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Conserved domains on  [gi|767999017|ref|XP_011524400|]
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E3 ubiquitin-protein ligase MIB1 isoform X2 [Homo sapiens]

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];
4-230 1.20e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  84 KRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKlprPWIVDEKKDDGYTALHLAALNNHVEVAELLVH 163
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767999017 164 QGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:COG0666  208 AG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
471-516 2.32e-25

third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger.


:

Pssm-ID: 438387  Cd Length: 46  Bit Score: 98.28  E-value: 2.32e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767999017 471 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16727    1 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIEKRILLY 46
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
327-364 9.85e-18

first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


:

Pssm-ID: 438384  Cd Length: 38  Bit Score: 76.37  E-value: 9.85e-18
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16724    1 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
374-411 4.79e-17

second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


:

Pssm-ID: 438385  Cd Length: 38  Bit Score: 74.44  E-value: 4.79e-17
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16725    1 EECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR 38
PHA03095 super family cl33707
ankyrin-like protein; Provisional
178-288 1.47e-03

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 178 TALHLAVERQH---TQIVRLLVRAGAKLDIQDKDGDTPLHEALRHH-TLSQLRQLQDM-QDVGKVDAAwepSKNTLIMGL 252
Cdd:PHA03095  49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAgADVNAKDKV---GRTPLHVYL 125
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767999017 253 GTQGAEKKsaasIACFLAANGADLSIRNKKGQSPLD 288
Cdd:PHA03095 126 SGFNINPK----VIRLLLRKGADVNALDLYGMTPLA 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-230 1.20e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  84 KRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKlprPWIVDEKKDDGYTALHLAALNNHVEVAELLVH 163
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767999017 164 QGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:COG0666  208 AG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
471-516 2.32e-25

third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger.


Pssm-ID: 438387  Cd Length: 46  Bit Score: 98.28  E-value: 2.32e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767999017 471 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16727    1 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIEKRILLY 46
PHA02874 PHA02874
ankyrin repeat protein; Provisional
32-219 1.50e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.20  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  32 DLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALH 111
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 112 HAALRGNPSAMRVLLSKLPRpwiVDEKKDDGYTALHLAALNNHvEVAELLVHqgNANLDIQNVNQQTALHLAVERQ-HTQ 190
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIHNR-SAIELLIN--NASINDQDIDGSTPLHHAINPPcDID 269
                        170       180
                 ....*....|....*....|....*....
gi 767999017 191 IVRLLVRAGAKLDIQDKDGDTPLHEALRH 219
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-173 1.37e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   77 LHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRpwivdEKKDDGYTALHLAALNNHVE 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV-----NLKDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....*..
gi 767999017  157 VAELLVHQGnANLDIQN 173
Cdd:pfam12796  76 IVKLLLEKG-ADINVKD 91
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
327-364 9.85e-18

first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438384  Cd Length: 38  Bit Score: 76.37  E-value: 9.85e-18
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16724    1 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
374-411 4.79e-17

second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438385  Cd Length: 38  Bit Score: 74.44  E-value: 4.79e-17
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16725    1 EECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR 38
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
372-417 4.38e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 52.38  E-value: 4.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767999017  372 KIEECVVCSDKKAAVLFQPCGHMCACENCANLM----KKCVQCRAVVERR 417
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIESV 50
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-214 4.89e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  74 DTPLHDAIskKRDDILAV---LLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRpwIVDEKKD----DGYTAL 146
Cdd:cd22192   18 ESPLLLAA--KENDVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPMTsdlyQGETAL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 147 HLAALNNHVEVAELLVHQGNanlDIQNVNQ----------------QTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGD 210
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGA---DVVSPRAtgtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                 ....
gi 767999017 211 TPLH 214
Cdd:cd22192  171 TVLH 174
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
472-505 1.08e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 48.20  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 767999017  472 MCPVCLDRLKN--MIFLCGHGTCQLCGDRM----SECPIC 505
Cdd:pfam13923   1 MCPICMDMLKDpsTTTPCGHVFCQDCILRAlragNECPLC 40
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
106-226 3.60e-07

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: 52.78  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  106 GFNALHHAALRGNPSAMRVLLSKLprpwivDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQN---VNQ------ 176
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNL------SCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPlelANDqytsef 125
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017  177 ---QTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGD---TPLHEALRHhtlSQLR 226
Cdd:TIGR00870 126 tpgITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvkSQGVDSFYH---GESP 178
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
327-370 8.21e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 45.83  E-value: 8.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767999017  327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRV----KKCLICKEQVQSR 370
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIESV 50
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
141-171 6.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 6.41e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767999017   141 DGYTALHLAALNNHVEVAELLVHQGnANLDI 171
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
178-288 1.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 178 TALHLAVERQH---TQIVRLLVRAGAKLDIQDKDGDTPLHEALRHH-TLSQLRQLQDM-QDVGKVDAAwepSKNTLIMGL 252
Cdd:PHA03095  49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAgADVNAKDKV---GRTPLHVYL 125
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767999017 253 GTQGAEKKsaasIACFLAANGADLSIRNKKGQSPLD 288
Cdd:PHA03095 126 SGFNINPK----VIRLLLRKGADVNALDLYGMTPLA 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-230 1.20e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  84 KRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKlprPWIVDEKKDDGYTALHLAALNNHVEVAELLVH 163
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767999017 164 QGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:COG0666  208 AG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-281 1.77e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 1.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  84 KRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRpwiVDEKKDDGYTALHLAALNNHVEVAELLVH 163
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 164 QGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQDMqdvGKVDAAWEP 243
Cdd:COG0666  175 AG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDK 250
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767999017 244 SKNTLIMGLGTQGAEKKSAASIACFLAANGADLSIRNK 281
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-213 3.44e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 3.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  84 KRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPrpwIVDEKKDDGYTALHLAALNNHVEVAELLVH 163
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 164 QGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPL 213
Cdd:COG0666  241 AG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-289 1.06e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 1.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  21 AVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVT 100
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 101 ITNNNGFNALHHAALRGNPSAMRVLLSKlprPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTAL 180
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEA---GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 181 HLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHhtlsqlrqlqdmqdvGKVDaawepskntlimglgtqgaekk 260
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN---------------GHLE---------------------- 200
                        250       260
                 ....*....|....*....|....*....
gi 767999017 261 saasIACFLAANGADLSIRNKKGQSPLDL 289
Cdd:COG0666  201 ----IVKLLLEAGADVNAKDNDGKTALDL 225
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
471-516 2.32e-25

third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the third RING-HC finger.


