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Conserved domains on  [gi|497815369|ref|NP_001265084|]
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E3 ubiquitin-protein ligase HACE1 [Gallus gallus]

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 ...
 587-936 4.66e-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: 473.21  E-value: 4.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 587 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSSEIVNPDYALFTQSADGT-TFQPNSNS 664
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 665 SVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 744
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 745 TDV-FGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 823
Cdd:cd00078  162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 824 IDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMggsglQNFTIAAVPYTANLL 903
Cdd:cd00078  242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|...
gi 497815369 904 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 936
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-249 2.04e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   3 RAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLV 82
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDA 162
Cdd:COG0666  105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 163 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDKNGITPLDLCVQGGY 241
Cdd:COG0666  185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGA 264


                 ....*...
gi 497815369 242 GETCEVLI 249
Cdd:COG0666  265 ALIVKLLL 272
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 587-936 4.66e-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: 473.21  E-value: 4.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 587 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSSEIVNPDYALFTQSADGT-TFQPNSNS 664
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 665 SVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 744
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 745 TDV-FGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 823
Cdd:cd00078  162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 824 IDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMggsglQNFTIAAVPYTANLL 903
Cdd:cd00078  242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|...
gi 497815369 904 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 936
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 612-935 4.93e-135

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: 407.78  E-value: 4.93e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   612 KQGIAVRFHGEEGM-GQGVVREWFDILSSEIVNPDYALFTQSADGTTFQPNSNSSV-NPDHLNYFRFAGQILGLALNHRQ 689
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   690 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGASILVTQ 767
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   768 ENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQ 847
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   848 WFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGgsglqNFTIAAVPYTANLLPTSSTCINMLKLPEYPSKEILKDR 927
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 497815369   928 LLVALHCG 935
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 636-938 2.22e-126

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.27  E-value: 2.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  636 ILSSEIVNPDYALF-TQSADGTTFQPNSNSSVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 712
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  713 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQIN 791
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  792 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGS 871
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497815369  872 SRVPHGGFAhimggsGLQNFTIAAVPYTA-NLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 938
Cdd:pfam00632 240 SRLPVGGFK------SLPKFTIVRKGGDDdDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
588-932 2.57e-117

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 379.50  E-value: 2.57e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 588 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSSEIVNPDYALFT-QSADGTTFQPNSNSS 665
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 666 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 745
Cdd:COG5021  597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 746 DVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 824
Cdd:COG5021  677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 825 DVNDWLKNTEYtSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGGSGLQNFTIAAVPYTANLLP 904
Cdd:COG5021  757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                        330       340
                 ....*....|....*....|....*...
gi 497815369 905 TSSTCINMLKLPEYPSKEILKDRLLVAL 932
Cdd:COG5021  836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-249 2.04e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   3 RAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLV 82
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDA 162
Cdd:COG0666  105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 163 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDKNGITPLDLCVQGGY 241
Cdd:COG0666  185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGA 264


                 ....*...
gi 497815369 242 GETCEVLI 249
Cdd:COG0666  265 ALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-194 3.99e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltaihwlavngrtellh 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 497815369  149 dlvqhvsnvdvedamGQTALHVACQNGHKTTVQCLLDSGADINRPN 194
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-261 1.97e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  35 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 106
Cdd:PHA03100  37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 107 RN--GQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTEL--LHDLVQHVSNVDVedamgqtalhvacqnghKTTVQC 182
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNY 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 183 LLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKY-LPDKNGITPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 261
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-221 8.43e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 8.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 100 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTE---LLHDLVQHVSNVDVEDAM--GQTALHVAC 172
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEaavVLMEAAPELVNEPMTSDLyqGETALHIAV 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497815369 173 QNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLMRGA 221
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 163-191 6.78e-06

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: 43.35  E-value: 6.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 497815369   163 MGQTALHVACQNGHKTTVQCLLDSGADIN 191
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 587-936 4.66e-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: 473.21  E-value: 4.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 587 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSSEIVNPDYALFTQSADGT-TFQPNSNS 664
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 665 SVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 744
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 745 TDV-FGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 823
Cdd:cd00078  162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 824 IDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMggsglQNFTIAAVPYTANLL 903
Cdd:cd00078  242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|...
gi 497815369 904 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 936
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 612-935 4.93e-135

