|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
510-859 |
3.42e-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: 3.42e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 510 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 587
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 588 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 667
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 668 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 746
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 747 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 826
Cdd:cd00078 242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316
|
330 340 350
....*....|....*....|....*....|...
gi 1007359986 827 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 859
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
535-858 |
8.43e-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: 8.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 535 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 612
Cdd:smart00119 4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 613 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 690
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 691 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 770
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 771 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 850
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
....*...
gi 1007359986 851 LLVALHCG 858
Cdd:smart00119 318 LLLAINEG 325
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
559-861 |
9.09e-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: 383.11 E-value: 9.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 559 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 635
Cdd:pfam00632 2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 636 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 714
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 715 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 794
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007359986 795 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 861
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
511-855 |
3.90e-116 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 374.10 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 511 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 588
Cdd:COG5021 517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 589 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 668
Cdd:COG5021 597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 669 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 747
Cdd:COG5021 677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 748 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 827
Cdd:COG5021 757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835
|
330 340
....*....|....*....|....*...
gi 1007359986 828 TSSTCINMLKLPEYPSKEILKDRLLVAL 855
Cdd:COG5021 836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
26-208 |
2.87e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.71 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 26 DNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666 49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 106 ARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLL 174
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1007359986 175 RGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYH 208
Cdd:COG0666 208 AGADvNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
69-179 |
7.46e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltatvqclldsgadinr 148
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110
....*....|....*....|....*....|.
gi 1007359986 149 pnvsGATPLYFACSHGQRDTAQILLLRGAKY 179
Cdd:pfam12796 61 ----GRTALHYAARSGHLEIVKLLLEKGADI 87
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
35-217 |
2.04e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 79.32 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 35 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 106
Cdd:PHA03100 37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 107 RN--GQKKCMSKLLEYSADVNICNNEGLTA-----------------------------TVQCLLDSGADINRPNVSGAT 155
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNIKNSDGENLlhlylesnkidlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007359986 156 PLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 217
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
98-126 |
1.12e-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: 1.12e-05
10 20
....*....|....*....|....*....
gi 1007359986 98 GCTPLHLAARNGQKKCMSKLLEYSADVNI 126
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
44-177 |
6.67e-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: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 44 RSVSELLSNSKFDVnYAFGRVKRSLLHIAANCGSVECLVLLLKkgANPN----------YQdisGCTPLHLAARNgqkkc 113
Cdd:cd22192 31 QAIKKLLKCPSCDL-FQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtsdlYQ---GETALHIAVVN----- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007359986 114 msklleysadvnicNNEGLtatVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 177
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 ... |
510-859 |
3.42e-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: 3.42e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 510 ILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMG-QGVVREWFDILSNEIVNPDYALFTQSADGT-TFQPNSNS 587
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSgLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 588 YVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVE 667
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 668 TDV-FGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE 746
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 747 IDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMggsglQNFTIAAVPYTPNLL 826
Cdd:cd00078 242 IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRL 316
|
330 340 350
....*....|....*....|....*....|...
gi 1007359986 827 PTSSTCINMLKLPEYPSKEILKDRLLVALHCGS 859
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
535-858 |
8.43e-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: 8.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 535 KQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYV-NPDHLNYFRFAGQILGLALNHRQ 612
Cdd:smart00119 4 KRVLEIEFEGEEGLdGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 613 LVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWI-LDNDISDLgLELTFS-VETDVFGAMEEVPLKPGGGSILVTQ 690
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSiVLTSEFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 691 NNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQ 770
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 771 WFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGgsglqNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDR 850
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
....*...