Pssm-ID: 438387  Cd Length: 46  Bit Score: 98.28  E-value: 2.32e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767999017 471 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16727    1 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIEKRILLY 46
PHA02874 PHA02874
ankyrin repeat protein; Provisional
32-219 1.50e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.20  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  32 DLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALH 111
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 112 HAALRGNPSAMRVLLSKLPRpwiVDEKKDDGYTALHLAALNNHvEVAELLVHqgNANLDIQNVNQQTALHLAVERQ-HTQ 190
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNH---IMNKCKNGFTPLHNAIIHNR-SAIELLIN--NASINDQDIDGSTPLHHAINPPcDID 269
                        170       180
                 ....*....|....*....|....*....
gi 767999017 191 IVRLLVRAGAKLDIQDKDGDTPLHEALRH 219
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
4-220 2.51e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.80  E-value: 2.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVH-HAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHI-----AVNKGhlqVVKTLLDFGCHPSLQDSEGDTPL 77
Cdd:PHA03095  80 ERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylsgfNINPK---VIRLLLRKGADVNALDLYGMTPL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  78 HDAISKKR--DDILAVLLEAGADVTITNNNGFNALHHAA--LRGNPSAMRVLLSKLPRPWIVDekkDDGYTALHLAALnn 153
Cdd:PHA03095 157 AVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATD---MLGNTPLHSMAT-- 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 154 HVEVAELLVHQ---GNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHH 220
Cdd:PHA03095 232 GSSCKRSLVLPlliAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
PHA03100 PHA03100
ankyrin repeat protein; Provisional
32-222 1.62e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  32 DLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLH---DAISKKRDD--ILAVLLEAGADVTITNNNG 106
Cdd:PHA03100  27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVkeIVKLLLEYGANVNAPDNNG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 107 FNALHHAALR--GNPSAMRVLLSklpRPWIVDEKKDDGYTALHLAALNNHV--EVAELLVHQG---------------NA 167
Cdd:PHA03100 107 ITPLLYAISKksNSYSIVEYLLD---NGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGvdinaknrvnyllsyGV 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017 168 NLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTL 222
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-173 1.37e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   77 LHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRpwivdEKKDDGYTALHLAALNNHVE 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV-----NLKDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....*..
gi 767999017  157 VAELLVHQGnANLDIQN 173
Cdd:pfam12796  76 IVKLLLEKG-ADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-206 1.46e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  110 LHHAALRGNPSAMRVLLSKLPRPWIVDekkDDGYTALHLAALNNHVEVAELLVHQGNANLDiqnVNQQTALHLAVERQHT 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD---KNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 767999017  190 QIVRLLVRAGAKLDIQD 206
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-208 3.25e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 3.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  22 VIEVLHRGSADLNARNKRRQTPLHIAVNK--GHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDD--ILAVLLEAGA 97
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGV 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  98 DVTITNnngfnalhhaalrgnpsamRV-LLSKLPRPwiVDEKKDDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQ 176
Cdd:PHA03100 168 DINAKN-------------------RVnYLLSYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYG 225
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767999017 177 QTALHLAVERQHTQIVRLLVRAGAklDIQDKD 208
Cdd:PHA03100 226 DTPLHIAILNNNKEIFKLLLNNGP--SIKTII 255
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
327-364 9.85e-18

first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438384  Cd Length: 38  Bit Score: 76.37  E-value: 9.85e-18
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16724    1 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
31-287 1.47e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  31 ADLNARNKRRQTPLHIAVNKGH---LQVVKTLLDFGCHPSLQDSEGDTPLHDAI-SKKRDDILAVLLEAGADVTITNNNG 106
Cdd:PHA03095  38 ADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIKAGADVNAKDKVG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 107 FNALHhaalrgnpsamrvllsklprpwivdekkddgytaLHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALHLAVER 186
Cdd:PHA03095 118 RTPLH----------------------------------VYLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 187 QHT--QIVRLLVRAGAKLDIQDKDGDTPLHealrHHTLS---QLRQLQDMQDVGKVDAAWEPSKNTLIMGLGTQGAEKks 261
Cdd:PHA03095 163 RNAnvELLRLLIDAGADVYAVDDRFRSLLH----HHLQSfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK-- 236
                        250       260
                 ....*....|....*....|....*.
gi 767999017 262 aASIACFLAANGADLSIRNKKGQSPL 287
Cdd:PHA03095 237 -RSLVLPLLIAGISINARNRYGQTPL 261
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
374-411 4.79e-17

second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438385  Cd Length: 38  Bit Score: 74.44  E-value: 4.79e-17
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16725    1 EECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR 38
PHA02874 PHA02874
ankyrin repeat protein; Provisional
22-288 1.08e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  22 VIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLqdsegdTPLHDAiskkRDDILAVLLEAGADVTI 101
Cdd:PHA02874  50 IVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCI----EKDMIKTILDCGIDVNI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 102 TNNNGFNALHHAALRGNPSAMRVLLSKLPRpwiVDEKKDDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALH 181
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 182 LAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTlSQLRQLQDMQDVGKVDA-AWEPSKNTLimglgtqgaEKK 260
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDIdGSTPLHHAI---------NPP 265
                        250       260
                 ....*....|....*....|....*...
gi 767999017 261 SAASIACFLAANGADLSIRNKKGQSPLD 288
Cdd:PHA02874 266 CDIDIIDILLYHKADISIKDNKGENPID 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-289 5.31e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 5.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  86 DDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPrpwIVDEKKDDGYTALHLAALNNHVEVAELLVHQG 165
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALL---ALALADALGALLLLAAALAGDLLVALLLLAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 166 nANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLqdmqdvgkVDA-----A 240
Cdd:COG0666   78 -ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL--------LEAgadvnA 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 241 WEPSKNTLIMglgtqGAEKKSAASIACFLAANGADLSIRNKKGQSPLDL 289
Cdd:COG0666  149 QDNDGNTPLH-----LAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-103 5.36e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 5.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   12 HHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGChpSLQDSEGDTPLHDAISKKRDDILAV 91
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|..
gi 767999017   92 LLEAGADVTITN 103
Cdd:pfam12796  80 LLEKGADINVKD 91
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
471-509 8.94e-16

RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438183 [Multi-domain]  Cd Length: 39  Bit Score: 70.78  E-value: 8.94e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 471 TMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAI 509
Cdd:cd16520    1 ILCPICMERKKNVVFLCGHGTCQKCAEKLKKCPICRKPI 39
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
374-411 1.78e-15

RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 438182  Cd Length: 38  Bit Score: 70.20  E-value: 1.78e-15
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16519    1 EECRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK 38
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
14-170 2.03e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.14  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  14 AAFGDEGAVIEVLhRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLL 93
Cdd:PLN03192 533 ASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  94 EAGAdvtITN-NNGFNALHHAALRGNPSAMRVLLsKLPRPwiVDEKKDDGYTALHLAALNNHVEVAELLVHQG----NAN 168
Cdd:PLN03192 612 HFAS---ISDpHAAGDLLCTAAKRNDLTAMKELL-KQGLN--VDSEDHQGATALQVAMAEDHVDMVRLLIMNGadvdKAN 685

                 ..
gi 767999017 169 LD 170
Cdd:PLN03192 686 TD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
47-230 4.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  47 AVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLL 126
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 127 skLPRPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQD 206
Cdd:PHA02875  89 --DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                        170       180
                 ....*....|....*....|....
gi 767999017 207 KDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:PHA02875 166 CCGCTPLIIAMAKGDIAICKMLLD 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
21-155 5.71e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 5.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  21 AVIEVLHRGSADLNARNKRRQTPLHIavnkgHLQ-------VVKTLLDFGCHPSLQDSEGDTPLHDA--ISKKRDDILAV 91
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMatGSSCKRSLVLP 242
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999017  92 LLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEkkdDGYTALHLAALNNHV 155
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS---DGNTPLSLMVRNNNG 303
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
327-364 1.29e-13

RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 438182  Cd Length: 38  Bit Score: 64.81  E-value: 1.29e-13
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16519    1 EECRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK 38
PHA02875 PHA02875
ankyrin repeat protein; Provisional
41-204 3.50e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.18  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  41 QTPLHIAVNKGHLQVVKTLLDFGCHpsLQD---SEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRG 117
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKF--ADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 118 NPSAMRVLLSKLPrpwIVDEKKDDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQ-TALHLAVERQHTQIVRLLV 196
Cdd:PHA02875 147 DIKGIELLIDHKA---CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG-ANIDYFGKNGCvAALCYAIENNKIDIVRLFI 222

                 ....*...
gi 767999017 197 RAGAKLDI 204
Cdd:PHA02875 223 KRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
12-93 3.72e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 71.85  E-value: 3.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  12 HHAAFGDegAV-IEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILA 90
Cdd:PTZ00322  88 QLAASGD--AVgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ...
gi 767999017  91 VLL 93
Cdd:PTZ00322 166 LLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
53-219 8.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 8.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  53 LQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAA-----LRGNPSAMRVLLS 127
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 128 KLPRpwiVDEKKDDGYTALHLAALN--NHVEVAELLVHQGnANLDIQNVNQQTALHLAVERQH--TQIVRLLVRAGAK-- 201
Cdd:PHA03100  95 YGAN---VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDin 170
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767999017 202 --------------LDIQDKDGDTPLHEALRH 219
Cdd:PHA03100 171 aknrvnyllsygvpINIKDVYGFTPLHYAVYN 202
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
32-247 8.53e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  32 DLNARNKRRQTPLHIAVN------KGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNN 105
Cdd:PLN03192 511 DLLGDNGGEHDDPNMASNlltvasTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 106 GFNALHHAALRGNPSAMRVL--LSKLPRPWIvdekkddGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALHLA 183
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILyhFASISDPHA-------AGDLLCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVA 662
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767999017 184 VERQHTQIVRLLVRAGAKLDIQDKDGD---TPLHEALRH----HTLSQLRQLQDMQDVGKVDAAWEPSKNT 247
Cdd:PLN03192 663 MAEDHVDMVRLLIMNGADVDKANTDDDfspTELRELLQKrelgHSITIVDSVPADEPDLGRDGGSRPGRLQ 733
PHA02878 PHA02878
ankyrin repeat protein; Provisional
43-214 1.95e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  43 PLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLH------------DAISKKRDDILAVLLEAGADVTITNN-NGFNA 109
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkEMIRSINKCSVFYTLVAIKDAFNNRNvEIFKI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 110 LHHAALRGNPSAMRVLLSKLPRPWIVDEK----------------KDDGYTALHLAALNNHVEVAELLVHQGnANLDIQN 173
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEitklllsygadinmkdRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767999017 174 VNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLH 214
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
PHA02875 PHA02875
ankyrin repeat protein; Provisional
42-213 2.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  42 TPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAIskKRDDILAV--LLEAGADVT-ITNNNGFNALHHAALRGN 118
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAV--EEGDVKAVeeLLDLGKFADdVFYKDGMTPLHLATILKK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 119 PSAMRVLLSKLPRPwivDEKKDDGYTALHLAALNNHVEVAELLVHQgNANLDIQNVNQQTALHLAVERQHTQIVRLLVRA 198
Cdd:PHA02875 115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
                        170
                 ....*....|....*
gi 767999017 199 GAKLDIQDKDGDTPL 213
Cdd:PHA02875 191 GANIDYFGKNGCVAA 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
26-78 1.11e-11

