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Conserved domains on  [gi|1182924236|ref|NP_001337484|]
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E3 ubiquitin-protein ligase HACE1 isoform f [Homo sapiens]

Protein Classification

ANKYR and HECTc domain-containing protein( domain architecture ID 12789490)

ANKYR and HECTc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 457-806 3.06e-160

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 469.35  E-value: 3.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 457 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 534
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 535 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 614
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 615 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 693
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 694 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 773
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182924236 774 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 806
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-154 1.31e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236   1 MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVEC 80
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182924236  81 LVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGN--LEIVKLLLEAGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 457-806 3.06e-160

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 469.35  E-value: 3.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 457 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 534
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 535 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 614
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 615 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 693
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 694 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 773
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182924236 774 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 806
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 482-805 6.92e-133

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 398.15  E-value: 6.92e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  482 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 559
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  560 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 637
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  638 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 717
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  718 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 797
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1182924236  798 LLVALHCG 805
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 506-808 4.84e-127

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 382.34  E-value: 4.84e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 506 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 582
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 583 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 661
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 662 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 741
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182924236 742 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 808
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
458-802 1.71e-116

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 373.72  E-value: 1.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 458 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 535
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 536 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 615
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 616 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 694
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 695 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 774
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1182924236 775 TSSTCINMLKLPEYPSKEILKDRLLVAL 802
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-154 1.31e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236   1 MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVEC 80
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182924236  81 LVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGN--LEIVKLLLEAGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-154 8.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAKYLPDkNGVTPLDLCVQGGYGETC 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH--LEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*.
gi 1182924236 149 EVLIQY 154
Cdd:pfam12796  78 KLLLEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 68-160 1.22e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  68 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGHGQrdTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGE 146
Cdd:PTZ00322   86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ--VVRVLLEFGADpTLLDKDGKTPLELAEENGFRE 162

                          90
                  ....*....|....
gi 1182924236 147 TCEVLIQYHPRLFQ 160
Cdd:PTZ00322  163 VVQLLSRHSQCHFE 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 66-93 7.84e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.84e-04
                           10        20
                   ....*....|....*....|....*...
gi 1182924236   66 RSLLHIAANCGSVECLVLLLKKGANPNY 93
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 457-806 3.06e-160

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 469.35  E-value: 3.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 457 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 534
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 535 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 614
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 615 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 693
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 694 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 773
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182924236 774 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 806
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 482-805 6.92e-133

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 398.15  E-value: 6.92e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  482 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 559
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  560 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 637
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  638 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 717
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  718 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 797
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1182924236  798 LLVALHCG 805
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 506-808 4.84e-127

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 382.34  E-value: 4.84e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 506 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 582
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 583 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 661
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 662 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 741
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182924236 742 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 808
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
458-802 1.71e-116

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 373.72  E-value: 1.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 458 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 535
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 536 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 615
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 616 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 694
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 695 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 774
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1182924236 775 TSSTCINMLKLPEYPSKEILKDRLLVAL 802
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-154 1.31e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236   1 MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVEC 80
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182924236  81 LVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGN--LEIVKLLLEAGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-155 1.41e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.09  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  25 EDNETAvytLMPMVMADQHRSVSELLSNsKFDVNYAfGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHL 104
Cdd:COG0666   118 KDGETP---LHLAAYNGNLEIVKLLLEA-GADVNAQ-DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1182924236 105 AARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYH 155
Cdd:COG0666   193 AAENGH--LEIVKLLLEAGADvNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-154 6.49e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 6.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  26 DNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666    49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1182924236 106 ARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:COG0666   128 AYNGN--LEIVKLLLEAGADvNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-154 8.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAKYLPDkNGVTPLDLCVQGGYGETC 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH--LEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*.
gi 1182924236 149 EVLIQY 154
Cdd:pfam12796  78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-152 1.85e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  48 ELLSNSKFDVNYAfGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAK-Y 126
Cdd:COG0666   170 KLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN--LEIVKLLLEAGADlN 246

