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Conserved domains on  [gi|1007360490|ref|NP_001308012|]
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E3 ubiquitin-protein ligase HACE1 isoform c [Homo sapiens]

Protein Classification

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

ANKYR and HECTc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 520-869 1.18e-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: 1.18e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 520 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 597
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 598 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 677
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 678 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 756
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 757 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 836
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1007360490 837 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 869
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-215 1.59e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  83 LLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 163 GATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLI 215
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLL 272
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 520-869 1.18e-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: 1.18e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 520 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 597
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 598 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 677
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 678 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 756
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 757 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 836
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1007360490 837 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 869
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 545-868 2.88e-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: 401.23  E-value: 2.88e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  545 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 622
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  623 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 700
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  701 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 780
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  781 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 860
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1007360490  861 LLVALHCG 868
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 569-871 3.09e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.65  E-value: 3.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 569 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 645
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 646 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 724
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 725 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 804
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007360490 805 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 871
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
521-865 9.64e-117

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 376.03  E-value: 9.64e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 521 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 598
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 599 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 678
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 679 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 757
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 758 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 837
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1007360490 838 TSSTCINMLKLPEYPSKEILKDRLLVAL 865
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-215 1.59e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  83 LLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 163 GATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLI 215
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-160 1.91e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  35 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltaihwlavngrtellh 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1007360490 115 dlvqhvsdvdvedamGQTALHVACQNGHKTTVQCLLDSGADINRPN 160
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-187 1.63e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   1 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 72
Cdd:PHA03100   37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  73 RN--GQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTEL--LHDLVQHVSDVDVE----------------DAMGQT 132
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKnrvnyllsygvpinikDVYGFT 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1007360490 133 ALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 187
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-187 1.30e-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: 61.95  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  66 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTELLHDLVQHVSDVdVEDAM------GQTALHVA 137
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 138 CQNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 187
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-157 5.03e-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: 43.73  E-value: 5.03e-06
                           10        20
                   ....*....|....*....|....*....
gi 1007360490  129 MGQTALHVACQNGHKTTVQCLLDSGADIN 157
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 ...
 520-869 1.18e-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: 1.18e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 520 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 597
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 598 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 677
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 678 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 756
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 757 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 836
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1007360490 837 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 869
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 545-868 2.88e-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: 401.23  E-value: 2.88e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  545 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 622
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  623 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 700
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  701 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 780
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  781 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 860
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1007360490  861 LLVALHCG 868
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 569-871 3.09e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.65  E-value: 3.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 569 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 645
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 646 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 724
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 725 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 804
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007360490 805 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 871
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
521-865 9.64e-117

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 376.03  E-value: 9.64e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 521 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 598
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 599 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 678
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 679 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 757
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 758 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 837
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1007360490 838 TSSTCINMLKLPEYPSKEILKDRLLVAL 865
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-215 1.59e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  83 LLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 163 GATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLI 215
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-218 5.23e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 5.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  83 LLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1007360490 163 GATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYH 218
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADvNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-194 5.79e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 5.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   4 VMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKL 83
Cdd:COG0666    95 ARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  84 LEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSG 163
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1007360490 164 ATPLYFACSHGQRDTAQILLLRGAKYLPDKN 194
Cdd:COG0666   253 LTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-217 7.42e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 7.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  15 LLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICN 94
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  95 NEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHG 174
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1007360490 175 QRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 217
Cdd:COG0666   165 NLEIVKLLLEAGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-167 7.58e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 7.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  14 ELLSNSKFDVNYAfGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNIC 93
Cdd:COG0666   137 KLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007360490  94 NNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPL 167
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-217 4.06e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 4.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  47 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVE 126
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 127 DAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQG 205
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADvNAQDNDGNTPLHLAAAN 163