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 59.67  E-value: 1.11e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767999017   26 LHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLH 78
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
4-140 3.77e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDR-AVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAIS 82
Cdd:PHA02878 164 DRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  83 KKRD-DILAVLLEAGADVTITNN-NGFNALhHAALRgNPSAMRVLLSKLPRPWIVDEKKD 140
Cdd:PHA02878 244 YCKDyDILKLLLEHGVDVNAKSYiLGLTAL-HSSIK-SERKLKLLLEYGADINSLNSYKL 301
PHA03100 PHA03100
ankyrin repeat protein; Provisional
32-105 4.25e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 4.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999017  32 DLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNN 105
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
469-516 4.58e-11

RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant; RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. Members of this subfamily contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438389  Cd Length: 48  Bit Score: 57.88  E-value: 4.58e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767999017 469 EQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16729    1 DDQLCPICLSNPKDMAFGCGHQTCCECGQSLTHCPICRQPITTRIKLY 48
PHA02878 PHA02878
ankyrin repeat protein; Provisional
19-218 1.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  19 EGAVIEVLHRGSADLNARNKRR-QTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGA 97
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  98 DVTITNNNGFNALHHAALRgnpsamrvLLSklprpwivdekkddgytalhlaalnnhVEVAELLVHQG---NANLDIQNV 174
Cdd:PHA02878 226 STDARDKCGNTPLHISVGY--------CKD---------------------------YDILKLLLEHGvdvNAKSYILGL 270
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767999017 175 nqqTALHLAVERQhtQIVRLLVRAGAKLDIQDKDGDTPLHEALR 218
Cdd:PHA02878 271 ---TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
4-113 2.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   4 DKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISK 83
Cdd:PHA02874 154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
                         90       100       110
                 ....*....|....*....|....*....|
gi 767999017  84 KRDDIlaVLLEAGADVTITNNNGFNALHHA 113
Cdd:PHA02874 234 NRSAI--ELLINNASINDQDIDGSTPLHHA 261
PHA02875 PHA02875
ankyrin repeat protein; Provisional
2-128 2.25e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   2 VLDKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAI 81
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767999017  82 SKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGN-PSAMRVLLSK 128
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNkIDIVRLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 3.18e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 3.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767999017   73 GDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLL 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
RING-HC_MIB2_rpt2 cd16728
second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
467-516 5.71e-10

second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. Especially, it promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2, activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the second RING-HC finger.


Pssm-ID: 438388  Cd Length: 51  Bit Score: 54.87  E-value: 5.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 467 IKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16728    1 MEERITCPICIDNHIKLVFQCGHGSCIECSSALKACPICRQAIRERIQIF 50
PHA02876 PHA02876
ankyrin repeat protein; Provisional
18-216 1.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  18 DEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGA 97
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  98 DVtitNNNGFNALHhaALRGNPSAMRVLLSKlpRPWIVDEKKDDGYTALHLAALNNHVE--VAELLvhQGNANLDIQNVN 175
Cdd:PHA02876 236 NI---NKNDLSLLK--AIRNEDLETSLLLYD--AGFSVNSIDDCKNTPLHHASQAPSLSrlVPKLL--ERGADVNAKNIK 306
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767999017 176 QQTALHLAVERQH-TQIVRLLVRAGAKLDIQDKDGDTPLHEA 216
Cdd:PHA02876 307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348
PHA02878 PHA02878
ankyrin repeat protein; Provisional
76-219 2.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  76 PLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLprpwivdEKKDDGYT--ALHLAALNN 153
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSI-------NKCSVFYTlvAIKDAFNNR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 154 HVEVAELLV---HQGNANLDIQNVNQ------------------------------QTALHLAVERQHTQIVRLLVRAGA 200
Cdd:PHA02878 113 NVEIFKIILtnrYKNIQTIDLVYIDKkskddiieaeitklllsygadinmkdrhkgNTALHYATENKDQRLTELLLSYGA 192
                        170
                 ....*....|....*....
gi 767999017 201 KLDIQDKDGDTPLHEALRH 219
Cdd:PHA02878 193 NVNIPDKTNNSPLHHAVKH 211
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
375-410 3.81e-09

first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. It promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2 activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438386  Cd Length: 38  Bit Score: 52.07  E-value: 3.81e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767999017 375 ECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQC 410
Cdd:cd16726    2 ECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKC 37
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
372-417 4.38e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 52.38  E-value: 4.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767999017  372 KIEECVVCSDKKAAVLFQPCGHMCACENCANLM----KKCVQCRAVVERR 417
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIESV 50
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-214 4.89e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  74 DTPLHDAIskKRDDILAV---LLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRpwIVDEKKD----DGYTAL 146
Cdd:cd22192   18 ESPLLLAA--KENDVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPMTsdlyQGETAL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 147 HLAALNNHVEVAELLVHQGNanlDIQNVNQ----------------QTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGD 210
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGA---DVVSPRAtgtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                 ....
gi 767999017 211 TPLH 214
Cdd:cd22192  171 TVLH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
17-165 5.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 5.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  17 GDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAG 96
Cdd:PHA02875  79 GDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767999017  97 ADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEKKDdgYTALHLAALNNHVEVAELLVHQG 165
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNKIDIVRLFIKRG 225
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
375-418 1.49e-08

