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Conserved domains on  [gi|1595776940|ref|NP_001356096|]
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E3 ubiquitin-protein ligase MIB2 isoform 5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 6.96e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 6.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776940 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.59e-34

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 124.25  E-value: 5.59e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 2.00e-28

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


:

Pssm-ID: 239079  Cd Length: 45  Bit Score: 107.54  E-value: 2.00e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 1.04e-24

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 97.70  E-value: 1.04e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 1.30e-23

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 94.62  E-value: 1.30e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 2.32e-17

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 76.87  E-value: 2.32e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 9.67e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 9.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 6.96e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 6.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776940 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.59e-34

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 124.25  E-value: 5.59e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 2.00e-28

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 107.54  E-value: 2.00e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 1.04e-24

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 97.70  E-value: 1.04e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 1.30e-23

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 94.62  E-value: 1.30e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-712 1.46e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.72  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 461 TKNQGRTALQVaaYLGQ-----VELVRLLLQARASMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTA 534
Cdd:PHA03095   43 RGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 535 LHVAVqRGF---LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHaslkg 611
Cdd:PHA03095  121 LHVYL-SGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDA-GADVYAVDDRFRSLLHH----- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 612 HVLAVR------KILARARQLVDAKKEDGFTALHLAALNN--HREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA03095  194 HLQSFKprarivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRA 272
                         250       260
                  ....*....|....*....|....*....
gi 1595776940 684 VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-561 1.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 469 LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTrsTALHVAVQRGFLEVVK 548
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1595776940 549 ILCERGCDVNLPD 561
Cdd:pfam12796  79 LLLEKGADINVKD 91
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 2.32e-17

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 76.87  E-value: 2.32e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 9.67e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 9.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
564-797 1.55e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 564 ADTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVD----AKKEDGFTALH 639
Cdd:cd22192    17 SESPLLLAAKENDVQA--IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 640 LAALNNHREVAQVLIREGrCDVN---------VRNRKL-----QSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:cd22192    95 IAVVNQNLNLVRELIARG-ADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 706 HV-ALQRHQLLP------LVADRAGGDPGPLQLLSrlqasglpgcteltvgaavacflalegadvsyaNHRGRSPLDLAT 778
Cdd:cd22192   174 HIlVLQPNKTFAcqmydlILSYDKEDDLQPLDLVP---------------------------------NNQGLTPFKLAA 220
                         250
                  ....*....|....*....
gi 1595776940 779 EGRVLKALQGCAQRFSTAQ 797
Cdd:cd22192   221 KEGNIVMFQHLVQKRRHIQ 239
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
85-129 1.83e-09

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.83e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1595776940   85 RHPNIICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHA 129
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
86-124 3.20e-07

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 47.48  E-value: 3.20e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776940  86 HPNIICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKH 124
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
456-605 2.08e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 456 PEQVDTKNQ-GRTALQVAAYLGQV-ELVRLLLqaraSMDLPDDEGNTVLHYTAM---GNQPEATRVLLSAGC-------A 523
Cdd:TIGR00870  42 KLNINCPDRlGRSALFVAAIENENlELTELLL----NLSCRGAVGDTLLHAISLeyvDAVEAILLHLLAAFRksgplelA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 524 VDARNGTRS---TALHVAVQRGFLEVVKILCERGCDVN--------LPDAHADTPLHS----AISAGAGASSIVEVLTEV 588
Cdd:TIGR00870 118 NDQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffVKSQGVDSFYHGesplNAAACLGSPSIVALLSED 197
                         170
                  ....*....|....*..
gi 1595776940 589 PGiDVTATNSQGFTLLH 605
Cdd:TIGR00870 198 PA-DILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
633-663 1.52e-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: 39.49  E-value: 1.52e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1595776940  633 DGFTALHLAALNNHREVAQVLIREGRcDVNV 663
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
639-708 1.13e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 639 HLAALNNhrEVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PTZ00322   88 QLAASGD--AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 6.96e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 6.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776940 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-705 1.34e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 416 LSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPD 495
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 496 DEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAG 575
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA--AA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 576 AGASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR-ARqlVDAKKEDGFTALHLAALNNHREVAQVLI 654
Cdd:COG0666   163 NGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAgAD--VNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 655 REGRcDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:COG0666   240 EAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
448-719 1.39e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 1.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 448 ALDLLRRHPEQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDAR 527
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 528 NGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 608 SLKGHVLAVRKILAR-ARqlVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPL 686
Cdd:COG0666   161 AANGNLEIVKLLLEAgAD--VNARDNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1595776940 687 LVDAGCSVNTEDEEGDTALHVALQRHQLLPLVA 719
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-713 5.44e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 5.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR-ARqlVDAKKEDGFT 636
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLE--IVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgAD--VNAQDNDGNT 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 637 ALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQ 713
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN 231
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.59e-34

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 124.25  E-value: 5.59e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 2.00e-28

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 107.54  E-value: 2.00e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 1.04e-24

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 97.70  E-value: 1.04e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 1.30e-23

Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate recognition domain for a second, membrane-distal epitope of the Notch ligand (C-box). Although the first Mib repeat of REP may play a dominant role in ligand binding, the two repeats appear to cooperate in the engagement of the Jag1 tail. Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. The structure and functional analysis, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. REP domains have a five-stranded anti-parallel twisted beta sheet topology similar to that of SH3 domains.


