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Conserved domains on  [gi|1182918615|ref|NP_001337483|]
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E3 ubiquitin-protein ligase HACE1 isoform e [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 ...
 476-825 1.21e-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: 471.28  E-value: 1.21e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 476 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 553
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 554 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 633
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 634 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 712
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 713 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 792
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182918615 793 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 825
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-174 6.82e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 6.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  83 LLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKN 150
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPlhlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDND 218

                         170       180
                  ....*....|....*....|....
gi 1182918615 151 GVTPLDLCVQGGYGETCEVLIQYH 174
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAG 242
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 476-825 1.21e-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: 471.28  E-value: 1.21e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 476 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 553
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 554 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 633
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 634 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 712
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 713 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 792
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182918615 793 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 825
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 501-824 2.99e-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: 399.69  E-value: 2.99e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  501 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 578
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  579 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 656
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  657 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 736
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  737 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 816
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1182918615  817 LLVALHCG 824
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 525-827 5.20e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 382.73  E-value: 5.20e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 525 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 601
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 602 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 680
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 681 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 760
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182918615 761 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 827
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
477-821 1.38e-116

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 374.49  E-value: 1.38e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 477 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 554
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 555 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 634
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 635 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 713
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 714 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 793
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1182918615 794 TSSTCINMLKLPEYPSKEILKDRLLVAL 821
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-174 6.82e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 6.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  83 LLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKN 150
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPlhlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDND 218

                         170       180
                  ....*....|....*....|....
gi 1182918615 151 GVTPLDLCVQGGYGETCEVLIQYH 174
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-145 6.75e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 6.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  35 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltatvqclldsgadinr 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918615 115 pnvsGATPLYFACSHGQRDTAQILLLRGAKY 145
Cdd:pfam12796  61 ----GRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-183 2.46e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   1 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 72
Cdd:PHA03100   37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  73 RN--GQKKCMSKLLEYSADVNICNNEGLTA-----------------------------TVQCLLDSGADINRPNVSGAT 121
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLlhlylesnkidlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182918615 122 PLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 183
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-92 1.11e-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: 1.11e-05
                           10        20
                   ....*....|....*....|....*....
gi 1182918615   64 GCTPLHLAARNGQKKCMSKLLEYSADVNI 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-143 5.58e-04

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: 43.46  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  10 RSVSELLSNSKFDVnYAFGRVKRSLLHIAANCGSVECLVLLLKkgANPN----------YQdisGCTPLHLAARNgqkkc 79
Cdd:cd22192    31 QAIKKLLKCPSCDL-FQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtsdlYQ---GETALHIAVVN----- 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918615  80 msklleysadvnicNNEGLtatVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 143
Cdd:cd22192   100 --------------QNLNL---VRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 476-825 1.21e-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: 471.28  E-value: 1.21e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 476 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 553
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 554 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 633
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 634 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 712
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 713 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 792
Cdd:cd00078   242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1182918615 793 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 825
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 501-824 2.99e-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: 399.69  E-value: 2.99e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  501 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 578
Cdd:smart00119   4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  579 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 656
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  657 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 736
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  737 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 816
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317


                   ....*...
gi 1182918615  817 LLVALHCG 824
Cdd:smart00119 318 LLLAINEG 325
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 525-827 5.20e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 382.73  E-value: 5.20e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 525 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 601
Cdd:pfam00632   2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 602 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 680
Cdd:pfam00632  82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 681 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 760
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182918615 761 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 827
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
477-821 1.38e-116

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 374.49  E-value: 1.38e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 477 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 554
Cdd:COG5021   517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 555 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 634
Cdd:COG5021   597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 635 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 713
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 714 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 793
Cdd:COG5021   757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835

                         330       340
                  ....*....|....*....|....*...
gi 1182918615 794 TSSTCINMLKLPEYPSKEILKDRLLVAL 821
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-174 6.82e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 6.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  83 LLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKN 150
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPlhlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADvNAKDND 218

                         170       180
                  ....*....|....*....|....
gi 1182918615 151 GVTPLDLCVQGGYGETCEVLIQYH 174
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-171 5.06e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   4 VMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKL 83
Cdd:COG0666    95 ARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  84 LEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNG 151
Cdd:COG0666   173 LEAGADVNARDNDGETPlhlaaenghleIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDG 252

                         170       180
                  ....*....|....*....|
gi 1182918615 152 VTPLDLCVQGGYGETCEVLI 171
Cdd:COG0666   253 LTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-173 1.68e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 1.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   3 MVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSK 82
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  83 LLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKN 150
Cdd:COG0666   106 LLEAGADVNARDKDGETPlhlaayngnleIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADvNARDND 185