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 50.76  E-value: 1.49e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767999017 375 ECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRV 418
Cdd:cd16515    3 ECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRV 46
PHA02875 PHA02875
ankyrin repeat protein; Provisional
77-217 1.63e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  77 LHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPwivDEKKDDGYTALHLAALNNHVE 156
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP---DVKYPDIESELHDAVEEGDVK 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767999017 157 VAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEAL 217
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
180-280 2.57e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  180 LHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQDMQDVGKVDAAWEPskntLIMglgtqgAEK 259
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA----LHY------AAR 70
                          90       100
                  ....*....|....*....|.
gi 767999017  260 KSAASIACFLAANGADLSIRN 280
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
2-103 2.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   2 VLDKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNK-GHLQVVKTLLDFGCHPSLQDS-EGDTPLHD 79
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHS 275
                         90       100
                 ....*....|....*....|....
gi 767999017  80 AIskKRDDILAVLLEAGADVTITN 103
Cdd:PHA02878 276 SI--KSERKLKLLLEYGADINSLN 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-196 4.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017  142 GYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALHLAVERQHTQIVRLLV 196
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
54-216 4.21e-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: 55.92  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  54 QVVKTLLDF----GCHPSLQDSE-------GDTPLHDAISKKRDDILAVLLEAGADVtitnnngfnalhHAALRG---NP 119
Cdd:cd22194  111 EIVRILLAFaeenGILDRFINAEyteeayeGQTALNIAIERRQGDIVKLLIAKGADV------------NAHAKGvffNP 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 120 samrvllsklprpwivdEKKDDGY----TALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAV------ERQHT 189
Cdd:cd22194  179 -----------------KYKHEGFyfgeTPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVtvaedsKTQND 241
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767999017 190 QIVRL----LVRAGAK-LD-IQDKDGDTPLHEA 216
Cdd:cd22194  242 FVKRMydmiLLKSENKnLEtIRNNEGLTPLQLA 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-93 4.42e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767999017   42 TPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLL 93
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-162 5.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 5.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017  108 NALHHAALRGNPSAMRVLLSKLPRPWIVDekkDDGYTALHLAALNNHVEVAELLV 162
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD---GNGETALHFAASNGNVEVLKLLL 54
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
376-422 5.51e-08

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 49.75  E-value: 5.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRVPFIM 422
Cdd:cd16714   17 CKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQKIFM 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-216 6.35e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 6.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017  161 LVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEA 216
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
72-287 6.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  72 EGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLsklprpwivdekkDDGY--TALHLA 149
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-------------DNGVdtSILPIP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 150 ALNNhvEVAELLVHQGnANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQ 229
Cdd:PHA02874 101 CIEK--DMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767999017 230 DmqdvgkvDAAWEPSKNTLIMGLGTQGAEKKSAASIAcFLAANGADLSIRNKKGQSPL 287
Cdd:PHA02874 178 E-------KGAYANVKDNNGESPLHNAAEYGDYACIK-LLIDHGNHIMNKCKNGFTPL 227
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
472-505 1.08e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 48.20  E-value: 1.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 767999017  472 MCPVCLDRLKN--MIFLCGHGTCQLCGDRM----SECPIC 505
Cdd:pfam13923   1 MCPICMDMLKDpsTTTPCGHVFCQDCILRAlragNECPLC 40
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
328-363 1.13e-07

first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known as novel zinc finger protein (Novelzin), putative NF-kappa-B-activating protein 002N, skeletrophin, or zinc finger ZZ type with ankyrin repeat domain protein 1, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands. It promotes Delta ubiquitylation and endocytosis in Notch activation. Overexpression of MIB2 activates NF-kappaB and interferon-stimulated response element (ISRE) reporter activity. Moreover, MIB2 acts as a novel component of the activated B-cell CLL/lymphoma 10 (BCL10) complex and controls BCL10-dependent NF-kappaB activation. It also functions as a founder myoblast-specific protein that regulates myoblast fusion and muscle stability. MIB2 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of two C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438386  Cd Length: 38  Bit Score: 47.83  E-value: 1.13e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767999017 328 ECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLIC 363
Cdd:cd16726    2 ECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKC 37
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
376-412 1.19e-07

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 48.02  E-value: 1.19e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRA 412
Cdd:cd16510    4 CKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
374-411 1.49e-07

first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known as DAPK-interacting protein 1 (DIP-1) or zinc finger ZZ type with ankyrin repeat domain protein 2, is a large, multi-domain E3 ubiquitin-protein ligase that promotes ubiquitination of the cytoplasmic tails of Notch ligands, and thus plays an essential role in controlling metazoan development by Notch signaling. It is also involved in Wnt/beta-catenin signaling and nuclear factor (NF)-kappaB signaling, and has been implicated in innate immunity, neuronal function, genomic stability, and cell death. MIB1 contains an MZM region with two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region consisting of three C3HC4-type RING-HC fingers. This model corresponds to the first RING-HC finger.


Pssm-ID: 438384  Cd Length: 38  Bit Score: 47.48  E-value: 1.49e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16724    1 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2-70 2.33e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 2.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767999017    2 VLDKDGDRAVHHAAFGDEGAVIEVLHRgSADLNARNKRRqTPLHIAVNKGHLQVVKTLLDFGCHPSLQD 70
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
374-414 2.39e-07

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 47.29  E-value: 2.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKK----CVQCRAVV 414
Cdd:cd16647    2 SECVICYERPVDTVLYRCGHMCMCYDCALQLKRrggsCPICRAPI 46
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
376-418 2.70e-07

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 47.47  E-value: 2.70e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRV 418
Cdd:cd16713   10 CKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTV 52
PHA02736 PHA02736
Viral ankyrin protein; Provisional
141-204 2.96e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 50.26  E-value: 2.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999017 141 DGYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDI 204
Cdd:PHA02736  91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
106-226 3.60e-07

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: 52.78  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  106 GFNALHHAALRGNPSAMRVLLSKLprpwivDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQN---VNQ------ 176
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNL------SCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPlelANDqytsef 125
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017  177 ---QTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGD---TPLHEALRHhtlSQLR 226
Cdd:TIGR00870 126 tpgITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvkSQGVDSFYH---GESP 178
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
470-515 4.97e-07

