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Conserved domains on  [gi|1720360882|ref|XP_030100842|]
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E3 ubiquitin-protein ligase HACE1 isoform X4 [Mus musculus]

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 ...
 524-873 1.05e-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: 472.82  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 524 ILLVHRDSIFRSSCEIVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 601
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 602 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 681
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 682 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 760
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 761 IDVNDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 840
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1720360882 841 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 873
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-222 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDA 132
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 133 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGY 211
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDNDGKTALDLAAENGN 231

                         170
                  ....*....|.
gi 1720360882 212 GQTCEVLIQYH 222
Cdd:COG0666   232 LEIVKLLLEAG 242
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 524-873 1.05e-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: 472.82  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 524 ILLVHRDSIFRSSCEIVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 601
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 602 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 681
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 682 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 760
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 761 IDVNDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 840
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1720360882 841 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 873
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 549-872 1.95e-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: 401.61  E-value: 1.95e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  549 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 626
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  627 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 704
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  705 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWIKNTEYTSGYEREDPVIQ 784
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  785 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 864
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1720360882  865 LLVALHCG 872
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 573-875 9.04e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.20  E-value: 9.04e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 573 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 649
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 650 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 728
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 729 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 808
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360882 809 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 875
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
525-869 3.88e-118

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 379.88  E-value: 3.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 525 LLVHRDSIFRSSCEIVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 602
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 603 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 682
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 683 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 761
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 762 DVNDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 841
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1720360882 842 TSSTCINMLKLPEYPSKEILKDRLLVAL 869
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-222 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDA 132
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 133 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGY 211
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDNDGKTALDLAAENGN 231

                         170
                  ....*....|.
gi 1720360882 212 GQTCEVLIQYH 222
Cdd:COG0666   232 LEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 1.81e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  72 LHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVtDVDVEDaMGQTALHVACQNGHKTTVQ 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720360882 152 CLLDSGADINRPN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-223 1.98e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 1.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  32 YTLMPMVMADQHSCGSV-ECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLLEYSADVNICNNEGLTAIHWL 108
Cdd:PHA03100   69 STPLHYLSNIKYNLTDVkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 109 AVNGRTEL--LHDLVQHVTDVDVedamgqtalhvacqnghKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQIL 186
Cdd:PHA03100  149 LESNKIDLkiLKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720360882 187 LLRGAKY-LPDKNGVTPLDLCVQGGYGQTCEVLIQYHP 223
Cdd:PHA03100  212 LDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 70-191 1.41e-09

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: 61.57  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  70 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTELLHDLVQHVTDVdVEDAM------GQTALHVA 141
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360882 142 CQNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 191
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-161 3.92e-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: 44.12  E-value: 3.92e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720360882  133 MGQTALHVACQNGHKTTVQCLLDSGADIN 161
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 ...
 524-873 1.05e-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: 472.82  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 524 ILLVHRDSIFRSSCEIVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 601
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 602 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 681
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 682 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 760
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 761 IDVNDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 840
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1720360882 841 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 873
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 549-872 1.95e-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: 401.61  E-value: 1.95e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  549 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 626
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  627 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 704
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  705 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWIKNTEYTSGYEREDPVIQ 784
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  785 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 864
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1720360882  865 LLVALHCG 872
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 573-875 9.04e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.20  E-value: 9.04e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 573 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 649
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 650 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 728
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 729 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 808
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360882 809 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 875
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
525-869 3.88e-118

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 379.88  E-value: 3.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 525 LLVHRDSIFRSSCEIVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 602
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 603 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 682
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 683 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 761
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 762 DVNDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 841
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1720360882 842 TSSTCINMLKLPEYPSKEILKDRLLVAL 869
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-222 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDA 132
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 133 MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGY 211
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDNDGKTALDLAAENGN 231

                         170
                  ....*....|.
gi 1720360882 212 GQTCEVLIQYH 222
Cdd:COG0666   232 LEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
46-219 5.80e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 5.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  46 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVT 125
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 126 DVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLD 204
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALL 257

                         170
                  ....*....|....*
gi 1720360882 205 LCVQGGYGQTCEVLI 219
Cdd:COG0666   258 LAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-221 2.37e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  51 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVE 130
Cdd:COG0666    37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 131 DAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQG 209
Cdd:COG0666   117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADvNARDNDGETPLHLAAEN 196

                         170
                  ....*....|..
gi 1720360882 210 GYGQTCEVLIQY 221
Cdd:COG0666   197 GHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
46-198 7.47e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 7.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  46 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVT 125
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360882 126 DVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKN 198
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
46-171 1.62e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  46 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVT 125
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720360882 126 DVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPL 171
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-221 2.13e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  51 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVE 130
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 131 DAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQG 209
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADvNAQDNDGNTPLHLAAAN 163

                         170
                  ....*....|..
gi 1720360882 210 GYGQTCEVLIQY 221
Cdd:COG0666   164 GNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 1.81e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  72 LHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVtDVDVEDaMGQTALHVACQNGHKTTVQ 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720360882 152 CLLDSGADINRPN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-223 1.98e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 1.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  32 YTLMPMVMADQHSCGSV-ECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLLEYSADVNICNNEGLTAIHWL 108
Cdd:PHA03100   69 STPLHYLSNIKYNLTDVkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 109 AVNGRTEL--LHDLVQHVTDVDVedamgqtalhvacqnghKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQIL 186
Cdd:PHA03100  149 LESNKIDLkiLKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720360882 187 LLRGAKY-LPDKNGVTPLDLCVQGGYGQTCEVLIQYHP 223
Cdd:PHA03100  212 LDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-193 4.88e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 4.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 105 IHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSgADINRPNvSGATPLYFACSHGQRDTAQ 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 1720360882 185 ILLLRGAKY 193
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-171 6.38e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  47 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC---MSKLLEYSADVN---ICnneGLTAIHWLAVNGRTE-LLHD 119
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNapeRC---GFTPLHLYLYNATTLdVIKL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720360882 120 LVQHVTDVDVEDAMGQTALHVAC--QNGHKTTVQCLLDSGADINRPNVSGATPL 171
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-221 1.60e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 138 LHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDkNGVTPLDLCVQGGYGQTCEV 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1720360882 218 LIQY 221
Cdd:pfam12796  80 LLEK 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-204 6.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 6.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  46 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVT 125
Cdd:PHA02874  135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 126 DVDVEDAMGQTALHVACQngHKTTVQCLLDSGADINRPNVSGATPLYFA----CShgqRDTAQILLLRGAKY-LPDKNGV 200
Cdd:PHA02874  215 HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADIsIKDNKGE 289


                  ....
gi 1720360882 201 TPLD 204
Cdd:PHA02874  290 NPID 293
PHA03095 PHA03095
ankyrin-like protein; Provisional
 53-207 8.36e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNgqKKCMSKLLEY--SADVNICN--NEGLTAIHWLAVNGRT--ELLHDLVQHVTD 126
Cdd:PHA03095  137 LLLRKGADVNALDLYGMTPLAVLLKS--RNANVELLRLliDAGADVYAvdDRFRSLLHHHLQSFKPraRIVRELIRAGCD 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 127 VDVEDAMGQTALHVA-----CQNGHkttVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLP-DKNGV 200
Cdd:PHA03095  215 PAATDMLGNTPLHSMatgssCKRSL---VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAvSSDGN 291


                  ....*..
gi 1720360882 201 TPLDLCV 207
Cdd:PHA03095  292 TPLSLMV 298
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-221 8.52e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 8.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  47 SVECLVLLLKKGANPNYQDisGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTD 126
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 127 VDVEDAMGQTALHVACQNGHKTTVQCLLDSGADIN----RPNVsgaTPLYFACSHGQRDTAQILLLRGAkylpDKNGVTp 202
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyfgkNGCV---AALCYAIENNKIDIVRLFIKRGA----DCNIMF- 232

                         170
                  ....*....|....*....
gi 1720360882 203 ldlCVQGGYGQTCEVLIQY 221
Cdd:PHA02875  233 ---MIEGEECTILDMICNM 248
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 53-203 1.37e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLA-----------VNGRTELLHD-- 119
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiIDNRSNINKNdl 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 120 -LVQHVTDVDVE---------------DAMGQTALHVACQNGHKTT-VQCLLDSGADINRPNVSGATPLYFACSHGQrDT 182
Cdd:PHA02876  243 sLLKAIRNEDLEtslllydagfsvnsiDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGY-DT 321