                          90       100
                  ....*....|....*....|....*.
gi 1182924236 127 LPDKNGVTPLDLCVQGGYGETCEVLI 152
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-126 4.51e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  34 LMPMVMADQHRSVSELLSN-SKFDVNYAFGRvkrSLLHIAANCGSVECLVLLLKKgANPNYQDiSGCTPLHLAARNGHgq 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgADANLQDKNGR---TALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGH-- 73

                          90
                  ....*....|....
gi 1182924236 113 RDTAQILLLRGAKY 126
Cdd:pfam12796  74 LEIVKLLLEKGADI 87
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-112 2.49e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1182924236  66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGHGQ 112
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 68-160 1.22e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  68 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGHGQrdTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGE 146
Cdd:PTZ00322   86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ--VVRVLLEFGADpTLLDKDGKTPLELAEENGFRE 162

                          90
                  ....*....|....
gi 1182924236 147 TCEVLIQYHPRLFQ 160
Cdd:PTZ00322  163 VVQLLSRHSQCHFE 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-154 6.14e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 6.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  26 DNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1182924236 106 ARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:COG0666    95 ARNGD--LEIVKLLLEAGADvNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-105 4.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1182924236  49 LLSNSKFDVNYaFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:pfam13857   1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-152 1.84e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  52 NSKFDVNYAFGRVKrSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARngHGQRDTAQILLLRGAkYL--PD 129
Cdd:PHA02874  112 DCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK--HNFFDIIKLLLEKGA-YAnvKD 187

                          90       100
                  ....*....|....*....|...
gi 1182924236 130 KNGVTPLDLCVQGGYGETCEVLI 152
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLI 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-154 2.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  35 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 106
Cdd:PHA03100   37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1182924236 107 RNGHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGET--CEVLIQY 154
Cdd:PHA03100  115 SKKSNSYSIVEYLLDNGANvNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 44-152 6.71e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  44 RSVSELLSNSKF--DVNYAFGRVKrslLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGhgqrDTAQILLL 121
Cdd:PHA02875   82 KAVEELLDLGKFadDVFYKDGMTP---LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG----DIKGIELL 154

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1182924236 122 ---RGAKYLPDKNGVTPLDLCVQGGYGETCEVLI 152
Cdd:PHA02875  155 idhKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-151 8.38e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 8.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182924236  77 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGHGQR-DTAQILLLRGAKY-LPDKNGVTPLDLCVQggYGETCEVL 151
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkDIVRLLLEAGADVnAPERCGFTPLHLYLY--NATTLDVI 100
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 66-120 5.23e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 5.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1182924236  66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNghGQRDTAQILL 120
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN--GFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-136 5.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  47 SELLSNSKFDVNyAFGRVKRSLLHIAANCGSVECLV-LLLKKGANPNYQDISGCTPLHLAARNGHgqrDTAQI--LLLRG 123
Cdd:PHA02876  256 SLLLYDAGFSVN-SIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPLYLMAKNGY---DTENIrtLIMLG 331

                          90
                  ....*....|....
gi 1182924236 124 AKY-LPDKNGVTPL 136
Cdd:PHA02876  332 ADVnAADRLYITPL 345
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-139 9.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 9.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1182924236  83 LLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGA-KYLPDKNGVTPLDLC 139
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGA--LEIVRVLLAYGVdLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-255 1.89e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236   3 RAMEQLNRL-TRSLRRARTVElPEDNETAVYTLMPMVMADQHRSVSELLSNS---KFDVNYAFgrvkrSLLHIAANcGSV 78
Cdd:PLN03192  466 KTLSQLLRLkTSTLIEAMQTR-QEDNVVILKNFLQHHKELHDLNVGDLLGDNggeHDDPNMAS-----NLLTVAST-GNA 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  79 ECLVLLLKKGANPNYQDISGCTPLHLAARNGHgqRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLiqYHpr 157
Cdd:PLN03192  539 ALLEELLKAKLDPDIGDSKGRTPLHIAASKGY--EDCVLVLLKHACNvHIRDANGNTALWNAISAKHHKIFRIL--YH-- 612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 158 lFQTIIQMTQNEDL-----REN---MLRQVLEH-LSQQSESQylKILTSLaEVATTNGH----KLLSLS------SNYDA 218
Cdd:PLN03192  613 -FASISDPHAAGDLlctaaKRNdltAMKELLKQgLNVDSEDH--QGATAL-QVAMAEDHvdmvRLLIMNgadvdkANTDD 688