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 46.52  E-value: 4.97e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767999017 470 QTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAIERRILL 515
Cdd:cd16515    1 ESECVVCMDAESQVIFLpCGHvCCCQTCSSSLSTCPLCRADITQRVRI 48
PHA02874 PHA02874
ankyrin repeat protein; Provisional
2-113 5.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   2 VLDKDGDRAVHHAA-FGDEGAVIEVLHRGSaDLNARNKRRQTPLHIAVNkgHLQVVKTLLDFGCHPSLQDSEGDTPLHDA 80
Cdd:PHA02874 185 VKDNNGESPLHNAAeYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767999017  81 ISKKRD-DILAVLLEAGADVTITNNNGFNALHHA 113
Cdd:PHA02874 262 INPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
469-512 5.77e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 46.21  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767999017  469 EQTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRM----SECPICRKAIERR 512
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLpCGHlCLCEECAERLlrkkKKCPICRQPIESV 50
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
472-513 5.79e-07

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 46.23  E-value: 5.79e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767999017 472 MCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAIERRI 513
Cdd:cd16500    2 LCKICMDAAIDCVLLeCGHmVTCTDCGKKLSECPICRQYVVRVV 45
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
327-370 8.21e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 45.83  E-value: 8.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767999017  327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRV----KKCLICKEQVQSR 370
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIESV 50
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
127-289 8.26e-07

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: 51.68  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 127 SKLPRP-WIVDE--KKDDGYTALHLAALN---NHVEVAELLVH--QGNANLDI--------QNVNQQTALHLAVERQHTQ 190
Cdd:cd22194   76 RKTDVPdFLMHKltASDTGKTCLMKALLNineNTKEIVRILLAfaEENGILDRfinaeyteEAYEGQTALNIAIERRQGD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 191 IVRLLVRAGAKLDIQDKD--------------GDTPLheALRHHTlSQLRQLQDMQDVGKVDAAWEPSK-NTLIMGLGTQ 255
Cdd:cd22194  156 IVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPL--ALAACT-NQPEIVQLLMEKESTDITSQDSRgNTVLHALVTV 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767999017 256 GAEKKS-AASI-----ACFLAANGADL-SIRNKKGQSPLDL 289
Cdd:cd22194  233 AEDSKTqNDFVkrmydMILLKSENKNLeTIRNNEGLTPLQL 273
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
322-364 1.22e-06

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438164 [Multi-domain]  Cd Length: 53  Bit Score: 45.56  E-value: 1.22e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767999017 322 DSETLEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16501    1 SGADADLCVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICR 43
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
329-364 1.33e-06

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 44.94  E-value: 1.33e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16510    4 CKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICR 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-226 2.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767999017  178 TALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLR 226
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
17-213 2.29e-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: 50.40  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  17 GDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDfgCHPSLQDS-------EGDTPLHDAISKKRDDIL 89
Cdd:cd22192   28 NDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIAVVNQNLNLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  90 AVLLEAGADVTitnnngfnalhhaalrgNPSAMRVLLSKLPRPWIVdekkdDGYTALHLAALNNHVEVAELLVHQGnANL 169
Cdd:cd22192  106 RELIARGADVV-----------------SPRATGTFFRPGPKNLIY-----YGEHPLSFAACVGNEEIVRLLIEHG-ADI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767999017 170 DIQNVNQQTALHLAVERQHT----QIVRLLVRAGAKLD------IQDKDGDTPL 213
Cdd:cd22192  163 RAQDSLGNTVLHILVLQPNKtfacQMYDLILSYDKEDDlqpldlVPNNQGLTPF 216
PHA02876 PHA02876
ankyrin repeat protein; Provisional
11-202 3.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  11 VHHAAFGD--EGAVIEVLHRGsADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFgchpslqdsegdtplhdaiskkrddi 88
Cdd:PHA02876 345 LHQASTLDrnKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDY-------------------------- 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  89 lavlleaGADVTITNNNGFNALHHAALRGNP-SAMRVLLSklpRPWIVDEKKDDGYTALHLAALNN-HVEVAELLVHQGn 166
Cdd:PHA02876 398 -------GADIEALSQKIGTALHFALCGTNPyMSVKTLID---RGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG- 466
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767999017 167 ANLDIQNVNQQTALHLAVErqHTQIVRLLVRAGAKL 202
Cdd:PHA02876 467 ADVNAINIQNQYPLLIALE--YHGIVNILLHYGAEL 500
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
147-221 3.97e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 3.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767999017 147 HLAALNNHVEVAELLvhQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHT 221
Cdd:PTZ00322  88 QLAASGDAVGARILL--TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
461-516 4.36e-06

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 44.36  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767999017 461 QQQLQDIKEQTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16714    5 EEKLRRLQEEKLCKICMDRNISIVFIpCGHlVTCKQCAEALDKCPICCTVITFKQKIF 62
PHA02876 PHA02876
ankyrin repeat protein; Provisional
11-230 5.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  11 VHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDfgchPSLQDSEGDTPLHDAISKKRDDILA 90
Cdd:PHA02876 182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID----NRSNINKNDLSLLKAIRNEDLETSL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  91 VLLEAGADVTITNNNGFNALHHAAlrGNPSAMRVLLSKLPRPWIVDEKKDDGYTALHLAALNNH-VEVAELLVHQGnANL 169
Cdd:PHA02876 258 LLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG-ADV 334
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767999017 170 DIQNVNQQTALHLAVE-RQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:PHA02876 335 NAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
469-516 6.72e-06

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) and similar proteins; CARP-2, also known as rififylin, caspase regulator CARP2, FYVE-RING finger protein Sakura (Fring), RING finger and FYVE-like domain-containing protein 1, RING finger protein 189 (RNF189), or RING finger protein 34-like, is an endosome-associated E3 ubiquitin-protein ligase that targets internalized receptor interacting kinase (RIP) for proteasome-mediated degradation. It acts as a negative regulator of tumor necrosis factor (TNF)-induced nuclear factor (NF)-kappaB activation. It also regulates the p53 signaling pathway by degrading 14-3-3sigma and stabilizing MDM2. As a caspase regulator, CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP2 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438367 [Multi-domain]  Cd Length: 50  Bit Score: 43.43  E-value: 6.72e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 469 EQTMCPVCLDRLKNMIFL-CGHG-TCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16707    1 DENLCKICMDSPIDCVLLeCGHMvTCTKCGKRMSECPICRQYVIRAVHVF 50
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 9.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 9.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017   59 LLDFG-CHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHA 113
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
468-516 9.44e-06