                         170       180
                  ....*....|....*....|...
gi 1182918615 151 GVTPLDLCVQGGYGETCEVLIQY 173
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-145 6.75e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 6.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  35 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltatvqclldsgadinr 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1182918615 115 pnvsGATPLYFACSHGQRDTAQILLLRGAKY 145
Cdd:pfam12796  61 ----GRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-183 2.46e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   1 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 72
Cdd:PHA03100   37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  73 RN--GQKKCMSKLLEYSADVNICNNEGLTA-----------------------------TVQCLLDSGADINRPNVSGAT 121
Cdd:PHA03100  115 SKksNSYSIVEYLLDNGANVNIKNSDGENLlhlylesnkidlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182918615 122 PLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 183
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-92 2.63e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   4 VMADQHRSVSELLSN-SKFDVNYAFGRvkrSLLHIAANCGSVECLVLLLKKgANPNYQDiSGCTPLHLAARNGQKKCMSK 82
Cdd:pfam12796   5 AKNGNLELVKLLLENgADANLQDKNGR---TALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1182918615  83 LLEYSADVNI 92
Cdd:pfam12796  80 LLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-123 7.68e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 7.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  22 DVNYAfGRVKRSLLHIAANCGSVEC---LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL-EYSADVNICNNEG 97
Cdd:PHA03095   39 DVNFR-GEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGADVNAKDKVG 117

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1182918615  98 LTA-------------TVQCLLDSGADINRPNVSGATPL 123
Cdd:PHA03095  118 RTPlhvylsgfninpkVIRLLLRKGADVNALDLYGMTPL 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-160 1.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  18 NSKFDVNYAFGRVKrSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEG 97
Cdd:PHA02874  112 DCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182918615  98 LT-----------ATVQCLLDSGADINRPNVSGATPLYFACSHgQRDTAQILLLRGAKYLPDKNGVTPLDLCVQ 160
Cdd:PHA02874  191 ESplhnaaeygdyACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAIN 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-84 3.68e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 3.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1182918615  32 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL 84
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-156 7.64e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 7.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  43 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC---MSKLLEYSADVN-------------ICNNEGLtATVQCLL 106
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNapercgftplhlyLYNATTL-DVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1182918615 107 DSGADINRPNVSGATPLYfACSHGQR---DTAQILLLRGAKylP---DKNGVTPLD 156
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLH-VYLSGFNinpKVIRLLLRKGAD--VnalDLYGMTPLA 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-173 2.01e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  10 RSVSELLSNSKF--DVNYAFGRVKrslLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYS 87
Cdd:PHA02875   82 KAVEELLDLGKFadDVFYKDGMTP---LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  88 ADVNICNNEGLT-----------ATVQCLLDSGADIN----RPNVsgaTPLYFACSHGQRDTAQILLLRGAkylpDKNGV 152
Cdd:PHA02875  159 ACLDIEDCCGCTpliiamakgdiAICKMLLDSGANIDyfgkNGCV---AALCYAIENNKIDIVRLFIKRGA----DCNIM 231

                         170       180
                  ....*....|....*....|.
gi 1182918615 153 TpldlCVQGGYGETCEVLIQY 173
Cdd:PHA02875  232 F----MIEGEECTILDMICNM 248
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-159 4.04e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   9 HRSVSELLSNSKFDVN--YAFGRVKRSLLHIAANCgSVECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLL 84
Cdd:PHA03095  131 NPKVIRLLLRKGADVNalDLYGMTPLAVLLKSRNA-NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  85 EYSADVNICNNEGLTAT-------------VQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLP-DKN 150
Cdd:PHA03095  210 RAGCDPAATDMLGNTPLhsmatgssckrslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAvSSD 289