                         170
                  ....*....|..
gi 1007360490 206 GYGETCEVLIQY 217
Cdd:COG0666   164 GNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-160 1.91e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  35 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltaihwlavngrtellh 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1007360490 115 dlvqhvsdvdvedamGQTALHVACQNGHKTTVQCLLDSGADINRPN 160
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-187 1.63e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   1 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 72
Cdd:PHA03100   37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  73 RN--GQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTEL--LHDLVQHVSDVDVE----------------DAMGQT 132
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKnrvnyllsygvpinikDVYGFT 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1007360490 133 ALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 187
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-167 5.79e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 5.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  43 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC---MSKLLEYSADVN---ICnneGLTAIHWLAVNGRTE-LLHD 115
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNapeRC---GFTPLHLYLYNATTLdVIKL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 116 LVQHVSDVDVEDAMGQTALHVAC--QNGHKTTVQCLLDSGADINRPNVSGATPL 167
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-189 5.90e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 5.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 101 IHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSgADINRPNvSGATPLYFACSHGQRDTAQ 180
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 1007360490 181 ILLLRGAKY 189
Cdd:pfam12796  79 LLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
134-217 3.77e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 134 LHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDkNGVTPLDLCVQGGYGETCEV 213
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1007360490 214 LIQY 217
Cdd:pfam12796  80 LLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-203 5.15e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 5.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  22 DVNYAfGRVKRSLLHI-----AANCGSVEclvLLLKKGANPNYQDISGCTPLHLAARNgqKKCMSKLLEY--SADVNICN 94
Cdd:PHA03095  109 DVNAK-DKVGRTPLHVylsgfNINPKVIR---LLLRKGADVNALDLYGMTPLAVLLKS--RNANVELLRLliDAGADVYA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  95 --NEGLTAIHWLAVNGRT--ELLHDLVQHVSDVDVEDAMGQTALHVA-----CQNGHkttVQCLLDSGADINRPNVSGAT 165
Cdd:PHA03095  183 vdDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRSL---VLPLLIAGISINARNRYGQT 259

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1007360490 166 PLYFACSHGQRDTAQILLLRGAKYLP-DKNGVTPLDLCV 203
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAvSSDGNTPLSLMV 298
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 2-217 6.52e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 6.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   2 PMVMADQHRSVS--ELLSNSKFDVNYAFGRVkRSLLHIAANCGSVECLVLLLKKGANPN---YQDisGCTPLHLAARNGQ 76
Cdd:PHA02875   38 PIKLAMKFRDSEaiKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  77 KKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADI 156
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007360490 157 N----RPNVsgaTPLYFACSHGQRDTAQILLLRGAkylpDKNGVTpldlCVQGGYGETCEVLIQY 217
Cdd:PHA02875  195 DyfgkNGCV---AALCYAIENNKIDIVRLFIKRGA----DCNIMF----MIEGEECTILDMICNM 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-227 6.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 6.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  31 KRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQ-----KKCMSKLLEYSADVNICNNEGLTAIHWLA 105
Cdd:PHA03100   35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 106 VN--GRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGH------------------KTTVQCLLDSGADINRPNVSGAT 165
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidlkilkllidkgvdinaKNRVNYLLSYGVPINIKDVYGFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007360490 166 PLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 227
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 2-249 7.56e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   2 PMVMADQHRSVSEL---LSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAAR-NGQK 77
Cdd:PHA02876  276 PLHHASQAPSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNK 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  78 KCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVA-CQNGHKTTVQCLLDSGADI 156
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANV 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 157 NRPNVSGATPLYFACSHGQR-DTAQILLLRGAkylpDKNGVTPLD---LCVQGGYGETCEVLIQYHPRLFQTIIqmtQNE 232
Cdd:PHA02876  436 NSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA----DVNAINIQNqypLLIALEYHGIVNILLHYGAELRDSRV---LHK 508

                         250
                  ....*....|....*....
gi 1007360490 233 DLRENM--LRQVLEHLSQQ 249
Cdd:PHA02876  509 SLNDNMfsFRYIIAHICIQ 527
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-199 9.14e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  49 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLA-----------VNGRTELLHD-- 115
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiIDNRSNINKNdl 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 116 -LVQHVSDVDVE---------------DAMGQTALHVACQNGHKTT-VQCLLDSGADINRPNVSGATPLYFACSHGQrDT 178
Cdd:PHA02876  243 sLLKAIRNEDLEtslllydagfsvnsiDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGY-DT 321