gi 1007359986 851 LLVALHCG 858
Cdd:smart00119 318 LLLAINEG 325
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
559-861 |
9.09e-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: 383.11 E-value: 9.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 559 ILSNEIVNPDYALF-TQSADGTTFQPNSNSYVNPDH--LNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQD 635
Cdd:pfam00632 2 LLSKELFDPNYGLFeYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 636 VASIDPEYAKNLQWILDNDISDLG-LELTFSVetDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQIN 714
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 715 AFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGS 794
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007359986 795 SRVPHGGFANimggsgLQNFTIAAVPYT-PNLLPTSSTCINMLKLPEYPSKEILKDRLLVAL-HCGSYG 861
Cdd:pfam00632 240 SRLPVGGFKS------LPKFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIeEGEGFG 302
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
511-855 |
3.90e-116 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 374.10 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 511 LLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGM-GQGVVREWFDILSNEIVNPDYALFT-QSADGTTFQPNSNSY 588
Cdd:COG5021 517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIdAGGLTREWLFLLSKEMFNPDYGLFEyITEDLYTLPINPLSS 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 589 VNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVET 668
Cdd:COG5021 597 INPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 669 DVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPE-I 747
Cdd:COG5021 677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 748 DVSDWIKNTEYtSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLP 827
Cdd:COG5021 757 DIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLP 835
|
330 340
....*....|....*....|....*...
gi 1007359986 828 TSSTCINMLKLPEYPSKEILKDRLLVAL 855
Cdd:COG5021 836 SAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
26-208 |
2.87e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.71 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 26 DNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRvKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666 49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 106 ARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLL 174
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1007359986 175 RGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYH 208
Cdd:COG0666 208 AGADvNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-205 |
1.28e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.15 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 1 MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVEC 80
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN-ARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 81 LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRP 149
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPlhlaaenghleIVKLLLEAGADVNAK 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1007359986 150 NVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLI 205
Cdd:COG0666 216 DNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
26-207 |
1.54e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.29 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 26 DNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 106 ARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLL 174
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPlhlaayngnleIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
|
170 180 190
....*....|....*....|....*....|....
gi 1007359986 175 RGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQY 207
Cdd:COG0666 175 AGADvNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
69-179 |
7.46e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 69 LHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYsADVNICNNegltatvqclldsgadinr 148
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110
....*....|....*....|....*....|.
gi 1007359986 149 pnvsGATPLYFACSHGQRDTAQILLLRGAKY 179
Cdd:pfam12796 61 ----GRTALHYAARSGHLEIVKLLLEKGADI 87
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
35-217 |
2.04e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 79.32 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 35 MPMVMADQHRSVS--ELLSNSKFDVN-YAFGrvKRSLLHIAANCGSVECLV-----LLLKKGANPNYQDISGCTPLHLAA 106
Cdd:PHA03100 37 LPLYLAKEARNIDvvKILLDNGADINsSTKN--NSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNGITPLLYAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 107 RN--GQKKCMSKLLEYSADVNICNNEGLTA-----------------------------TVQCLLDSGADINRPNVSGAT 155
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNIKNSDGENLlhlylesnkidlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007359986 156 PLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLfQTIIQ 217
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI-KTIIE 256
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
34-126 |
9.67e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 34 LMPMVMADQHRSVSELLSN-SKFDVNYAFGRvkrSLLHIAANCGSVECLVLLLKKgANPNYQDiSGCTPLHLAARNGQKK 112
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENgADANLQDKNGR---TALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75
|
90
....*....|....