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: 407.78  E-value: 4.93e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   612 KQGIAVRFHGEEGM-GQGVVREWFDILSSEIVNPDYALFTQSADGTTFQPNSNSSV-NPDHLNYFRFAGQILGLALNHRQ 689
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   690 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGASILVTQ 767
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   768 ENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQ 847
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   848 WFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGgsglqNFTIAAVPYTANLLPTSSTCINMLKLPEYPSKEILKDR 927
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 497815369   928 LLVALHCG 935
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 636-938 2.22e-126

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.27  E-value: 2.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  636 ILSSEIVNPDYALF-TQSADGTTFQPNSNSSVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 712
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  713 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQIN 791
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  792 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGS 871
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497815369  872 SRVPHGGFAhimggsGLQNFTIAAVPYTA-NLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 938
Cdd:pfam00632 240 SRLPVGGFK------SLPKFTIVRKGGDDdDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
588-932 2.57e-117

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 379.50  E-value: 2.57e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 588 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSSEIVNPDYALFT-QSADGTTFQPNSNSS 665
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 666 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 745
Cdd:COG5021  597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 746 DVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 824
Cdd:COG5021  677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 825 DVNDWLKNTEYtSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGGSGLQNFTIAAVPYTANLLP 904
Cdd:COG5021  757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                        330       340
                 ....*....|....*....|....*...
gi 497815369 905 TSSTCINMLKLPEYPSKEILKDRLLVAL 932
Cdd:COG5021  836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-249 2.04e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   3 RAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLV 82
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDA 162
Cdd:COG0666  105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 163 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDKNGITPLDLCVQGGY 241
Cdd:COG0666  185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGA 264


                 ....*...
gi 497815369 242 GETCEVLI 249
Cdd:COG0666  265 ALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-252 2.12e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.51  E-value: 2.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  25 DDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHL 104
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 105 AARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLL 184
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497815369 185 DSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDKNGITPLDLCVQGGYGETCEVLIQYH 252
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-234 4.69e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 4.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   1 MERAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVEC 80
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  81 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVE 160
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497815369 161 DAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKYLPDKNGITPLD 234
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-251 8.88e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 8.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  49 LLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICN 128
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 129 NEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHG 208
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 497815369 209 QRDTAQILLMRGAK-YLPDKNGITPLDLCVQGGYGETCEVLIQY 251
Cdd:COG0666  165 NLEIVKLLLEAGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-251 7.30e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 7.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  81 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVE 160
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 161 DAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDKNGITPLDLCVQG 239
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADvNAQDNDGNTPLHLAAAN 163

                        170
                 ....*....|..
gi 497815369 240 GYGETCEVLIQY 251
Cdd:COG0666  164 GNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-194 3.99e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltaihwlavngrtellh 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 497815369  149 dlvqhvsnvdvedamGQTALHVACQNGHKTTVQCLLDSGADINRPN 194
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-261 1.97e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  35 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 106
Cdd:PHA03100  37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 107 RN--GQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTEL--LHDLVQHVSNVDVedamgqtalhvacqnghKTTVQC 182
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNY 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 183 LLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKY-LPDKNGITPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 261
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
135-223 1.24e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  135 IHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSgADINRPNvSGATPLYFACSHGQRDTAQ 214
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 497815369  215 ILLMRGAKY 223
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-201 1.58e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  77 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC---MSKLLEYSADVN---ICnneGLTAIHWLAVNGRTE-LLHD 149
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNapeRC---GFTPLHLYLYNATTLdVIKL 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497815369 150 LVQHVSNVDVEDAMGQTALHVAC--QNGHKTTVQCLLDSGADINRPNVSGATPL 201
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
168-251 8.21e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  168 LHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKYLPDkNGITPLDLCVQGGYGETCEV 247
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 497815369  248 LIQY 251
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-251 9.14e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 9.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  36 PMVMADQHRSVS--ELLSNSKFDVNYAFGRVkRSLLHIAANCGSVECLVLLLKKGANPN---YQDisGCTPLHLAARNGQ 110
Cdd:PHA02875  38 PIKLAMKFRDSEaiKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 111 KKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADI 190
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497815369 191 N----RPNVsgaTPLYFACSHGQRDTAQILLMRGAkylpDKNGITpldlCVQGGYGETCEVLIQY 251
Cdd:PHA02875 195 DyfgkNGCV---AALCYAIENNKIDIVRLFIKRGA----DCNIMF----MIEGEECTILDMICNM 248
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 83-233 7.95e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.95  E-value: 7.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLA-----------VNGRTELLHD-- 149
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiIDNRSNINKNdl 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 150 -LVQHVSNVDVE---------------DAMGQTALHVACQNGHKTT-VQCLLDSGADINRPNVSGATPLYFACSHGQrDT 212
Cdd:PHA02876 243 sLLKAIRNEDLEtslllydagfsvnsiDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGY-DT 321