                         170       180
                  ....*....|....*....|....
gi 1007360490 179 AQI--LLLRGAKY-LPDKNGVTPL 199
Cdd:PHA02876  322 ENIrtLIMLGADVnAADRLYITPL 345
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 12-204 4.58e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  12 VSELLSNSKFDVNYAFGRVKRSLL---HIAAN-------------------CGSVECLVLLLKKGANPNYQDISGCTPLH 69
Cdd:PHA02874   50 IVELFIKHGADINHINTKIPHPLLtaiKIGAHdiikllidngvdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLH 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  70 LAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCL 149
Cdd:PHA02874  130 YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1007360490 150 LDSGADINRPNVSGATPLYFACSHgQRDTAQILLLRGAKYLPDKNGVTPLDLCVQ 204
Cdd:PHA02874  210 IDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-199 4.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  38 AANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKK------------------CMSK-----LLEYSADVNICN 94
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILDCGIDVNIKD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  95 NEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHG 174
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         170       180
                  ....*....|....*....|....*.
gi 1007360490 175 QRDTAQILLLRGAKYLPD-KNGVTPL 199
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKcKNGFTPL 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-174 4.33e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   9 HRSVSELLSNSKFDVN--YAFGRVKRSLLHIAANCgSVECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLL 84
Cdd:PHA03095  131 NPKVIRLLLRKGADVNalDLYGMTPLAVLLKSRNA-NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  85 EYSADVNICNNEGLTAIHWLAVNG--RTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:PHA03095  210 RAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                         170
                  ....*....|..
gi 1007360490 163 GATPLYFACSHG 174
Cdd:PHA03095  290 GNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-92 4.43e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490   4 VMADQHRSVSELLSN-SKFDVNYAFGRvkrSLLHIAANCGSVECLVLLLKKgANPNYQDiSGCTPLHLAARNGQKKCMSK 82
Cdd:pfam12796   5 AKNGNLELVKLLLENgADANLQDKNGR---TALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1007360490  83 LLEYSADVNI 92
Cdd:pfam12796  80 LLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-187 4.78e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  38 AANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIhWLAVNGRTELLHDLV 117
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 118 QHVSDVDVEDAMGQTaLHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 187
Cdd:PLN03192  611 YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 12-170 1.12e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  12 VSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN 91
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  92 ICNNEGLTAIHWLAvnGRT---ELLHDLVQHVSDVDVEDA-MGQTALHVACQNGHKTTVqcLLDSGADINRPNVSGATPL 167
Cdd:PHA02878  229 ARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKL--LLEYGADINSLNSYKLTPL 304


                  ...
gi 1007360490 168 YFA 170
Cdd:PHA02878  305 SSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-84 5.40e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.40e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1007360490  32 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL 84
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-215 3.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  42 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNG---RTELLHDLVQ 118
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdvkAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 119 HVSDVDVEDamGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL-LRGAKYLPDKNGVT 197
Cdd:PHA02875   93 FADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIdHKACLDIEDCCGCT 170

                         170
                  ....*....|....*...
gi 1007360490 198 PLDLCVQGGYGETCEVLI 215
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
132-183 3.60e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 3.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1007360490 132 TALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 183
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-277 4.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 4.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  35 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL----------EYSADVNICNNEGLTAIHWL 104
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsinkcsvfyTLVAIKDAFNNRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 105 AVNG---------------------RTELLHDLVQHVSDVDVEDA-MGQTALHVACQNGHKTTVQCLLDSGADINRPNVS 162
Cdd:PHA02878  121 LTNRykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 163 GATPLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVqgGYGETCEVLiqyhprlfQTIIQMTQNEDLRENMLRQ 241
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISV--GYCKDYDIL--------KLLLEHGVDVNAKSYILGL 270

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1007360490 242 VLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSS 277
Cdd:PHA02878  271 TALHSSIKSERKLKLLLEYGADINSLNSYKLTPLSS 306
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-215 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  66 TPLHLAARNGQKKCMSKLLEYSADVNICN----NEGLTAI--------HWLAVNG-----------RTELLHDLVQHVSD 122
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAIkigahdiiKLLIDNGvdtsilpipciEKDMIKTILDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 123 VDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAkYL--PDKNGVTPLD 200
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YAnvKDNNGESPLH 195

                         170
                  ....*....|....*
gi 1007360490 201 LCVQGGYGETCEVLI 215
Cdd:PHA02874  196 NAAEYGDYACIKLLI 210
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 126-223 1.18e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 126 EDAMGQTALHVA----CQ---NGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVT 197
Cdd:PTZ00322   71 EEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDKDGKT 150

                          90       100
                  ....*....|....*....|....*.
gi 1007360490 198 PLDLCVQGGYGETCEVLIQYHPRLFQ 223
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHSQCHFE 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-187 1.30e-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: 61.95  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  66 TPLHLAARNGQKKCMSKLLEySADVNICNNEGL--TAIHWLAVNGRTELLHDLVQHVSDVdVEDAM------GQTALHVA 137
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLK-CPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007360490 138 CQNGHKTTVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 187
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-150 3.52e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490  97 GLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLL 150
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-183 2.74e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 104 LAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL 183
Cdd:PTZ00322   89 LAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-119 1.09e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  34 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELL 113
Cdd:PTZ00322   86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*.
gi 1007360490 114 HDLVQH 119
Cdd:PTZ00322  165 QLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-258 1.33e-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: 55.40  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  29 RVKRSLLHIAANCGSVECLVLLLK-KGANPNYQDISGCTPLHLAARNGQKKCMSKLLEysADVNICNN-------EGLTA 100
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 101 IHWLAVNGRTELLHDLVQHVSDVDVEDAMG------QTAL-----HV----ACQnGHKTTVQCLLDSGADINRPNVSGAT 165
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLiyygeHPlsfaACV-GNEEIVRLLIEHGADIRAQDSLGNT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 166 PLY---------FAC-------SHGQRDTAQILLLrgakyLPDKNGVTPLDLCVQGGYGETCEVLIQYHpRLFQ------ 223
Cdd:cd22192   172 VLHilvlqpnktFACqmydlilSYDKEDDLQPLDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQKR-RHIQwtygpl 245