                         170       180
                  ....*....|....*....|....
gi 1720360882 183 AQI--LLLRGAKY-LPDKNGVTPL 203
Cdd:PHA02876  322 ENIrtLIMLGADVnAADRLYITPL 345
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-208 8.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 8.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  54 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAM 133
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360882 134 GQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHgQRDTAQILLLRGAKYLPDKNGVTPLDLCVQ 208
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 33-203 2.42e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.99  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  33 TLMPMVmaDQHSCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKK------------------CMSK-----LLE 89
Cdd:PHA02874   35 TTTPLI--DAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  90 YSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGAT 169
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720360882 170 PLYFACSHGQRDTAQILLLRGAKYLPD-KNGVTPL 203
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-253 2.74e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 2.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  54 LLKKGANPNYQDISGCTPLHLAARNG-----------------------------------QKKCMSKLLEYSADVNICN 98
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGydtenirtlimlgadvnaadrlyitplhqastldrNKDIVITLLELGANVNARD 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  99 NEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVA-CQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSH 177
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKK 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 178 GQR-DTAQILLLRGAkylpDKNGVTPLD---LCVQGGYGQTCEVLIQYHPRLFQTIVqmtQNEDLRENM--LRQVLQHLS 251
Cdd:PHA02876  453 NCKlDVIEMLLDNGA----DVNAINIQNqypLLIALEYHGIVNILLHYGAELRDSRV---LHKSLNDNMfsFRYIIAHIC 525


                  ..
gi 1720360882 252 QQ 253
Cdd:PHA02876  526 IQ 527
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-164 1.35e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  54 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIhWLAV----------------------- 110
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAIsakhhkifrilyhfasisdphaa 622

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360882 111 ---------NGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPN 164
Cdd:PLN03192  623 gdllctaakRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-178 3.55e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  47 SVECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNG--RTELLHDLVQ 122
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLI 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360882 123 HVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHG 178
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-192 2.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  49 ECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWlAVNGRTELL--HDLVQHVTD 126
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMsvKTLIDRGAN 434

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360882 127 VDVEDAMGQTALHVACQNGHKTTV-QCLLDSGADINRPNVSGATPLYFACshGQRDTAQILLLRGAK 192
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNCKLDViEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 2.97e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720360882 136 TALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 39-219 5.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  39 MADQHSCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNG---RTE 115
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdvkAVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 116 LLHDLVQHVTDVDVEDamGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL-LRGAKYL 194
Cdd:PHA02875   86 ELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIdHKACLDI 163

                         170       180
                  ....*....|....*....|....*
gi 1720360882 195 PDKNGVTPLDLCVQGGYGQTCEVLI 219
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-242 6.53e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 6.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  53 LLLKKGANPNYQDI-SGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVED 131
Cdd:PHA02878  152 LLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 132 AMGQTALHVA---CQNghKTTVQCLLDSGADIN-RPNVSGATPLYFACsHGQRDTAqiLLLrgaKYLPDKNGV-----TP 202
Cdd:PHA02878  232 KCGNTPLHISvgyCKD--YDILKLLLEHGVDVNaKSYILGLTALHSSI-KSERKLK--LLL---EYGADINSLnsyklTP 303

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720360882 203 LDLCVQGGYGQTCEVLIQYHPRLFQTIVQMTQN-EDLRENM 242
Cdd:PHA02878  304 LSSAVKQYLCINIGRILISNICLLKRIKPDIKNsEGFIDNM 344
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 70-191 1.41e-09

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: 61.57  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  70 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTELLHDLVQHVTDVdVEDAM------GQTALHVA 141
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360882 142 CQNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 191
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-154 3.33e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720360882 101 GLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLL 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-218 3.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  54 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL----------EYSADVNICNNEGLTAIHWLAVNG----------- 112
Cdd:PHA02878   56 LLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsinkcsvfyTLVAIKDAFNNRNVEIFKIILTNRykniqtidlvy 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 113 ----------RTELLHDLVQHVTDVDVEDA-MGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRD 181
Cdd:PHA02878  136 idkkskddiiEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720360882 182 TAQILLLRGAKY-LPDKNGVTPLDLCVqgGYGQTCEVL 218
Cdd:PHA02878  216 IVHILLENGASTdARDKCGNTPLHISV--GYCKDYDIL 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-227 4.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 130 EDAMGQTALHVA----CQ---NGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVT 201
Cdd:PTZ00322   71 EEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDKDGKT 150