                  ....*....
gi 1182918615 151 GVTPLDLCV 159
Cdd:PHA03095  290 GNTPLSLMV 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-205 1.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  22 DVNyAFGRVKRSLLHIAANCGSVECLVL-LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA 100
Cdd:PHA02876  333 DVN-AADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615 101 ------------TVQCLLDSGADINRPNVSGATPLYFACSHGQR-DTAQILLLRGAkylpDKNGVTPLD---LCVQGGYG 164
Cdd:PHA02876  412 lhfalcgtnpymSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA----DVNAINIQNqypLLIALEYH 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1182918615 165 ETCEVLIQYHPRLFQTIIqmtQNEDLRENM--LRQVLEHLSQQ 205
Cdd:PHA02876  488 GIVNILLHYGAELRDSRV---LHKSLNDNMfsFRYIIAHICIQ 527
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 97-179 1.97e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  97 GLTATVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYHP 175
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                  ....
gi 1182918615 176 RLFQ 179
Cdd:PTZ00322  173 CHFE 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 12-155 4.97e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  12 VSELLSNSKFDVNYAFGRVKRSLL---HIAAN-------------------CGSVECLVLLLKKGANPNYQDISGCTPLH 69
Cdd:PHA02874   50 IVELFIKHGADINHINTKIPHPLLtaiKIGAHdiikllidngvdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLH 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  70 LAARNGQKKCMSKLLEYSADVNICNNEGL----TAT-------VQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQIL 138
Cdd:PHA02874  130 YAIKKGDLESIKMLFEYGADVNIEDDNGCypihIAIkhnffdiIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                         170
                  ....*....|....*...
gi 1182918615 139 LLRGAKYLPD-KNGVTPL 155
Cdd:PHA02874  210 IDHGNHIMNKcKNGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-118 5.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  49 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNV 117
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidTIKAIIDNRSNINKNDL 242


                  .
gi 1182918615 118 S 118
Cdd:PHA02876  243 S 243
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 12-174 1.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  12 VSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN 91
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  92 ICNNEGLT------------ATVQCLLDSGADIN-RPNVSGATPLYFACsHGQRDTAqiLLLrgaKYLPDKNGV-----T 153
Cdd:PHA02878  229 ARDKCGNTplhisvgyckdyDILKLLLEHGVDVNaKSYILGLTALHSSI-KSERKLK--LLL---EYGADINSLnsyklT 302

                         170       180
                  ....*....|....*....|.
gi 1182918615 154 PLDLCVQGGYGETCEVLIQYH 174
Cdd:PHA02878  303 PLSSAVKQYLCINIGRILISN 323
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 32-143 2.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  32 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN-------ICN--NEGLTATV 102
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDphaagdlLCTaaKRNDLTAM 638

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1182918615 103 QCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 143
Cdd:PLN03192  639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank_5 pfam13857
Ankyrin repeats (many copies);
15-71 4.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1182918615  15 LLSNSKFDVNYaFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 71
Cdd:pfam13857   1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-139 6.13e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  34 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNicnnegltatvqcLLDSgadin 113
Cdd:PTZ00322   86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT-------------LLDK----- 146

                          90       100
                  ....*....|....*....|....*.
gi 1182918615 114 rpnvSGATPLYFACSHGQRDTAQILL 139
Cdd:PTZ00322  147 ----DGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-100 1.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1182918615  49 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA 100
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-95 2.27e-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: 44.59  E-value: 2.27e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1182918615  64 GCTPLHLAA-RNGQKKCMSKLLEYSADVNICNN 95
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 33-171 3.73e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  33 SLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN-ICNNEGLT----ATV----- 102
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTplhlATIlkkld 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1182918615 103 --QCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL-LRGAKYLPDKNGVTPLDLCVQGGYGETCEVLI 171
Cdd:PHA02875  117 imKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIdHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-172 3.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  38 AANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNI-----CNNEgltaTVQCLLDSGADI 112
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipcIEKD----MIKTILDCGIDV 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1182918615 113 NRPNVSGATPLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQ 172
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-173 7.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 7.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  42 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSA--DVNICN---------NEGLTATVQCLLDSGA 110
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDieselhdavEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182918615 111 DINrpNV---SGATPLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQY 173
Cdd:PHA02875   93 FAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPdIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-139 9.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 9.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1182918615  66 TPLHLAARNGQKKCMSKLLEysadvnicnnegltatvqclldSGADINRPNVSGATPLYFACSHGQRDTAQILL 139
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLE----------------------KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-92 1.11e-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: 1.11e-05
                           10        20
                   ....*....|....*....|....*....
gi 1182918615   64 GCTPLHLAARNGQKKCMSKLLEYSADVNI 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-130 2.70e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  32 RSLLHIAANcgSV----ECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC--MSKLLEYSADVNICNNEGLT----AT 101
Cdd:PHA03095  188 RSLLHHHLQ--SFkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTplhyAA 265

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1182918615 102 V-------QCLLDSGADINRPNVSGATPLYFACSHG 130
Cdd:PHA03095  266 VfnnpracRRLIALGADINAVSSDGNTPLSLMVRNN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-118 4.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  32 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSadvnICNNEG--------LTATVQ 103
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS----QCHFELganakpdsFTGKPP 191