gi 1007359986 113 CMSKLLEYSADVNI 126
Cdd:pfam12796 76 IVKLLLEKGADINV 89
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
56-157 |
9.69e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.13 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 56 DVNYAfGRVKRSLLHIAANCGSVEC---LVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL-EYSADVNICNNEG 131
Cdd:PHA03095 39 DVNFR-GEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGADVNAKDKVG 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 1007359986 132 LTA-------------TVQCLLDSGADINRPNVSGATPL 157
Cdd:PHA03095 118 RTPlhvylsgfninpkVIRLLLRKGADVNALDLYGMTPL 156
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
52-194 |
1.65e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.30 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 52 NSKFDVNYAFGRVKrSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEG 131
Cdd:PHA02874 112 DCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007359986 132 LT-----------ATVQCLLDSGADINRPNVSGATPLYFACSHgQRDTAQILLLRGAKYLPDKNGVTPLDLCVQ 194
Cdd:PHA02874 191 ESplhnaaeygdyACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDIDGSTPLHHAIN 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
66-118 |
3.90e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.83 E-value: 3.90e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1007359986 66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLL 118
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
77-190 |
9.79e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.05 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 77 SVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC---MSKLLEYSADVN-------------ICNNEGLtATVQCLL 140
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNapercgftplhlyLYNATTL-DVIKLLI 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007359986 141 DSGADINRPNVSGATPLYfACSHGQR---DTAQILLLRGAKylP---DKNGVTPLD 190
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLH-VYLSGFNinpKVIRLLLRKGAD--VnalDLYGMTPLA 157
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
44-207 |
2.13e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.86 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 44 RSVSELLSNSKF--DVNYAFGRVKrslLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYS 121
Cdd:PHA02875 82 KAVEELLDLGKFadDVFYKDGMTP---LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 122 ADVNICNNEGLT-----------ATVQCLLDSGADIN----RPNVsgaTPLYFACSHGQRDTAQILLLRGAkylpDKNGV 186
Cdd:PHA02875 159 ACLDIEDCCGCTpliiamakgdiAICKMLLDSGANIDyfgkNGCV---AALCYAIENNKIDIVRLFIKRGA----DCNIM 231
|
170 180
....*....|....*....|.
gi 1007359986 187 TpldlCVQGGYGETCEVLIQY 207
Cdd:PHA02875 232 F----MIEGEECTILDMICNM 248
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
43-193 |
5.49e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.27 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 43 HRSVSELLSNSKFDVN--YAFGRVKRSLLHIAANCgSVECLVLLLKKGANPNYQDISGCTPLHLAARN--GQKKCMSKLL 118
Cdd:PHA03095 131 NPKVIRLLLRKGADVNalDLYGMTPLAVLLKSRNA-NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 119 EYSADVNICNNEGLTAT-------------VQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLP-DKN 184
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLhsmatgssckrslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAvSSD 289
|
....*....
gi 1007359986 185 GVTPLDLCV 193
Cdd:PHA03095 290 GNTPLSLMV 298
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
56-239 |
1.13e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 58.92 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 56 DVNyAFGRVKRSLLHIAANCGSVECLVL-LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA 134
Cdd:PHA02876 333 DVN-AADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 135 ------------TVQCLLDSGADINRPNVSGATPLYFACSHGQR-DTAQILLLRGAkylpDKNGVTPLD---LCVQGGYG 198
Cdd:PHA02876 412 lhfalcgtnpymSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA----DVNAINIQNqypLLIALEYH 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1007359986 199 ETCEVLIQYHPRLFQTIIqmtQNEDLRENM--LRQVLEHLSQQ 239
Cdd:PHA02876 488 GIVNILLHYGAELRDSRV---LHKSLNDNMfsFRYIIAHICIQ 527
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
131-213 |
2.65e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 131 GLTATVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGETCEVLIQYHP 209
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADpTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
|
....
gi 1007359986 210 RLFQ 213
Cdd:PTZ00322 173 CHFE 176
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
33-189 |
4.14e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.51 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 33 TLMPMVmaDQHRS----VSELLSNSKFDVNYAFGRVKRSLL---HIAAN-------------------CGSVECLVLLLK 86
Cdd:PHA02874 35 TTTPLI--DAIRSgdakIVELFIKHGADINHINTKIPHPLLtaiKIGAHdiikllidngvdtsilpipCIEKDMIKTILD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 87 KGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGL----TAT-------VQCLLDSGADINRPNVSGAT 155
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCypihIAIkhnffdiIKLLLEKGAYANVKDNNGES 192
|
170 180 190
....*....|....*....|....*....|....*
gi 1007359986 156 PLYFACSHGQRDTAQILLLRGAKYLPD-KNGVTPL 189
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPL 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
83-152 |
5.59e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.61 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA-----------TVQCLLDSGADINRPNV 151
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidTIKAIIDNRSNINKNDL 242
|
.