                          90       100
                  ....*....|....*....|....*.
gi 1720360882 202 PLDLCVQGGYGQTCEVLIQYHPRLFQ 227
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHSQCHFE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-88 2.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720360882  46 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL 88
Cdd:pfam13637  12 GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-187 4.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 108 LAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 187
Cdd:PTZ00322   89 LAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-129 1.52e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.52e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDV 129
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 108-186 1.53e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 1.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360882 108 LAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQIL 186
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_4 pfam13637
Ankyrin repeats (many copies);
70-121 1.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720360882  70 TPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLV 121
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-123 3.75e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 3.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQH 123
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
53-106 6.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIH 106
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 54-208 2.23e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.21  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  54 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGR--TELLHDLVQHVTDVD--- 128
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnsv 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 129 ------------------------------VEDAMGQTALH--VACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACS 176
Cdd:PHA02946  138 deegcgpllactdpservfkkimsigfearIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720360882 177 HGQRDTAQILLLRGAKYLPDKN--GVTPLDLCVQ 208
Cdd:PHA02946  218 KTVKNVDIINLLLPSTDVNKQNkfGDSPLTLLIK 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-191 2.57e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882   3 RAMEQLNRL-TRSLRRARTVElPEDNETAVYTLMpmvmadQHSCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQK 81
Cdd:PLN03192  466 KTLSQLLRLkTSTLIEAMQTR-QEDNVVILKNFL------QHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNA 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  82 KCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVACQNGHKTT------------ 149
Cdd:PLN03192  539 ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrilyhfasisd 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360882 150 ------VQC-------------LLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 191
Cdd:PLN03192  619 phaagdLLCtaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-99 3.25e-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: 44.20  E-value: 3.25e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720360882  68 GCTPLHLAA-RNGQKKCMSKLLEYSADVNICNN 99
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-161 3.92e-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: 44.12  E-value: 3.92e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720360882  133 MGQTALHVACQNGHKTTVQCLLDSGADIN 161
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 1.23e-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: 42.57  E-value: 1.23e-05
                           10        20
                   ....*....|....*....|....*....
gi 1720360882   68 GCTPLHLAARNGQKKCMSKLLEYSADVNI 96
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-164 1.78e-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: 42.28  E-value: 1.78e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720360882 134 GQTALHVAC-QNGHKTTVQCLLDSGADINRPN 164
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-164 3.82e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  47 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQK-----KCMSKLLEYSADVNICNNEGLTAIHWLAVNG---RTELLH 118
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720360882 119 DLVQHVTDVDVEDAMGQTALHVACQNGHKT---TVQCLLDSGADINRPN 164
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 46-220 4.18e-05

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: 47.31  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  46 GSVECLVLLLK-KGANPNYQDISGCTPLHLAARNGQKKCMSKLLEysADVNICNN-------EGLTAIHWLAVNGRTELL 117
Cdd:cd22192    28 NDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIAVVNQNLNLV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882 118 HDLVQHVTDVDVEDAMG------QTAL-----HV----ACQnGHKTTVQCLLDSGADINRPNVSGATPLY---------F 173
Cdd:cd22192   106 RELIARGADVVSPRATGtffrpgPKNLiyygeHPlsfaACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktF 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720360882 174 AC-------SHGQRDTAQILLLrgakyLPDKNGVTPLDLCVQGGYGQTCEVLIQ 220
Cdd:cd22192   185 ACqmydlilSYDKEDDLQPLDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 134-161 6.05e-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: 40.70  E-value: 6.05e-05
                          10        20
                  ....*....|....*....|....*...
gi 1720360882 134 GQTALHVACQNGHKTTVQCLLDSGADIN 161
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 2.11e-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: 39.16  E-value: 2.11e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720360882  68 GCTPLHLAARNGQKKCMSKLLEYSADVNI 96
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-206 2.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360882 153 LLDSG-ADINRPNVSGATPLYFACSHGQRDTAQILLLRGA-KYLPDKNGVTPLDLC 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 2.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360882 120 LVQHVT-DVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFA 174
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 15-105 7.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360882  15 LRRARTVELPEDNETAVYTlMPMVMADQhsCGSVECLVLLLKKGANPN-YQDISGCTPLHLAARNGQKKCMSKLLEYSAD 93
Cdd:PHA02884   53 LKLGADPEAPFPLSENSKT-NPLIYAID--CDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGAD 129

                          90
                  ....*....|..
gi 1720360882  94 VNICNNEGLTAI 105
Cdd:PHA02884  130 INIQTNDMVTPI 141
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-99 1.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720360882  53 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNN 99
Cdd:PHA03100  210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_5 pfam13857
Ankyrin repeats (many copies);
87-141 6.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360882  87 LLEY-SADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTDVDVEDAMGQTALHVA 141
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-105 8.24e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 8.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360882  38 VMADQHSCGSVecLVL-LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAI 105
Cdd:PHA03095  228 SMATGSSCKRS--LVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_5 pfam13857
Ankyrin repeats (many copies);
44-75 9.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.56e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720360882  44 SCGSVECLVLLLKKGANPNYQDISGCTPLHLA 75
Cdd:pfam13857  25 KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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