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1007360490 224 --TIIQMTQNEDLRENMlrQVLEHLSQQSESQYLKIL 258
Cdd:cd22192   246 tsTLYDLTEIDSWGDEQ--SVLELIVSSKKREARKIL 280
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 11-125 1.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  11 SVSELLSNSKFDVNyAFGRVKrsllhiaancgsveclvLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADV 90
Cdd:PHA03100  157 KILKLLIDKGVDIN-AKNRVN-----------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1007360490  91 NICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDV 125
Cdd:PHA03100  219 NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-117 2.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1007360490  66 TPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLV 117
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
15-71 5.53e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1007360490  15 LLSNSKFDVNYaFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 71
Cdd:pfam13857   1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-102 6.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007360490  49 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIH 102
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 50-204 1.61e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.59  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  50 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGR--TELLHDLVQHVSDVD--- 124
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnsv 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490 125 ------------------------------VEDAMGQTALH--VACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACS 172
Cdd:PHA02946  138 deegcgpllactdpservfkkimsigfearIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1007360490 173 HGQRDTAQILLLRGAKYLPDKN--GVTPLDLCVQ 204
Cdd:PHA02946  218 KTVKNVDIINLLLPSTDVNKQNkfGDSPLTLLIK 251
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-95 3.54e-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: 3.54e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1007360490  64 GCTPLHLAA-RNGQKKCMSKLLEYSADVNICNN 95
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-157 5.03e-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: 43.73  E-value: 5.03e-06
                           10        20
                   ....*....|....*....|....*....
gi 1007360490  129 MGQTALHVACQNGHKTTVQCLLDSGADIN 157
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-92 1.52e-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: 1.52e-05
                           10        20
                   ....*....|....*....|....*....
gi 1007360490   64 GCTPLHLAARNGQKKCMSKLLEYSADVNI 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 130-160 1.97e-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: 1.97e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1007360490 130 GQTALHVAC-QNGHKTTVQCLLDSGADINRPN 160
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 43-160 5.13e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  43 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQK-----KCMSKLLEYSADVNICNNEGLTAIHWLAVNG---RTELLH 114
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1007360490 115 DLVQHVSDVDVEDAMGQTALHVACQNGHKT---TVQCLLDSGADINRPN 160
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 130-157 6.98e-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: 6.98e-05
                          10        20
                  ....*....|....*....|....*...
gi 1007360490 130 GQTALHVACQNGHKTTVQCLLDSGADIN 157
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
116-170 1.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007360490 116 LVQHVS-DVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFA 170
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-87 1.62e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007360490  32 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYS 87
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-92 2.43e-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: 2.43e-04
                          10        20
                  ....*....|....*....|....*....
gi 1007360490  64 GCTPLHLAARNGQKKCMSKLLEYSADVNI 92
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
149-202 2.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007360490 149 LLDSG-ADINRPNVSGATPLYFACSHGQRDTAQILLLRGA-KYLPDKNGVTPLDLC 202
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 32-61 3.47e-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: 38.81  E-value: 3.47e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1007360490  32 RSLLHIAA-NCGSVECLVLLLKKGANPNYQD 61
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 30-101 6.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 6.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007360490  30 VKRSLLHIAANCGSVECLVLLLKKGANPN-YQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAI 101
Cdd:PHA02884   69 SKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-59 1.18e-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: 37.18  E-value: 1.18e-03
                           10        20
                   ....*....|....*....|....*...
gi 1007360490   32 RSLLHIAANCGSVECLVLLLKKGANPNY 59
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-137 1.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007360490  83 LLEY-SADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVA 137
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 22-185 9.75e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.48  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  22 DVNYAFGRVKRSLLHIAA---NCGSVECLVLLL---------KKGANPNYQD--ISGCTPLHLAARNGQKKCMSKLLEYS 87
Cdd:cd21882    17 DSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLeaapdsgnpKELVNAPCTDefYQGQTALHIAIENRNLNLVRLLVENG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007360490  88 ADVNI-------------CNNEGLTAIHWLAVNGRTELLHDLVQH---VSDVDVEDAMGQTALHVACQNGHKTTVQC--- 148
Cdd:cd21882    97 ADVSAratgrffrkspgnLFYFGELPLSLAACTNQEEIVRLLLENgaqPAALEAQDSLGNTVLHALVLQADNTPENSafv 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1007360490 149 ------LLDSGADINR-------PNVSGATPLYFACSHGQRDTAQILLLR 185
Cdd:cd21882   177 cqmynlLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHILQR 226
 
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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