                        170       180
                 ....*....|....*....|....
gi 497815369 213 AQI--LLMRGAKY-LPDKNGITPL 233
Cdd:PHA02876 322 ENIrtLIMLGADVnAADRLYITPL 345
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-237 9.67e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 9.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  56 DVNYAfGRVKRSLLHI-----AANCGSVEclvLLLKKGANPNYQDISGCTPLHLAARNgqKKCMSKLLEY--SADVNICN 128
Cdd:PHA03095 109 DVNAK-DKVGRTPLHVylsgfNINPKVIR---LLLRKGADVNALDLYGMTPLAVLLKS--RNANVELLRLliDAGADVYA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 129 --NEGLTAIHWLAVNGRT--ELLHDLVQHVSNVDVEDAMGQTALHVA-----CQNGHkttVQCLLDSGADINRPNVSGAT 199
Cdd:PHA03095 183 vdDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRSL---VLPLLIAGISINARNRYGQT 259

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497815369 200 PLYFACSHGQRDTAQILLMRGAKYLP-DKNGITPLDLCV 237
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAvSSDGNTPLSLMV 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-283 7.82e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 7.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  27 NETAVYTLMPMVMADQHRSVSEL---LSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLH 103
Cdd:PHA02876 267 NSIDDCKNTPLHHASQAPSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 104 LAAR-NGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVA-CQNGHKTTVQ 181
Cdd:PHA02876 347 QASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 182 CLLDSGADINRPNVSGATPLYFACSHGQR-DTAQILLMRGAkylpDKNGITPLD---LCVQGGYGETCEVLIQYHPRLFQ 257
Cdd:PHA02876 427 TLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA----DVNAINIQNqypLLIALEYHGIVNILLHYGAELRD 502

                        250       260
                 ....*....|....*....|....*...
gi 497815369 258 TIIqmtQNEDLRENM--LRQVLEHLSQQ 283
Cdd:PHA02876 503 SRV---LHKSLNDNMfsFRYIIAHICIQ 527
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-233 8.26e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 8.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  56 DVNYAfGRVKRSLLHIAANCGSVEC---LVLLLKKGANPNYQDISGCTPLHLAARNGQK--------------------- 111
Cdd:PHA03095  39 DVNFR-GEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTldvikllikagadvnakdkvg 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 112 -----KCMSK----------LLEYSADVNICNNEGLTAIHWLAVNGRT--ELLHDLVQHVSNVDVEDAMGQTALHVACQN 174
Cdd:PHA03095 118 rtplhVYLSGfninpkvirlLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHHHLQS 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497815369 175 GHKTT--VQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQI--LLMRGAKY-LPDKNGITPL 233
Cdd:PHA03095 198 FKPRAriVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISInARNRYGQTPL 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-221 2.61e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.13  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   3 RAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNS---KFDVNYAFgrvkrSLLHIAANcGSVE 79
Cdd:PLN03192 466 KTLSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNggeHDDPNMAS-----NLLTVAST-GNAA 539

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  80 CLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIhWLAVNGRTELLHDLVQHVSNVDV 159
Cdd:PLN03192 540 LLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRILYHFASISD 618