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) and similar proteins; CARP1, also known as caspase regulator CARP1, FYVE-RING finger protein Momo, RING finger homologous to inhibitor of apoptosis protein (RFI), RING finger protein 34 (RNF34), or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell which negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric, and colorectal cancers, suggesting a possible association with the development of digestive tract cancers. It regulates the p53 signaling pathway by degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP1 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438366 [Multi-domain]  Cd Length: 54  Bit Score: 43.09  E-value: 9.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767999017 468 KEQTMCPVCLDRLKNMIFL-CGHG-TCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16706    2 SDDNLCRICMDAVIDCVLLeCGHMvTCTKCGKRMSECPICRQYVVRAVHVF 52
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
464-516 1.01e-05

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 42.85  E-value: 1.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017 464 LQDIKEQTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16713    1 LRRLQEERTCKVCMDKEVSIVFIpCGHlVVCTECAPSLRKCPICRATIKGTVRTF 55
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
470-507 1.20e-05

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 42.24  E-value: 1.20e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767999017 470 QTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRK 507
Cdd:cd16510    1 EKLCKICMDREVNIVFLpCGHlVTCAQCAASLRKCPICRT 40
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
376-416 1.32e-05

RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) and similar proteins; MYLIP, also known as inducible degrader of the low-density lipoprotein (LDL)-receptor (IDOL), or MIR, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR, and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains an ERM-homology domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438186 [Multi-domain]  Cd Length: 52  Bit Score: 42.56  E-value: 1.32e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVER 416
Cdd:cd16523    5 CMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCRSRVEH 45
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
469-516 1.41e-05

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438164 [Multi-domain]  Cd Length: 53  Bit Score: 42.48  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 469 EQTMCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAIERRILLY 516
Cdd:cd16501    4 DADLCVVCMDAPIDTVFLeCGHlACCRLCSKRLRVCPICRQPISRVVRIF 53
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
327-373 1.48e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 42.25  E-value: 1.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRV----KKCLICKEQVQSRTKI 373
Cdd:cd23129    3 DECVVCMDAPRDAVCVPCGHVAGCMSCLKALmqssPLCPICRAPVRQVIKV 53
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
329-372 2.37e-05

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 42.07  E-value: 2.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTK 372
Cdd:cd16713   10 CKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTVR 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
22-222 2.43e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  22 VIEVLHRGSADLNARNKRRQTPLHIAVNKGH---LQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRD---DILAVLLEA 95
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  96 GADVTITNNN-GFNALHhAALRGNPSAMRVLLSKLprpwIVDE----KKDDGYTALHLAALnnhveVAELLVHQGNANLD 170
Cdd:PHA02798 171 GVDINTHNNKeKYDTLH-CYFKYNIDRIDADILKL----FVDNgfiiNKENKSHKKKFMEY-----LNSLLYDNKRFKKN 240
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999017 171 IQ-------NVNQQ-----TALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTL 222
Cdd:PHA02798 241 ILdfifsyiDINQVdelgfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESK 304
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
468-512 2.77e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 41.84  E-value: 2.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767999017 468 KEQTMCPVCLDRLKNMIFL-CGHGTCQLCGDRM--SECPICRKAIERR 512
Cdd:cd16602    1 QEEAVCAICLDYFKDPVSIgCGHNFCRVCVTQLwgFTCPQCRKSFPRR 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
7-128 2.84e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   7 GDRAVHHAAF-GDEGAVIEVLHRGSADLNAR------NKRR-------QTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSE 72
Cdd:cd22192   89 GETALHIAVVnQNLNLVRELIARGADVVSPRatgtffRPGPknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767999017  73 GDTPLHDAI---SKKR-----DDILAvlLEAGADV----TITNNNGFNALHHAALRGNPSAMRVLLSK 128
Cdd:cd22192  169 GNTVLHILVlqpNKTFacqmyDLILS--YDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
375-418 3.39e-05

RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and similar proteins; This subfamily includes Arabidopsis thaliana MIP1, RING finger protein 4 (RF4) and RING finger protein 298 (RF298). MIP1 interacts with MND1, HOP2 and XRI1. RF4 and RF298 are putative E3 ubiquitin-protein ligase that may mediate E2-dependent protein ubiquitination. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 41.34  E-value: 3.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 375 ECVVCSDKKAAVLFQPCGHMCACENCANL-----MKKCVQCRAVVERRV 418
Cdd:cd23128    5 ECVMCMEEERSVVFLPCAHQVVCSGCNDLhekkgMRECPSCRGEIQERI 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-149 3.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767999017   92 LLEAG-ADVTITNNNGFNALHHAALRGNPSAMRVLLsKLPRPWIVDEKkdDGYTALHLA 149
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDE--EGLTALDLA 56
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
376-420 4.44e-05

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 40.83  E-value: 4.44e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRVPF 420
Cdd:cd16500    3 CKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICRQYVVRVVHF 47
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
374-416 4.97e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 41.09  E-value: 4.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLM----KKCVQCRAVVER 416
Cdd:cd23129    3 DECVVCMDAPRDAVCVPCGHVAGCMSCLKALmqssPLCPICRAPVRQ 49
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
110-227 5.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 110 LHHAALRGNPSAMRVLLSKLPRPWIVDEkkdDGYTALHLAALNNHVEVAELLVHQGnANLDIQNVNQQTALHLAVERQHT 189
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDY---DGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFR 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 190 QIVRLLVR-------AGAKLDIQDKDGDTPLHE----ALRHHTLSQLRQ 227
Cdd:PTZ00322 162 EVVQLLSRhsqchfeLGANAKPDSFTGKPPSLEdspiSSHHPDFSAVPQ 210
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
72-216 5.75e-05

