDFHAHHRGFnNGTFEYEEYVSLVSVSDPDEGYETiLDLMSLQDSLD 163
Cdd:pfam07651  81 RRRISSLLRIssFSLSWDYGAFIRAYAKYLDERLDFHRKLPRD-PGTFERVEYGSLVAVGDPNERYLT-MSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  164 EFSQIIFASIQ----SERRNTECKISALIPLIAESYGIYKFITSMLRAMHRQLNDA--EGDAALQPLKERYELQHARLFE 237
Cdd:pfam07651 159 KLQKLLFRLLKcrptGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELskPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 330443694  238 FYADCSSVKYLTTLVtIPKLPVDAPDVFLIND 269
Cdd:pfam07651 239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALE 269
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 763-965 4.30e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 266.54  E-value: 4.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   763 HLRVDVPKPLLSLALMIIDAVVALVKAAIQCQNEIAT--TTSIPLNQFYLKNSRWTEGLISAAKAVAGATNVLITTASKL 840
Cdd:smart00307   1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAqgRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   841 ITsednENTSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCSKDVTDACRSLGNHVM-GMIEDdhstSQQQQ 919
Cdd:smart00307  81 VT----GKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKsGMIFD----EEQEE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 330443694   920 PLDFT--SEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYYNQ 965
Cdd:smart00307 153 EEDFSklSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 8-120 1.70e-62

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 206.77  E-value: 1.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   8 LQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRD 87
Cdd:cd17007    1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 330443694  88 WIRSLGRVHSGGS--SYSKLIREYVRYLVLKLDFH 120
Cdd:cd17007   81 WLESLGRQSSGSGakGYGRLIKEYVRYLLDKLAFH 115
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
 811-963 1.27e-55

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 188.95  E-value: 1.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  811 KNSRWTEGLISAAKAVAGATNVLITTASKLITSEDnentSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCS 890
Cdd:pfam01608   1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQG----SEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAAS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443694  891 KDVTDACRSLGNHVMGMIEDDHSTSQQQQPLDFTSEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYY 963
Cdd:pfam01608  77 KAVTDATKNLVAAVKSAAELQEEEIEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
6-127 7.99e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 7.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694     6 SDLQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLAND--EVQLFKMLIVLHKIIQEGHPSALAEAI 83
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTknWRVVYKALILLHYLLRNGSPRVILEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 330443694    84 RDRDWIRSLGR---VHSGGSSYSKLIREYVRYLVLKLDFHAHHRGFN 127
Cdd:smart00273  81 RNRNRILNLSDfqdIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 420-546 1.03e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 420 ALTNQYEKDQALLQQYDQRVQQLESEITTMDS---TASKQLAN--KDEQLTALQDQLdvwerkyESLAKLYSQLRQEHLN 494
Cdd:COG1579   42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNvrNNKEYEALQKEI-------ESLKRRISDLEDEILE 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443694 495 LLPRFKKLQLKVNSAQESIQK-KEQLEHKLKQKDLQMAELVKDRDRARLELER 546
Cdd:COG1579  115 LMERIEELEEELAELEAELAElEAELEEKKAELDEELAELEAELEELEAEREE 167
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 7-269 1.18e-88

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 284.19  E-value: 1.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694    7 DLQKALKKACSVEETAPKRKHVRACIVYTWD-HQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRD 85
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   86 RDWIRSLGRV--HSGGSSYSKLIREYVRYLVLKLDFHAHHRGFnNGTFEYEEYVSLVSVSDPDEGYETiLDLMSLQDSLD 163
Cdd:pfam07651  81 RRRISSLLRIssFSLSWDYGAFIRAYAKYLDERLDFHRKLPRD-PGTFERVEYGSLVAVGDPNERYLT-MSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  164 EFSQIIFASIQ----SERRNTECKISALIPLIAESYGIYKFITSMLRAMHRQLNDA--EGDAALQPLKERYELQHARLFE 237
Cdd:pfam07651 159 KLQKLLFRLLKcrptGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELskPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 330443694  238 FYADCSSVKYLTTLVtIPKLPVDAPDVFLIND 269
Cdd:pfam07651 239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALE 269
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
 763-965 4.30e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 266.54  E-value: 4.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   763 HLRVDVPKPLLSLALMIIDAVVALVKAAIQCQNEIAT--TTSIPLNQFYLKNSRWTEGLISAAKAVAGATNVLITTASKL 840
Cdd:smart00307   1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAqgRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   841 ITsednENTSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCSKDVTDACRSLGNHVM-GMIEDdhstSQQQQ 919
Cdd:smart00307  81 VT----GKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKsGMIFD----EEQEE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 330443694   920 PLDFT--SEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYYNQ 965
Cdd:smart00307 153 EEDFSklSLHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 8-120 1.70e-62

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 206.77  E-value: 1.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   8 LQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRD 87
Cdd:cd17007    1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 330443694  88 WIRSLGRVHSGGS--SYSKLIREYVRYLVLKLDFH 120
Cdd:cd17007   81 WLESLGRQSSGSGakGYGRLIKEYVRYLLDKLAFH 115
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
 811-963 1.27e-55

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 188.95  E-value: 1.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  811 KNSRWTEGLISAAKAVAGATNVLITTASKLITSEDnentSPEQFIVASKEVAASTIQLVAASRVKTSIHSKAQDKLEHCS 890
Cdd:pfam01608   1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQG----SEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAAS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443694  891 KDVTDACRSLGNHVMGMIEDDHSTSQQQQPLDFTSEHTLKTAEMEQQVEILKLEQSLSNARKRLGEIRRHAYY 963
Cdd:pfam01608  77 KAVTDATKNLVAAVKSAAELQEEEIEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 8-120 1.72e-39