                          90
                  ....*....|....*
gi 1182918615 104 CLLDSGADINRPNVS 118
Cdd:PTZ00322  192 SLEDSPISSHHPDFS 206
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-155 1.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  12 VSELLSNSKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAA---------------RNGQ 76
Cdd:PHA02876  160 IAEMLLEGGADVN-AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrSNIN 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  77 KKCMS------------KLLEYSA-----DVNICNNEGLTATVQC---------LLDSGADINRPNVSGATPLYFACSHG 130
Cdd:PHA02876  239 KNDLSllkairnedletSLLLYDAgfsvnSIDDCKNTPLHHASQApslsrlvpkLLERGADVNAKNIKGETPLYLMAKNG 318

                         170       180
                  ....*....|....*....|....*...
gi 1182918615 131 QrDTAQI--LLLRGAKY-LPDKNGVTPL 155
Cdd:PHA02876  319 Y-DTENIrtLIMLGADVnAADRLYITPL 345
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-92 1.99e-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: 1.99e-04
                          10        20
                  ....*....|....*....|....*....
gi 1182918615  64 GCTPLHLAARNGQKKCMSKLLEYSADVNI 92
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
105-158 2.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1182918615 105 LLDSG-ADINRPNVSGATPLYFACSHGQRDTAQILLLRGA-KYLPDKNGVTPLDLC 158
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 32-61 2.29e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.29e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1182918615  32 RSLLHIAA-NCGSVECLVLLLKKGANPNYQD 61
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-143 5.58e-04

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: 43.46  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  10 RSVSELLSNSKFDVnYAFGRVKRSLLHIAANCGSVECLVLLLKkgANPN----------YQdisGCTPLHLAARNgqkkc 79
Cdd:cd22192    31 QAIKKLLKCPSCDL-FQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtsdlYQ---GETALHIAVVN----- 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918615  80 msklleysadvnicNNEGLtatVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 143
Cdd:cd22192   100 --------------QNLNL---VRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 50-173 6.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  50 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA----------------TVQCLLDSGADIN 113
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPlhylsnikynltdvkeIVKLLLEYGANVN 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182918615 114 RPNVSGATPLYFACSH--GQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGET--CEVLIQY 173
Cdd:PHA03100  101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANvNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-59 8.94e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.94e-04
                           10        20
                   ....*....|....*....|....*...
gi 1182918615   32 RSLLHIAANCGSVECLVLLLKKGANPNY 59
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-61 1.01e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1182918615   4 VMADQHRSVSELLSNSKFDVNYAfgrvKRSLLHIAANCGSVECLVLLLKKGANPNYQD 61
Cdd:pfam12796  38 AKNGHLEIVKLLLEHADVNLKDN----GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-114 1.88e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  35 LHIAANCGSVECLVL--LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTATVQCLLDSGADI 112
Cdd:PHA03095  226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305


                  ..
gi 1182918615 113 NR 114
Cdd:PHA03095  306 VR 307
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 30-99 2.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 2.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1182918615  30 VKRSLLHIAANCGSVECLVLLLKKGANPN-YQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLT 99
Cdd:PHA02884   69 SKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVT 139
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-100 3.38e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615   1 MPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCM 80
Cdd:COG0666   191 HLAAENGHLEIVKLLLEA-GADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                          90       100
                  ....*....|....*....|
gi 1182918615  81 SKLLEYSADVNICNNEGLTA 100
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTL 288
PHA02798 PHA02798
ankyrin-like protein; Provisional
 43-172 3.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  43 SVECLVLLLKKGANPNYQDISGCTPLhlaarngqkkC--MSKLLEYSADVNIcnnegltatVQCLLDSGADINRPNVSGA 120
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPL----------CtiLSNIKDYKHMLDI---------VKILIENGADINKKNSDGE 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1182918615 121 TPLYFACSHGQRDTAQILLL---RGAK-YLPDKNGVTPLDLCVQGGYG---ETCEVLIQ 172
Cdd:PHA02798  111 TPLYCLLSNGYINNLEILLFmieNGADtTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 32-58 8.59e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 8.59e-03
                          10        20
                  ....*....|....*....|....*..
gi 1182918615  32 RSLLHIAANCGSVECLVLLLKKGANPN 58
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 50-151 8.82e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182918615  50 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA-------------TVQCLLDSGADINRP- 115
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyylsgtddevieRINLLVQYGAKINNSv 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1182918615 116 NVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKNG 151
Cdd:PHA02946  138 DEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFG 173
 
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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