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497815369 160 EDAMGQTaLHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGA 221
Cdd:PLN03192 619 PHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 33-238 3.04e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  33 TLMPMVmaDQHRS----VSELLSNSKFDVNYAFGRVKRSLL---HIAAN-------------------CGSVECLVLLLK 86
Cdd:PHA02874  35 TTTPLI--DAIRSgdakIVELFIKHGADINHINTKIPHPLLtaiKIGAHdiikllidngvdtsilpipCIEKDMIKTILD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  87 KGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQT 166
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497815369 167 ALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHgQRDTAQILLMRGAKYLPDKNGITPLDLCVQ 238
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAIN 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-126 2.77e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369   34 LMPMVMADQHRSVSELLSN-SKFDVNYAFGRvkrSLLHIAANCGSVECLVLLLKKgANPNYQDiSGCTPLHLAARNGQKK 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgADANLQDKNGR---TALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....
gi 497815369  113 CMSKLLEYSADVNI 126
Cdd:pfam12796  76 IVKLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-208 4.29e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  43 HRSVSELLSNSKFDVN--YAFGRVKRSLLHIAANCgSVECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLL 118
Cdd:PHA03095 131 NPKVIRLLLRKGADVNalDLYGMTPLAVLLKSRNA-NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 119 EYSADVNICNNEGLTAIHWLAVNG--RTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 196
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                        170
                 ....*....|..
gi 497815369 197 GATPLYFACSHG 208
Cdd:PHA03095 290 GNTPLSLMVRNN 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 46-204 4.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  46 VSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN 125
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 126 ICNNEGLTAIHWLAvnGRT---ELLHDLVQHVSNVDVEDA-MGQTALHVACQNGHKTTVqcLLDSGADINRPNVSGATPL 201
Cdd:PHA02878 229 ARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKL--LLEYGADINSLNSYKLTPL 304


                 ...
gi 497815369 202 YFA 204
Cdd:PHA02878 305 SSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-118 8.35e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 8.35e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 497815369   66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL 118
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-217 5.57e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497815369  166 TALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 217
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-221 8.43e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 8.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 100 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTE---LLHDLVQHVSNVDVEDAM--GQTALHVAC 172
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEaavVLMEAAPELVNEPMTSDLyqGETALHIAV 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497815369 173 QNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLMRGA 221
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 156-257 1.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.22  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 156 NVDVEDAMGQTALHVA----CQ---NGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAK-YLPDK 227
Cdd:PTZ00322  67 NLTTEEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDK 146

                         90       100       110
                 ....*....|....*....|....*....|
gi 497815369 228 NGITPLDLCVQGGYGETCEVLIQYHPRLFQ 257
Cdd:PTZ00322 147 DGKTPLELAEENGFREVVQLLSRHSQCHFE 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 76-249 1.92e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  76 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNG---RTELLHDLVQ 152
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdvkAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 153 HVSNVDVEDamGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL-MRGAKYLPDKNGIT 231
Cdd:PHA02875  93 FADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIdHKACLDIEDCCGCT 170

                        170
                 ....*....|....*...
gi 497815369 232 PLDLCVQGGYGETCEVLI 249
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-311 2.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL----------EYSADVNICNNEGLTAIHWL 138
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsinkcsvfyTLVAIKDAFNNRNVEIFKII 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 139 AVNG---------------------RTELLHDLVQHVSNVDVEDA-MGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 196
Cdd:PHA02878 121 LTNRykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 197 GATPLYFACSHGQRDTAQILLMRGAKY-LPDKNGITPLDLCVqgGYGETCEVLiqyhprlfQTIIQMTQNEDLRENMLRQ 275
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISV--GYCKDYDIL--------KLLLEHGVDVNAKSYILGL 270

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 497815369 276 VLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSS 311
Cdd:PHA02878 271 TALHSSIKSERKLKLLLEYGADINSLNSYKLTPLSS 306
Ank_4 pfam13637
Ankyrin repeats (many copies);
131-184 9.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 497815369  131 GLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLL 184
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 68-153 1.35e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  68 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELL 147
Cdd:PTZ00322  86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....*.
gi 497815369 148 HDLVQH 153
Cdd:PTZ00322 165 QLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 138-217 1.79e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 138 LAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 217
Cdd:PTZ00322  89 LAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
100-151 2.94e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 2.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497815369  100 TPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLV 151
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 63-292 5.39e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  63 RVKRSLLHIAANCGSVECLVLLLK-KGANPNYQDISGCTPLHLAARNGQKKCMSKLLEysADVNICNN-------EGLTA 134
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 135 IHWLAVNGRTELLHDLVQHVSNVDVEDAMG------QTAL-----HV----ACQnGHKTTVQCLLDSGADINRPNVSGAT 199
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLiyygeHPlsfaACV-GNEEIVRLLIEHGADIRAQDSLGNT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 200 PLY---------FAC-------SHGQRDTAQILLMrgakyLPDKNGITPLDLCVQGGYGETCEVLIQYHpRLFQ------ 257
Cdd:cd22192  172 VLHilvlqpnktFACqmydlilSYDKEDDLQPLDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQKR-RHIQwtygpl 245