Pssm-ID: 465720  Cd Length: 67  Bit Score: 94.62  E-value: 1.30e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-712 1.46e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.72  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 461 TKNQGRTALQVaaYLGQ-----VELVRLLLQARASMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTA 534
Cdd:PHA03095   43 RGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 535 LHVAVqRGF---LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHaslkg 611
Cdd:PHA03095  121 LHVYL-SGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDA-GADVYAVDDRFRSLLHH----- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 612 HVLAVR------KILARARQLVDAKKEDGFTALHLAALNN--HREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA03095  194 HLQSFKprarivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRA 272
                         250       260
                  ....*....|....*....|....*....
gi 1595776940 684 VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-561 1.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 469 LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTrsTALHVAVQRGFLEVVK 548
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1595776940 549 ILCERGCDVNLPD 561
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
544-778 3.35e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.71  E-value: 3.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 544 LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASS-IVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR 622
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVRLLLEA-GADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 623 ARQLVDAKKEDGFTALH--LAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQ--QAHLGLVPLLVDAGCSVNTED 698
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 699 EEGDTALHVALQR--------HQLLPLVADRAGGDPGPLQLLSRLQASGlpGCTELTVGaavacFLALEGADVSYANHRG 770
Cdd:PHA03095  185 DRFRSLLHHHLQSfkprarivRELIRAGCDPAATDMLGNTPLHSMATGS--SCKRSLVL-----PLLIAGISINARNRYG 257

                  ....*...
gi 1595776940 771 RSPLDLAT 778
Cdd:PHA03095  258 QTPLHYAA 265
PHA03095 PHA03095
ankyrin-like protein; Provisional
478-708 9.22e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.17  E-value: 9.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHY---TAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGF-LEVVKILCER 553
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 554 GCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLhHASLKGH--VLAVRKILARARQLVDAKK 631
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPL-AVLLKSRnaNVELLRLLIDAGADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 632 EDGFTALHLAAlNNHREVAQV---LIREGrCDVNVRNRKLQSPLHLAVQQ---AHLGLVPLLvDAGCSVNTEDEEGDTAL 705
Cdd:PHA03095  185 DRFRSLLHHHL-QSFKPRARIvreLIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLL-IAGISINARNRYGQTPL 261

                  ...
gi 1595776940 706 HVA 708
Cdd:PHA03095  262 HYA 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
490-699 7.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 7.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 490 SMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTALH-----VAVQRGFLEVVKILCERGCDVNLPDAH 563
Cdd:PHA03100   26 DLNDYSYKKPVLPLYLAKeARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 564 ADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHhASLKG----------------HVLAVRKI--LARARQ 625
Cdd:PHA03100  106 GITPLLYAISKKSNSYSIVEYLLDN-GANVNIKNSDGENLLH-LYLESnkidlkilkllidkgvDINAKNRVnyLLSYGV 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 626 LVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDE 699
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 2.32e-17

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 76.87  E-value: 2.32e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
PHA02876 PHA02876
ankyrin repeat protein; Provisional
478-715 2.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.66  E-value: 2.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMDLPDDEGNTVLHYTAmgNQPEATRV---LLSAGCAVDARNGTRSTALHVAVQRGF-LEVVKILCER 553
Cdd:PHA02876  253 LETSLLLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIML 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 554 GCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvpGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKED 633
Cdd:PHA02876  331 GADVNAADRLYITPLHQASTLDRNKDIVITLLEL--GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 634 GfTALHLAAL-NNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQ-AHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR 711
Cdd:PHA02876  409 G-TALHFALCgTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEY 486