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1182924236 219 QMKS--LLRIV--RMFCHVFRIGPSSPSNGIDMGYNGNKTP 255
Cdd:PLN03192  689 DFSPteLRELLqkRELGHSITIVDSVPADEPDLGRDGGSRP 729
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 66-95 2.05e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.05e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1182924236  66 RSLLHIAA-NCGSVECLVLLLKKGANPNYQD 95
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-131 7.06e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  26 DNETAvytLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666   185 DGETP---LHLAAENGHLEIVKLLLEA-GADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                          90       100
                  ....*....|....*....|....*.
gi 1182924236 106 ARNGHGQRDTAQILLLRGAKYLPDKN 131
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDL 285
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 66-93 7.84e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.84e-04
                           10        20
                   ....*....|....*....|....*...
gi 1182924236   66 RSLLHIAANCGSVECLVLLLKKGANPNY 93
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-95 8.99e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 8.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1182924236  38 VMADQHRSVSELLSNSKFDVNYAfgrvKRSLLHIAANCGSVECLVLLLKKGANPNYQD 95
Cdd:pfam12796  38 AKNGHLEIVKLLLEHADVNLKDN----GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 45-124 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  45 SVSELLSNSKFDVNyAFGRVKRSL----------------LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARN 108
Cdd:PHA03100  157 KILKLLIDKGVDIN-AKNRVNYLLsygvpinikdvygftpLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                          90
                  ....*....|....*.
gi 1182924236 109 GHGqrDTAQILLLRGA 124
Cdd:PHA03100  236 NNK--EIFKLLLNNGP 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 46-214 1.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  46 VSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARngHGQRDTAQILLLRGAK 125
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK--HYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236 126 Y-LPDKNGVTPLDLCVqgGYGETCEVLiqyhprlfQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATT 204
Cdd:PHA02878  227 TdARDKCGNTPLHISV--GYCKDYDIL--------KLLLEHGVDVNAKSYILGLTALHSSIKSERKLKLLLEYGADINSL 296

                         170
                  ....*....|
gi 1182924236 205 NGHKLLSLSS 214
Cdd:PHA02878  297 NSYKLTPLSS 306
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-155 1.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  65 KRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGHGQRD---TAQILLLRGA-KYLPDKNGVTPLDLCV 140
Cdd:PHA03100   35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDvkeIVKLLLEYGAnVNAPDNNGITPLLYAI 114

                          90
                  ....*....|....*..
gi 1182924236 141 QG--GYGETCEVLIQYH 155
Cdd:PHA03100  115 SKksNSYSIVEYLLDNG 131
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-124 3.91e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.91e-03
                          10        20
                  ....*....|....*....|....*..
gi 1182924236  98 GCTPLHLAARNgHGQRDTAQILLLRGA 124
Cdd:pfam00023   2 GNTPLHLAAGR-RGNLEIVKLLLSKGA 27
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 27-154 5.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182924236  27 NETAVYTLMPMVMADQHRSVS-------ELLSNSKFDVNyAFGRVKRSLLHIAANC--GSVECLVLLLKKGANPNYQDIS 97
Cdd:PHA03100   62 NSSTKNNSTPLHYLSNIKYNLtdvkeivKLLLEYGANVN-APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182924236  98 GCTPLHLAARNGHGQRDTAQILLLRGA--------KYL---------PDKNGVTPLDLCVQGGYGETCEVLIQY 154
Cdd:PHA03100  141 GENLLHLYLESNKIDLKILKLLIDKGVdinaknrvNYLlsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDL 214
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 66-92 7.69e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 7.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 1182924236  66 RSLLHIAANCGSVECLVLLLKKGANPN 92
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
 
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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