gi 1007359986 152 S 152
Cdd:PHA02876 243 S 243
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
46-208 |
1.89e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 46 VSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN 125
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 126 ICNNEGLT------------ATVQCLLDSGADIN-RPNVSGATPLYFACsHGQRDTAqiLLLrgaKYLPDKNGV-----T 187
Cdd:PHA02878 229 ARDKCGNTplhisvgyckdyDILKLLLEHGVDVNaKSYILGLTALHSSI-KSERKLK--LLL---EYGADINSLnsyklT 302
|
170 180
....*....|....*....|.
gi 1007359986 188 PLDLCVQGGYGETCEVLIQYH 208
Cdd:PHA02878 303 PLSSAVKQYLCINIGRILISN 323
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
3-177 |
2.43e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.49 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 3 RAMEQLNRL-TRSLRRARTVElPEDNETAVYTLMPMVMADQHRSVSELLSNS---KFDVNYAFgrvkrSLLHIAANcGSV 78
Cdd:PLN03192 466 KTLSQLLRLkTSTLIEAMQTR-QEDNVVILKNFLQHHKELHDLNVGDLLGDNggeHDDPNMAS-----NLLTVAST-GNA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 79 ECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAT----------------------- 135
Cdd:PLN03192 539 ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisd 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007359986 136 ------VQC-------------LLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGA 177
Cdd:PLN03192 619 phaagdLLCtaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
49-105 |
5.05e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 5.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1007359986 49 LLSNSKFDVNYaFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:pfam13857 1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
68-173 |
8.22e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 68 LLHIAANCGSVEcLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNicnnegltatvqcLLDSgadin 147
Cdd:PTZ00322 86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT-------------LLDK----- 146
|
90 100
....*....|....*....|....*.
gi 1007359986 148 rpnvSGATPLYFACSHGQRDTAQILL 173
Cdd:PTZ00322 147 ----DGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
83-134 |
1.90e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1007359986 83 LLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA 134
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
98-129 |
2.36e-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: 2.36e-06
10 20 30
....*....|....*....|....*....|...
gi 1007359986 98 GCTPLHLAA-RNGQKKCMSKLLEYSADVNICNN 129
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
67-205 |
4.17e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.99 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 67 SLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVN-ICNNEGLT----ATV----- 136
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTplhlATIlkkld 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007359986 137 --QCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILL-LRGAKYLPDKNGVTPLDLCVQGGYGETCEVLI 205
Cdd:PHA02875 117 imKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIdHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
76-207 |
8.28e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 76 GSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSA--DVNICN---------NEGLTATVQCLLDSGA 144
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDieselhdavEEGDVKAVEELLDLGK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007359986 145 DINrpNV---SGATPLYFACSHGQRDTAQILLLRGAKY-LPDKNGVTPLDLCVQGGYGETCEVLIQY 207
Cdd:PHA02875 93 FAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPdIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
100-173 |
9.68e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 9.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007359986 100 TPLHLAARNGQKKCMSKLLEysadvnicnnegltatvqclldSGADINRPNVSGATPLYFACSHGQRDTAQILL 173
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLE----------------------KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
98-126 |
1.12e-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: 1.12e-05
10 20
....*....|....*....|....*....
gi 1007359986 98 GCTPLHLAARNGQKKCMSKLLEYSADVNI 126
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
66-164 |
3.34e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.33 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 66 RSLLHIAANcgSV----ECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKC--MSKLLEYSADVNICNNEGLT----AT 135
Cdd:PHA03095 188 RSLLHHHLQ--SFkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTplhyAA 265
|
90 100 110
....*....|....*....|....*....|....*.