                  ....
gi 1595776940 712 HQLL 715
Cdd:PHA02876  487 HGIV 490
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-698 3.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 604 LHHASLKGHVLAVrKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRCDVNVRNRklqSPLHLAVQQAHLGL 683
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1595776940 684 VPLLVDAGCSVNTED 698
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
469-777 8.58e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 8.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 469 LQVAAYLGQVELVRLLLQARAS-MDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVV 547
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 548 KILCERGCDVNL---PDAHADTplhsaisagagASSIVEVltevpGIDVTATNSQGFTLLHHASLKGHvLAVRKILARAR 624
Cdd:PHA02874   85 KLLIDNGVDTSIlpiPCIEKDM-----------IKTILDC-----GIDVNIKDAELKTFLHYAIKKGD-LESIKMLFEYG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 625 QLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTA 704
Cdd:PHA02874  148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 705 LHVA-LQRHQLLPLVADRAGGDPGPLQLLSRLQASGLPGCTELTVGAavacfLALEGADVSYANHRGRSPLDLA 777
Cdd:PHA02874  227 LHNAiIHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIDIIDI-----LLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
502-597 1.26e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 502 LHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERgCDVNLPDaHADTPLHSAISagAGASSI 581
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAAR--SGHLEI 76
                          90
                  ....*....|....*.
gi 1595776940 582 VEVLTEvPGIDVTATN 597
Cdd:pfam12796  77 VKLLLE-KGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
521-708 2.09e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 521 GCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASS---IVEVLTEVpGIDVTATN 597
Cdd:PHA03100   25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDvkeIVKLLLEY-GANVNAPD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 598 SQGFTLLHHASLK--GHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHR--EVAQVLIREG---------------R 658
Cdd:PHA03100  104 NNGITPLLYAISKksNSYSIVEYLLDNGAN-VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGvdinaknrvnyllsyG 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776940 659 CDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
89-133 2.79e-15

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 70.16  E-value: 2.79e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776940  89 IICDCCKKHgLRGMRWKCRVCFDYDLCTQCY--MHNKHDLTHAFERY 133
Cdd:cd02249     1 YSCDGCLKP-IVGVRYHCLVCEDFDLCSSCYakGKKGHPPDHSFTEI 46
Ank_2 pfam12796
Ankyrin repeats (3 copies);
535-665 7.43e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 7.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 535 LHVAVQRGFLEVVKILCERGCDVNLpdahadtplhsaisagagassivevltevpgidvtaTNSQGFTLLHHASLKGHVL 614
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL------------------------------------QDKNGRTALHLAAKNGHLE 44
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 615 AVRKILARARQLVdakKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRN 665
Cdd:pfam12796  45 IVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
466-712 4.54e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 4.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 466 RTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYT----------------------------AMGNQPEATRVL 517
Cdd:PHA02876  179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdsknidtikaiidnrsninkndlsllkAIRNEDLETSLL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 518 L-SAGCAVDARNGTRSTALHVAVQRGFL-EVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvpGIDVTA 595
Cdd:PHA02876  259 LyDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIML--GADVNA 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 596 TNSQGFTLLHHASL----KGHVLAVRKILARarqlVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSP 671
Cdd:PHA02876  337 ADRLYITPLHQASTldrnKDIVITLLELGAN----VNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTA 411
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1595776940 672 LHLAVQQAHLGL-VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA02876  412 LHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKN 453
PHA02874 PHA02874
ankyrin repeat protein; Provisional
479-677 1.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 479 ELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVN 558
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 559 LPDAHADTPLHSAISAGAGAsSIVEVLTEVPGIDVTATNsqGFTLLHHASLkgHVLAVRKILARARQLVDaKKEDGFTAL 638
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKN--GFTPLHNAII--HNRSAIELLINNASIND-QDIDGSTPL 258
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1595776940 639 HlAALNN--HREVAQVLIREgRCDVNVRNRKLQSPLHLAVQ 677
Cdd:PHA02874  259 H-HAINPpcDIDIIDILLYH-KADISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
483-694 1.01e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 483 LLLQARASMDLPDDEGNtVLHYTAMGNQPEATRvLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDA 562
Cdd:PLN03192  512 LLGDNGGEHDDPNMASN-LLTVASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 563 HADTPLHSAISagAGASSIVEVLTEVpgidVTATNSQ-GFTLLHHASLKGHVLAVRKILARARQlVDAKKEDGFTALHLA 641
Cdd:PLN03192  590 NGNTALWNAIS--AKHHKIFRILYHF----ASISDPHaAGDLLCTAAKRNDLTAMKELLKQGLN-VDSEDHQGATALQVA 662
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 642 ALNNHREVAQVLIREGRCDVNVRNRKLQSPLHL--AVQQAHLGLVPLLVDAGCSV 694
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTDDDFSPTELreLLQKRELGHSITIVDSVPAD 717
PHA02874 PHA02874
ankyrin repeat protein; Provisional
458-607 1.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 458 QVDTKN-QGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALH 536
Cdd:PHA02874  116 DVNIKDaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 537 VAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGagaSSIVEVLTEVPGIDVTATNsqGFTLLHHA 607
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN---RSAIELLINNASINDQDID--GSTPLHHA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
477-709 5.87e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 5.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 477 QVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAG---------------CAVDARN--------GTRST 533
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNidtikaiiDNRSN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 534 ------ALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAgASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:PHA02876  237 inkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPS-LSRLVPKLLE-RGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 608 SLKGH-VLAVRKILARARQlVDAKKEDGFTALHLAA-LNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVP 685
Cdd:PHA02876  315 AKNGYdTENIRTLIMLGAD-VNAADRLYITPLHQAStLDRNKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIIN 392
                         250       260
                  ....*....|....*....|....
gi 1595776940 686 LLVDAGCSVNTEDEEGDTALHVAL 709
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFAL 416
PHA02878 PHA02878
ankyrin repeat protein; Provisional
477-678 8.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 477 QVELVRLLLQARASMDLPD-DEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGC 555
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 556 DVNLPDAHADTPLHsaISAGAGAS-SIVEVLTEvPGIDVTATNSqgftllhhaslkghvlavrkILararqlvdakkedG 634
Cdd:PHA02878  226 STDARDKCGNTPLH--ISVGYCKDyDILKLLLE-HGVDVNAKSY--------------------IL-------------G 269
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1595776940 635 FTALHLAAlnnHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQ 678
Cdd:PHA02878  270 LTALHSSI---KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
444-653 9.62e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 444 NVARALdlLRRHPEQVDTKNQGRTALqvAAYLGQ----VELVRLLLQARASMDLPDDEGNTVLHYTAmgnqpeatrvlls 519
Cdd:PHA03095  133 KVIRLL--LRKGADVNALDLYGMTPL--AVLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHL------------- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 520 agcavdarNGTRSTAlhvavqrgflEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvPGIDVTATNSQ 599
Cdd:PHA03095  196 --------QSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLI-AGISINARNRY 256
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 600 GFTLLHHASLKGHVLAVRKILAR-ARqlVDAKKEDGFTALHLAALN-NHREVAQVL 653
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALgAD--INAVSSDGNTPLSLMVRNnNGRAVRAAL 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 9.67e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 9.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
581-786 1.88e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.75  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 581 IVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRcD 660
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 661 VNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLlplvadraggdpgplqllsrlqasgl 740
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL-------------------------- 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1595776940 741 pgcteltvgAAVACFLALeGADVSYANHRGRSPLDLATEGR---VLKAL 786
Cdd:COG0666   134 ---------EIVKLLLEA-GADVNAQDNDGNTPLHLAAANGnleIVKLL 172
PHA02878 PHA02878
ankyrin repeat protein; Provisional
461-652 3.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 461 TKNQGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQ 540
Cdd:PHA02878  164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 541 RGF-LEVVKILCERGCDVNLPDAHAD-TPLHSAISagagASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRK 618
Cdd:PHA02878  244 YCKdYDILKLLLEHGVDVNAKSYILGlTALHSSIK----SERKLKLLLEY-GADINSLNSYKLTPLSSAVKQYLCINIGR 318
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1595776940 619 ILA-----RARQLVDAKKEDGFTaLHLAALNNHREVAQV 652
Cdd:PHA02878  319 ILIsniclLKRIKPDIKNSEGFI-DNMDCITSNKRLNQI 356
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
89-130 8.51e-11