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 497815369 258 --TIIQMTQNEDLRENMlrQVLEHLSQQSESQYLKIL 292
Cdd:cd22192  246 tsTLYDLTEIDSWGDEQ--SVLELIVSSKKREARKIL 280
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-105 7.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497815369   49 LLSNSKFDVNYaFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:pfam13857   1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-136 8.91e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 8.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 497815369   83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIH 136
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 84-238 2.63e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.82  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  84 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLA-----VNGRTELLHDLVQHVSN-V 157
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtddeVIERINLLVQYGAKINNsV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 158 DVE-----------------------------DAMGQTAL--HVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACS 206
Cdd:PHA02946 138 DEEgcgpllactdpservfkkimsigfearivDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                        170       180       190
                 ....*....|....*....|....*....|....
gi 497815369 207 HGQRDTAQILLMRGAKYLPDKN--GITPLDLCVQ 238
Cdd:PHA02946 218 KTVKNVDIINLLLPSTDVNKQNkfGDSPLTLLIK 251
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-129 5.01e-06

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: 43.82  E-value: 5.01e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 497815369   98 GCTPLHLAA-RNGQKKCMSKLLEYSADVNICNN 129
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 163-191 6.78e-06

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: 43.35  E-value: 6.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 497815369   163 MGQTALHVACQNGHKTTVQCLLDSGADIN 191
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 98-126 2.09e-05

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: 42.19  E-value: 2.09e-05
                           10        20
                   ....*....|....*....|....*....
gi 497815369    98 GCTPLHLAARNGQKKCMSKLLEYSADVNI 126
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 164-194 2.79e-05

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: 41.89  E-value: 2.79e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 497815369  164 GQTALHVAC-QNGHKTTVQCLLDSGADINRPN 194
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
183-236 4.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 497815369  183 LLDSG-ADINRPNVSGATPLYFACSHGQRDTAQILLMRGA-KYLPDKNGITPLDLC 236
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 164-191 7.58e-05

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: 40.32  E-value: 7.58e-05
                          10        20
                  ....*....|....*....|....*...
gi 497815369  164 GQTALHVACQNGHKTTVQCLLDSGADIN 191
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 66-121 1.90e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497815369  66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYS 121
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank_5 pfam13857
Ankyrin repeats (many copies);
150-204 2.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 497815369  150 LVQHVS-NVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFA 204
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-126 2.64e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.64e-04
                          10        20
                  ....*....|....*....|....*....
gi 497815369   98 GCTPLHLAARNGQKKCMSKLLEYSADVNI 126
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 66-95 4.68e-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: 38.42  E-value: 4.68e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 497815369   66 RSLLHIAA-NCGSVECLVLLLKKGANPNYQD 95
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 64-135 8.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 8.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497815369  64 VKRSLLHIAANCGSVECLVLLLKKGANPN-YQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAI 135
Cdd:PHA02884  69 SKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 66-93 1.53e-03

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: 36.80  E-value: 1.53e-03
                           10        20
                   ....*....|....*....|....*...
gi 497815369    66 RSLLHIAANCGSVECLVLLLKKGANPNY 93
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-171 6.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 6.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 497815369  117 LLEY-SADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVA 171
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 56-202 7.39e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369  56 DVNYAFGRVKRSLLHiaANCGS----VECLVLLLKKGANPNYQDISGCTPLHLAARNGQ--KKCMSKLLEYSADVNI--C 127
Cdd:PHA02716 168 NLNYVCKKTGYGILH--AYLGNmyvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMkcV 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497815369 128 N---------------NEGLTAIHWLAVNGRT-----ELLHDLVQHVSNVDV---------------EDAMGQTALH--V 170
Cdd:PHA02716 246 NgmspimtyiinidniNPEITNIYIESLDGNKvknipMILHSYITLARNIDIsvvysflqpgvklhyKDSAGRTCLHqyI 325

                        170       180       190
                 ....*....|....*....|....*....|..
gi 497815369 171 ACQNGHKTTVQCLLDSGADINRPNVSGATPLY 202
Cdd:PHA02716 326 LRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH 357
 
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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