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 142.13  E-value: 1.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   8 LQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRD 87
Cdd:cd16986    1 FEKAVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSLLGGYLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 330443694  88 WIRSLGRVHSGG----SSYSKLIREYVRYLVLKLDFH 120
Cdd:cd16986   81 WLPELVRVKNTQqslsEFYSQLIKKYVRYLELKVVFH 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
6-127 7.99e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 7.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694     6 SDLQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLAND--EVQLFKMLIVLHKIIQEGHPSALAEAI 83
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTknWRVVYKALILLHYLLRNGSPRVILEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 330443694    84 RDRDWIRSLGR---VHSGGSSYSKLIREYVRYLVLKLDFHAHHRGFN 127
Cdd:smart00273  81 RNRNRILNLSDfqdIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 8-120 1.91e-32

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 122.00  E-value: 1.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   8 LQKALKKACSVEETAPKRKHVRACIVYTWDH---QSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIR 84
Cdd:cd03564    1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGggrADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 330443694  85 DRDWIRSLGRVH----SGGSSYSKLIREYVRYLVLKLDFH 120
Cdd:cd03564   81 YSGHIFNLSNFKddssPEAWDLSAFIRRYARYLEERLECF 120
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 11-120 7.28e-29

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 111.61  E-value: 7.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  11 ALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRDWIR 90
Cdd:cd17006    4 SINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSRLK 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 330443694  91 SLGRV--HSGGsSYSKLIREYVRYLVLKLDFH 120
Cdd:cd17006   84 ELGKLwgHLKD-GYGKLIAQYCKLLITKLEFH 114
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 11-120 1.44e-15

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 73.53  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  11 ALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDR---- 86
Cdd:cd17013    4 SINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKnels 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 330443694  87 DWIRSLGRVHSGgssYSKLIREYVRYLVLKLDFH 120
Cdd:cd17013   84 DMSRMWGHLSEG---YGQLCSIYLKLLITKMEFH 114
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 11-120 3.43e-13

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.


Pssm-ID: 340811  Cd Length: 114  Bit Score: 66.81  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  11 ALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRDWIR 90
Cdd:cd17014    4 SISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNIR 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 330443694  91 SLG----RVHSGgssYSKLIREYVRYLVLKLDFH 120
Cdd:cd17014   84 ETGslwgHLHDR---YGQLVSLYTKLLCTKIEFH 114
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 9-113 4.06e-07

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 49.49  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694   9 QKALKKACSVEETAPKRKHVRACIVYTwdHQSSKAVFTTLKTLplandEVQL--------FKMLIVLHKIIQEGHPSALA 80
Cdd:cd16988    2 EKLVKGATKIKLAPPKAKYLDPILLAT--YSSDASFGEIVRAL-----SRRLrdnswtvvFKSLIVLHLMIREGETDDVL 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 330443694  81 EAIRDRDWI---RSLGRVHSGGSSYSKLIREYVRYL 113
Cdd:cd16988   75 LYYLSRPDFldlRKIRNGSSAGSGQLQNIQRYAAYL 110
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 420-546 1.03e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 420 ALTNQYEKDQALLQQYDQRVQQLESEITTMDS---TASKQLAN--KDEQLTALQDQLdvwerkyESLAKLYSQLRQEHLN 494
Cdd:COG1579   42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNvrNNKEYEALQKEI-------ESLKRRISDLEDEILE 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443694 495 LLPRFKKLQLKVNSAQESIQK-KEQLEHKLKQKDLQMAELVKDRDRARLELER 546
Cdd:COG1579  115 LMERIEELEEELAELEAELAElEAELEEKKAELDEELAELEAELEELEAEREE 167
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
452-546 4.78e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694  452 TASKQLANKDEQLTALQDQLDVWERKYESLAKLYSQL--RQEHLNLLPRFKKLQLKVNSAQESI-QKKEQLEH------K 522
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIaELEAELERldassdD 686

                          90       100
                  ....*....|....*....|....
gi 330443694  523 LKQKDLQMAELVKDRDRARLELER 546
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDE 710
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
429-548 8.13e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 429 QALLQQYDQRVQQLESEIttmdsTASKQLANKDEQLTALQDQLDVWERKYESLAKLYS----------QLRQEHLNLLPR 498
Cdd:COG1566   89 EAQLAAAEAQLARLEAEL-----GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKkgavsqqeldEARAALDAAQAQ 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 330443694 499 FKKLQLKVNSAQESIQKKEQLEhklkQKDLQMAELVKDRDRARLELERSI 548
Cdd:COG1566  164 LEAAQAQLAQAQAGLREEEELA----AAQAQVAQAEAALAQAELNLARTT 209
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
437-550 1.01e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 437 QRVQQLESEIttmdstasKQLANKDEQLTALQDQLDVWERKYESLAKLYSQLRQEHLNLlprfkklqLKVNSAQESIQKK 516
Cdd:COG4717   71 KELKELEEEL--------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQEL 134

                         90       100       110
                 ....*....|....*....|....*....|....
gi 330443694 517 EQLEHKLKQKDLQMAELvKDRDRARLELERSINN 550
Cdd:COG4717  135 EALEAELAELPERLEEL-EERLEELRELEEELEE 167
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 424-546 5.74e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443694 424 QYEKDQALL----QQYDQRVQQLESEITtmdsTASKQLANKDEQLTALQDQLDVWERKYESLAKLYSQLRQEHLNLLPRF 499
Cdd:COG1196  299 RLEQDIARLeerrRELEERLEELEEELA----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 330443694 500 KKLQLKVNSAQESIQ--KKEQLEHKLKQKDLQMAELVKDRDRARLELER 546
Cdd:COG1196  375 AEAEEELEELAEELLeaLRAAAELAAQLEELEEAEEALLERLERLEEEL 423
 
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