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 57.27  E-value: 8.51e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1595776940  89 IICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDlTHAF 130
Cdd:cd02340     1 VICDGCQGP-IVGVRYKCLVCPDYDLCESCEAKGVHP-EHAM 40
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
564-797 1.55e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 564 ADTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVD----AKKEDGFTALH 639
Cdd:cd22192    17 SESPLLLAAKENDVQA--IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 640 LAALNNHREVAQVLIREGrCDVN---------VRNRKL-----QSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:cd22192    95 IAVVNQNLNLVRELIARG-ADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 706 HV-ALQRHQLLP------LVADRAGGDPGPLQLLSrlqasglpgcteltvgaavacflalegadvsyaNHRGRSPLDLAT 778
Cdd:cd22192   174 HIlVLQPNKTFAcqmydlILSYDKEDDLQPLDLVP---------------------------------NNQGLTPFKLAA 220
                         250
                  ....*....|....*....
gi 1595776940 779 EGRVLKALQGCAQRFSTAQ 797
Cdd:cd22192   221 KEGNIVMFQHLVQKRRHIQ 239
PHA03100 PHA03100
ankyrin repeat protein; Provisional
442-588 2.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 442 LGNVARALDLLRRHPEQVDTK-NQGRTALQVAAY--LGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPE------ 512
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPdNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkl 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 513 ----------ATRV--LLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAIsagagASS 580
Cdd:PHA03100  162 lidkgvdinaKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-----LNN 236

                  ....*...
gi 1595776940 581 IVEVLTEV 588
Cdd:PHA03100  237 NKEIFKLL 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
535-711 4.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 535 LHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAgAGASSIVEVLTEVPGIDVTAT-----------NSQGFTL 603
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKE-PNKLGMKEMIRSINKCSVFYTlvaikdafnnrNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 604 LHHASLKG------------------HVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRN 665
Cdd:PHA02878  120 ILTNRYKNiqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776940 666 RKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR 711
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
85-129 1.83e-09