gi 1007359986 136 V-------QCLLDSGADINRPNVSGATPLYFACSHG 164
Cdd:PHA03095 266 VfnnpracRRLIALGADINAVSSDGNTPLSLMVRNN 301
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
66-152 |
5.12e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 66 RSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSadvnICNNEG--------LTATVQ 137
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS----QCHFELganakpdsFTGKPP 191
|
90
....*....|....*
gi 1007359986 138 CLLDSGADINRPNVS 152
Cdd:PTZ00322 192 SLEDSPISSHHPDFS 206
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
98-126 |
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 1007359986 98 GCTPLHLAARNGQKKCMSKLLEYSADVNI 126
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
26-134 |
2.16e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 44.17 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 26 DNETAvytLMPMVMADQHRSVSELLSNsKFDVNyAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLA 105
Cdd:COG0666 185 DGETP---LHLAAENGHLEIVKLLLEA-GADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
|
90 100
....*....|....*....|....*....
gi 1007359986 106 ARNGQKKCMSKLLEYSADVNICNNEGLTA 134
Cdd:COG0666 260 AAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-95 |
2.38e-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: 2.38e-04
10 20 30
....*....|....*....|....*....|.
gi 1007359986 66 RSLLHIAA-NCGSVECLVLLLKKGANPNYQD 95
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
139-192 |
2.48e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007359986 139 LLDSG-ADINRPNVSGATPLYFACSHGQRDTAQILLLRGA-KYLPDKNGVTPLDLC 192
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
84-207 |
6.14e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.12 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 84 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA----------------TVQCLLDSGADIN 147
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPlhylsnikynltdvkeIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007359986 148 RPNVSGATPLYFACSH--GQRDTAQILLLRGAK-YLPDKNGVTPLDLCVQGGYGET--CEVLIQY 207
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANvNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
44-177 |
6.67e-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: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 44 RSVSELLSNSKFDVnYAFGRVKRSLLHIAANCGSVECLVLLLKkgANPN----------YQdisGCTPLHLAARNgqkkc 113
Cdd:cd22192 31 QAIKKLLKCPSCDL-FQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtsdlYQ---GETALHIAVVN----- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007359986 114 msklleysadvnicNNEGLtatVQCLLDSGADINRPNVSGAT--------------PLYFACSHGQRDTAQILLLRGA 177
Cdd:cd22192 100 --------------QNLNL---VRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGA 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-93 |
9.03e-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: 9.03e-04
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
38-95 |
1.07e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.94 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007359986 38 VMADQHRSVSELLSNSKFDVNYAfgrvKRSLLHIAANCGSVECLVLLLKKGANPNYQD 95
Cdd:pfam12796 38 AKNGHLEIVKLLLEHADVNLKDN----GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
69-148 |
2.11e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 69 LHIAANCGSVECLVL--LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTATVQCLLDSGADI 146
Cdd:PHA03095 226 LHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
|
..
gi 1007359986 147 NR 148
Cdd:PHA03095 306 VR 307
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
64-133 |
2.47e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.74 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007359986 64 VKRSLLHIAANCGSVECLVLLLKKGANPN-YQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLT 133
Cdd:PHA02884 69 SKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVT 139
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
77-206 |
2.84e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.97 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 77 SVECLVLLLKKGANPNYQDISGCTPLhlaarngqkkC--MSKLLEYSADVNIcnnegltatVQCLLDSGADINRPNVSGA 154
Cdd:PHA02798 50 STDIVKLFINLGANVNGLDNEYSTPL----------CtiLSNIKDYKHMLDI---------VKILIENGADINKKNSDGE 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007359986 155 TPLYFACSHGQRDTAQILLL---RGAK-YLPDKNGVTPLDLCVQGGYG---ETCEVLIQ 206
Cdd:PHA02798 111 TPLYCLLSNGYINNLEILLFmieNGADtTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-92 |
8.43e-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: 8.43e-03
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
84-185 |
9.42e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 39.27 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007359986 84 LLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTA-------------TVQCLLDSGADINRP- 149
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyylsgtddevieRINLLVQYGAKINNSv 137
|
90 100 110
....*....|....*....|....*....|....*.
gi 1007359986 150 NVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKNG 185
Cdd:PHA02946 138 DEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFG 173
|
|
|