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.83e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1595776940   85 RHPNIICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHA 129
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
429-600 3.36e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 429 DPEHPGRLVVEAALGNVARALDLLR--RHPEQVDTKnqGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVL---- 502
Cdd:PLN03192  522 DPNMASNLLTVASTGNAALLEELLKakLDPDIGDSK--GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnai 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 503 ---HYT------------------------AMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGC 555
Cdd:PLN03192  600 sakHHKifrilyhfasisdphaagdllctaAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776940 556 DV---NLPDAHADTPLHSAISAGAGASSIVEVLTeVPGIDVTATNSQG 600
Cdd:PLN03192  680 DVdkaNTDDDFSPTELRELLQKRELGHSITIVDS-VPADEPDLGRDGG 726
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-708 4.84e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 4.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 653 LIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
604-709 5.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 604 LHHASLKGHVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKG 150
                          90       100
                  ....*....|....*....|....*.
gi 1595776940 684 VPLLVDAGCSVNTEDEEGDTALHVAL 709
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAM 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
539-707 1.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 539 VQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRK 618
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYA--AERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 619 ILARARQLvdaKKEDgfTALhLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLG-LVPLLVDAGCSVNTE 697
Cdd:PHA02876  230 IIDNRSNI---NKND--LSL-LKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAK 303
                         170
                  ....*....|
gi 1595776940 698 DEEGDTALHV 707
Cdd:PHA02876  304 NIKGETPLYL 313
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-518 1.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 465 GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLL 518
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
89-131 2.69e-08

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 50.42  E-value: 2.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHN----KHDLTHAFE 131
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGvtteRHLFDHPMQ 47
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
89-132 3.56e-08

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 50.28  E-value: 3.56e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFER 132
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGR 44
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
428-662 4.48e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 56.69  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 428 SDPEHPGRLVVEAALGNVARALdllrrhpEQVDTKNQGRTALQVAAYLGQVELVRLLLQ-------ARASMDLPD----- 495
Cdd:cd22194    15 DDMDSPQSPQDDTPSNPNSPSA-------ELAKEEQRDKKKRLKKVSEAAVEELGELLKelkdlsrRRRKTDVPDflmhk 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 496 ----DEGNTVLHYTAMG---NQPEATRVLLS----AGC-------AVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:cd22194    88 ltasDTGKTCLMKALLNineNTKEIVRILLAfaeeNGIldrfinaEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 558 NlpdAHA-----------------DTPLhsAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLH-----HASLKGHVLA 615
Cdd:cd22194   168 N---AHAkgvffnpkykhegfyfgETPL--ALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHalvtvAEDSKTQNDF 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 616 VR----KILARA--RQLVDAKKEDGFTALHLAALNNHREVAQ-VLIREGRCDVN 662
Cdd:cd22194   243 VKrmydMILLKSenKNLETIRNNEGLTPLQLAAKMGKAEILKyILSREIKEKPN 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
517-571 1.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 517 LLSAG-CAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSA 571
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
91-128 1.84e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 48.12  E-value: 1.84e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776940  91 CDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTH 128
Cdd:cd02334     3 CNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSH 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
442-559 2.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 442 LGNVARALDLLR---RHPEQVDTKNQGRTA-LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVL 517
Cdd:PHA02875  108 LATILKKLDIMKlliARGADPDIPNTDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1595776940 518 LSAGCAVD--ARNGTrSTALHVAVQRGFLEVVKILCERGCDVNL 559
Cdd:PHA02875  188 LDSGANIDyfGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
86-124 3.20e-07

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 47.48  E-value: 3.20e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776940  86 HPNIICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKH 124
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
PHA02876 PHA02876
ankyrin repeat protein; Provisional
516-715 4.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 516 VLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGA--GASSIVEVLTEVPGIDV 593
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNidTIKAIIDNRSNINKNDL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 594 TATNS--------------QGFTL----------LHHASLKGHV-LAVRKILARARQlVDAKKEDGFTALHLAALNNH-R 647
Cdd:PHA02876  243 SLLKAirnedletslllydAGFSVnsiddckntpLHHASQAPSLsRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGYdT 321
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595776940 648 EVAQVLIREGrCDVNVRNRKLQSPLHLA-VQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLL 715
Cdd:PHA02876  322 ENIRTLIMLG-ADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
PHA02875 PHA02875
ankyrin repeat protein; Provisional
448-575 7.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 448 ALDLLRRHPEQVDTKNQG-RTALQVAAYLGQVELVRLLLQARASM-DLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVD 525
Cdd:PHA02875   50 AIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776940 526 ARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAG 575
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA02875 PHA02875
ankyrin repeat protein; Provisional
464-558 8.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 464 QGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGF 543
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                          90
                  ....*....|....*
gi 1595776940 544 LEVVKILCERGCDVN 558
Cdd:PHA02875  181 IAICKMLLDSGANID 195
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
472-658 1.20e-06

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: 51.94  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 472 AAYLGQVELVRLLL-------QARASMdlpddeGNTVLHYTAMGNQPEATRVLLSAG-------CAVDARNGtrSTALHV 537
Cdd:cd22192    24 AAKENDVQAIKKLLkcpscdlFQRGAL------GETALHVAALYDNLEAAVVLMEAApelvnepMTSDLYQG--ETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 538 AVQRGFLEVVKILCERGCDVNLPDA--------------HADTPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTL 603
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFA--ACVGNEEIVRLLIE-HGADIRAQDSLGNTV 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 604 LHHASLKGHVLAVRK----ILARARQLVDAKKE-----DGFTALHLAALNNHREVAQVLIREGR 658
Cdd:cd22192   173 LHILVLQPNKTFACQmydlILSYDKEDDLQPLDlvpnnQGLTPFKLAAKEGNIVMFQHLVQKRR 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
498-550 1.66e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776940 498 GNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKIL 550
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
602-654 1.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776940 602 TLLHHASLKGHVLAVRKILArARQLVDAKKEDGFTALHLAALNNHREVAQVLI 654
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
456-605 2.08e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 456 PEQVDTKNQ-GRTALQVAAYLGQV-ELVRLLLqaraSMDLPDDEGNTVLHYTAM---GNQPEATRVLLSAGC-------A 523
Cdd:TIGR00870  42 KLNINCPDRlGRSALFVAAIENENlELTELLL----NLSCRGAVGDTLLHAISLeyvDAVEAILLHLLAAFRksgplelA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 524 VDARNGTRS---TALHVAVQRGFLEVVKILCERGCDVN--------LPDAHADTPLHS----AISAGAGASSIVEVLTEV 588
Cdd:TIGR00870 118 NDQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffVKSQGVDSFYHGesplNAAACLGSPSIVALLSED 197
                         170
                  ....*....|....*..
gi 1595776940 589 PGiDVTATNSQGFTLLH 605
Cdd:TIGR00870 198 PA-DILTADSLGNTLLH 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
532-710 2.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 532 STALHVAVQRGFLEVV-KILCERGCDVNLPDAHADTPLHSAISAGAgaSSIVEVLTEvPGIDVTATNsqgfTLLHHASLK 610
Cdd:PHA02874    2 SQDLRMCIYSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGD--AKIVELFIK-HGADINHIN----TKIPHPLLT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 611 GhvlavrkILARARQLVDAKKEDGF--TALHLAALNNhrEVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLV 688
Cdd:PHA02874   75 A-------IKIGAHDIIKLLIDNGVdtSILPIPCIEK--DMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLF 144
                         170       180
                  ....*....|....*....|..
gi 1595776940 689 DAGCSVNTEDEEGDTALHVALQ 710
Cdd:PHA02874  145 EYGADVNIEDDNGCYPIHIAIK 166
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-705 4.94e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 533 TALHVAVQRGFLEVVKILCERGC--DVNLPDAhaDTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLK 610
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGDVKA--VEELLDLGKFADDVFYKDGMTPLHLATIL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 611 GHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHREVAQVLIREGRCdVNVRNRKLQSPLHLAVQQAHLGLVPLLVDA 690
Cdd:PHA02875  113 KKLDIMKLLIARGAD-PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
                         170
                  ....*....|....*
gi 1595776940 691 GCSVNTEDEEGDTAL 705
Cdd:PHA02875  191 GANIDYFGKNGCVAA 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
619-675 5.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 619 ILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIrEGRCDVNVRNRKLQSPLHLA 675
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
440-495 5.44e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 5.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 440 AALGNVARALDLLRRHPeQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPD 495
Cdd:pfam12796  37 AAKNGHLEIVKLLLEHA-DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
515-585 5.45e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 5.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 515 RVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAGasSIVEVL 585
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLL 167
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
89-128 7.41e-06

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 43.73  E-value: 7.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTH 128
Cdd:cd02345     1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRH 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
603-776 7.82e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 603 LLHHASLKGhvlavrkiLARARQLVDAKKEDG-----FTALHLAALNNhREVAQVLIREGRcDVNVRNRKLQSPLHLAVQ 677
Cdd:PLN03192  498 LQHHKELHD--------LNVGDLLGDNGGEHDdpnmaSNLLTVASTGN-AALLEELLKAKL-DPDIGDSKGRTPLHIAAS 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 678 QAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR---------HQLLPLVADRAGGD-------PGPLQLLSRLQASGL- 740
Cdd:PLN03192  568 KGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkifrilYHFASISDPHAAGDllctaakRNDLTAMKELLKQGLn 647
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776940 741 ------PGCTELTVGAA-----VACFLALEGADVSYAN-HRGRSPLDL 776
Cdd:PLN03192  648 vdsedhQGATALQVAMAedhvdMVRLLIMNGADVDKANtDDDFSPTEL 695
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
91-125 2.92e-05

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 41.78  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1595776940  91 CDCCKKHglRGMRWKCRVCFDYDLCTQCYMHNKHD 125
Cdd:cd02337     3 CNECKHH--VETRWHCTVCEDYDLCITCYNTKNHP 35
Ank_5 pfam13857
Ankyrin repeats (many copies);
451-504 4.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 451 LLRRHPEQVDTKNQ-GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHY 504
Cdd:pfam13857   1 LLEHGPIDLNRLDGeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA03100 PHA03100
ankyrin repeat protein; Provisional
481-606 6.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 6.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 481 VRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLP 560
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776940 561 DAH----ADTPLHSAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLHH 606
Cdd:PHA03100  255 IETllyfKDKDLNTITKIKMLKKSIMYMFLLDPGFYKNRKLIENSKSLKD 304
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
574-662 7.48e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 574 AGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHREVAQVL 653
Cdd:PTZ00322   90 AASGDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD-PTLLDKDGKTPLELAEENGFREVVQLL 167

                  ....*....
gi 1595776940 654 IREGRCDVN 662
Cdd:PTZ00322  168 SRHSQCHFE 176
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
488-605 1.29e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 45.56  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 488 RASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGtrSTALHVAVQRGFLEVVKILCERGCDVNlpdAHA--- 564
Cdd:cd22193    35 KALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEG--QTALHIAIERRQGDIVALLVENGADVH---AHAkgr 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 565 --------------DTPLhsAISAGAGASSIVEVLTEVP--GIDVTATNSQGFTLLH 605
Cdd:cd22193   110 ffqpkyqgegfyfgELPL--SLAACTNQPDIVQYLLENEhqPADIEAQDSRGNTVLH 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
633-663 1.52e-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: 39.49  E-value: 1.52e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1595776940  633 DGFTALHLAALNNHREVAQVLIREGRcDVNV 663
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
89-131 1.93e-04

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 39.58  E-value: 1.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCY----MHNKHDLTHAFE 131
Cdd:cd02335     1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFsagaEIGKHRNDHNYR 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
633-666 2.11e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 2.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1595776940 633 DGFTALHLAAL-NNHREVAQVLIREGrCDVNVRNR 666
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKG-ADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-575 2.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776940 531 RSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAG 575
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
428-492 2.19e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 428 SDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQVELVRLLLQARASMD 492
Cdd:PLN03192  617 SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDhQGATALQVAMAEDHVDMVRLLIMNGADVD 682
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
533-559 2.42e-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: 38.72  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 1595776940  533 TALHVAVQRGFLEVVKILCERGCDVNL 559
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
533-561 3.25e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1595776940 533 TALHVAV-QRGFLEVVKILCERGCDVNLPD 561
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
670-714 4.25e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776940 670 SPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQL 714
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
Ank_4 pfam13637
Ankyrin repeats (many copies);
636-688 6.61e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776940 636 TALHLAALNNHREVAQVLIrEGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLV 688
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
466-695 7.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 466 RTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLE 545
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 546 VVKILCERGC---DVNLPDahADTPLHSAIsagagASSIVEVLTEV--PGIDVTATNSQGFTLLHHASLKGHVLAVrKIL 620
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKD--GMTPLHLAT-----ILKKLDIMKLLiaRGADPDIPNTDKFSPLHLAVMMGDIKGI-ELL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 621 ARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVN 695
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
633-663 7.41e-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: 37.62  E-value: 7.41e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1595776940 633 DGFTALHLAALNNHREVAQVLIREGrCDVNV 663
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
591-641 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 591 IDVTATNSQGFTLLHHASLKGHVLAVRKILARaRQLVDAKKEDGFTALHLA 641
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
639-708 1.13e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 639 HLAALNNhrEVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PTZ00322   88 QLAASGD--AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
470-550 1.44e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 470 QVAAYLGQVEL-----------VRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVA 538
Cdd:PTZ00322   76 PVVAHMLTVELcqlaasgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
                          90
                  ....*....|..
gi 1595776940 539 VQRGFLEVVKIL 550
Cdd:PTZ00322  156 EENGFREVVQLL 167
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
89-127 1.66e-03

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 36.79  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1595776940  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCY--MHNKHDLT 127
Cdd:cd02342     1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICFsrMGNEGEYT 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
533-558 1.73e-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: 36.47  E-value: 1.73e-03
                          10        20
                  ....*....|....*....|....*.
gi 1595776940 533 TALHVAVQRGFLEVVKILCERGCDVN 558
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
465-605 1.76e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.79  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 465 GRTALQVAA-YL--GQVELVRLLLQARASMDLPDDegntvlhytamgnqpeatrvLLSAGCAVDARNGtrSTALHVAVQR 541
Cdd:cd21882    26 GKTCLHKAAlNLndGVNEAIMLLLEAAPDSGNPKE--------------------LVNAPCTDEFYQG--QTALHIAIEN 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776940 542 GFLEVVKILCERGCDVNLP---DAHADTP--------LHSAISAGAGASSIVEVLTEVPG--IDVTATNSQGFTLLH 605
Cdd:cd21882    84 RNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgeLPLSLAACTNQEEIVRLLLENGAqpAALEAQDSLGNTVLH 160
PHA02736 PHA02736
Viral ankyrin protein; Provisional
593-691 1.91e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 593 VTATNSQGFTLLHHASLKGHVLAVRKI--LARARQLVDAKKE-DGFTALHLAALNNHREVAQVLIREGRCDVNVRNRKLQ 669
Cdd:PHA02736   48 VLEYNRHGKQCVHIVSNPDKADPQEKLklLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFK 127
                          90       100
                  ....*....|....*....|..
gi 1595776940 670 SPLHLAVQQAHLGLVPLLVDAG 691
Cdd:PHA02736  128 TPYYVACERHDAKMMNILRAKG 149
Ank_5 pfam13857
Ankyrin repeats (many copies);
484-538 1.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776940 484 LLQAR-ASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVA 538
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
600-708 3.16e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 600 GFTLLHHASLKGHV---LAVRKILARAR-----QLVDAKKEDGF----TALHLAALNNHREVAQVLIREGrCDVNVRN-- 665
Cdd:TIGR00870  82 GDTLLHAISLEYVDaveAILLHLLAAFRksgplELANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG-ASVPARAcg 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 666 ------------RKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:TIGR00870 161 dffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL 215
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
464-496 3.59e-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. 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: 35.73  E-value: 3.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1595776940 464 QGRTALQVAAY-LGQVELVRLLLQARASMDLPDD 496
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
243-742 3.81e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.01  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  243 PAELQRRVSADGQPFQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQM------GTVHRITDRGDVRVQFNHETRWT 316
Cdd:COG3321    854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALaaallaLAAAAAAALALAAAALAALLALV 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  317 FHPGALTKHNSFWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAVGGQRWTFSPSCLVAYR 396
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  397 PEEDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKNQGRTALQVAAYLG 476
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  477 QVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGcAVDARNGTRSTALHVAVQRGFLEVVKILCERGCD 556
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAA-ALAAAAAAAAALALAAAAAALAAALAAALLAAAA 1172
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  557 VNLPDAHADTPLHSAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKEDGFT 636
Cdd:COG3321   1173 LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAA 1252
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940  637 ALHLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLLP 716
Cdd:COG3321   1253 AALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAA 1332
                          490       500
                   ....*....|....*....|....*.
gi 1595776940  717 LVADRAGGDPGPLQLLSRLQASGLPG 742
Cdd:COG3321   1333 LAAAVAAALALAAAAAAAAAAAAAAA 1358
Ank_4 pfam13637
Ankyrin repeats (many copies);
566-613 3.86e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 3.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776940 566 TPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHV 613
Cdd:pfam13637   3 TALHAA--AASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNV 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
553-607 4.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 4.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776940 553 RGCDVNLPDAHADTPLHSAISagAGASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAK--YGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
533-605 5.31e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.17  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 533 TALHVAVQRGFLEVVKILCERGCDVNlpdAHADTPLHSAISAGAG---------------ASSIVEVLTEVP--GIDVTA 595
Cdd:cd22196    96 TALHIAIERRNMHLVELLVQNGADVH---ARASGEFFKKKKGGPGfyfgelplslaactnQLDIVKFLLENPhsPADISA 172
                          90
                  ....*....|
gi 1595776940 596 TNSQGFTLLH 605
Cdd:cd22196   173 RDSMGNTVLH 182
PHA02859 PHA02859
ankyrin repeat protein; Provisional
478-602 5.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 478 VELVRLLLQARASMD-LPDDEGNTVLHYTAMGNQ---PEATRVLLSAGCAVDARNGTRSTALHVAVQRGF--LEVVKILC 551
Cdd:PHA02859   66 VEILKFLIENGADVNfKTRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCNFNvrINVIKLLI 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776940 552 ERGCDVNLPDAHADTPLHSAISAGAgASSIVEVLTEVpGIDVTATNSQGFT 602
Cdd:PHA02859  146 DSGVSFLNKDFDNNNILYSYILFHS-DKKIFDFLTSL-GIDINETNKSGYN 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
398-545 6.82e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 398 EEDANLDVAERARENKSSLSVALDK-LRTQKS-DPEHPGRLVVE----AALGNVARALDLLRRHPEQVDTKNQGRTALQV 471
Cdd:PTZ00322   42 EEIARIDTHLEALEATENKDATPDHnLTTEEViDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHI 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776940 472 AAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRvLLSAGCAVDARNGTRSTALHVAVQRGFLE 545
Cdd:PTZ00322  122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFELGANAKPDSFTGKPPSLE 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
444-530 7.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776940 444 NVARALDLLRRHPEQVDTKNQ-GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGC 522
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                  ....*...
gi 1595776940 523 AVDARNGT 530
Cdd:PHA03100  250 SIKTIIET 257
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
91-128 8.56e-03

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 35.10  E-value: 8.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1595776940  91 CDCCKKHGLRGMRWKCRVC--FDYDLCTQC-YMHNKHDLTH 128
Cdd:cd02341     3 CDSCGIEPIPGTRYHCSECddGDFDLCQDCvVKGESHQEDH 43
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
464-493 8.73e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 8.73e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1595776940  464 QGRTALQVAAYLGQVELVRLLLQARASMDL 493
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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