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: 45.94  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  72 EGDTPLHDAISKKRDDILAVLLEAGADVtitnnngfnalhHAALRGnpsamRVLLSKLPRPWIVdekkdDGYTALHLAAL 151
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADV------------HAHAKG-----RFFQPKYQGEGFY-----FGELPLSLAAC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 152 NNHVEVAELLVH--QGNANLDIQNVNQQTALHLAVE-----RQHTQIVR----LLVRAGAKL-------DIQDKDGDTPL 213
Cdd:cd22193  133 TNQPDIVQYLLEneHQPADIEAQDSRGNTVLHALVTvadntKENTKFVTrmydMILIRGAKLcptveleEIRNNDGLTPL 212

                 ...
gi 767999017 214 HEA 216
Cdd:cd22193  213 QLA 215
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
328-373 6.23e-05

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 40.35  E-value: 6.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767999017 328 ECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKI 373
Cdd:cd16515    3 ECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVRI 48
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
175-207 7.25e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 7.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767999017  175 NQQTALHLAVERQ-HTQIVRLLVRAGAKLDIQDK 207
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
327-374 8.63e-05

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 40.36  E-value: 8.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRVKK----CLICKEQVQSRTKIE 374
Cdd:cd16647    2 SECVICYERPVDTVLYRCGHMCMCYDCALQLKRrggsCPICRAPIKDVIKIY 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
142-200 9.63e-05

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: 44.87  E-value: 9.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767999017 142 GYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQ-------------QTALHLAVERQHTQIVRLLVRAGA 200
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgQTALHIAIENRNLNLVRLLVENGA 97
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
466-506 9.66e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 40.50  E-value: 9.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999017 466 DIKEQTMCPVCLDRLKNMIFL-CGHGTCQLC----------GDRMSECPICR 506
Cdd:cd16591    2 NIKEEVTCPICLELLTEPLSLdCGHSFCQACitanhkesvnQEGESSCPVCR 53
PHA02859 PHA02859
ankyrin repeat protein; Provisional
22-108 1.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  22 VIEVLHRGSADLNARNKRRQTPLH-----IAVNkghLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDD-ILAVLLEA 95
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLHmymcnFNVR---INVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKkIFDFLTSL 181
                         90
                 ....*....|...
gi 767999017  96 GADVTITNNNGFN 108
Cdd:PHA02859 182 GIDINETNKSGYN 194
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
469-508 1.46e-04

RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 39.71  E-value: 1.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 469 EQTMCPVCLDRL-KNMIFLCGHGTCQLC------GDRMSECPICRKA 508
Cdd:cd23132    1 EEFLCCICLDLLyKPVVLECGHVFCFWCvhrcmnGYDESHCPLCRRP 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
141-173 1.48e-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: 1.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767999017  141 DGYTALHLAAL-NNHVEVAELLVHQGnANLDIQN 173
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKG-ADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
7-60 2.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017    7 GDRAVHHAA-FGDEgAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLL 60
Cdd:pfam13637   1 ELTALHAAAaSGHL-ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02791 PHA02791
ankyrin-like protein; Provisional
41-196 2.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  41 QTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEgdTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPS 120
Cdd:PHA02791  31 HSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQ 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017 121 AMRVLLSKLPRpwIVDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQNVnqQTALHLAVERQHTQIVRLLV 196
Cdd:PHA02791 109 TVKLFVKKNWR--LMFYGKTGWKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDMMILLL 180
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
376-415 2.47e-04

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and similar proteins; RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection, and promoting the degradation of IRF3, another important component required for virus-triggered interferon induction. Although RNF26 substrates of ubiquitination remain unclear at present, RNF26 upregulation in gastric cancer might be implicated in carcinogenesis through dysregulation of growth regulators. RNF26 contains an N-terminal leucine zipper domain and a C-terminal modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438442 [Multi-domain]  Cd Length: 60  Bit Score: 39.32  E-value: 2.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLM-------KKCVQCRAVVE 415
Cdd:cd16788    8 CVICQDQSKTVLILPCRHMCLCRQCANILlqqpvyrRNCPLCRTMIL 54
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
328-364 2.48e-04

RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438183 [Multi-domain]  Cd Length: 39  Bit Score: 38.43  E-value: 2.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767999017 328 ECMVCSDMKRDTLFGpCGHiATCSLCSPRVKKCLICK 364
Cdd:cd16520    2 LCPICMERKKNVVFL-CGH-GTCQKCAEKLKKCPICR 36
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
329-367 2.58e-04

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 38.91  E-value: 2.58e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQV 367
Cdd:cd16500    3 CKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICRQYV 41
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
329-373 2.75e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 38.97  E-value: 2.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKI 373
Cdd:cd16714   17 CKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQKI 61
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
456-514 3.06e-04

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 39.97  E-value: 3.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767999017 456 DVQKLQQQLQDIKEQTMCPVCLDRLKNMIFL-CGHGTCQLC-------GDRMSECPICRKAIERRIL 514
Cdd:cd16498    2 RIERVQEVISAMQKNLECPICLELLKEPVSTkCDHQFCRFCilkllqkKKKPAPCPLCKKSVTKRSL 68
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
41-70 3.16e-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: 38.04  E-value: 3.16e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767999017   41 QTPLHIAVNK-GHLQVVKTLLDFGCHPSLQD 70
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
88-225 3.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  88 ILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEkkdDGYTALHLAALNNHVEVAELLVHQGNa 167
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL---DDLSVLECAVDSKNIDTIKAIIDNRS- 235
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767999017 168 nldiqNVNQQT-ALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQL 225
Cdd:PHA02876 236 -----NINKNDlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL 289
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
376-419 3.37e-04

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinase signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438164 [Multi-domain]  Cd Length: 53  Bit Score: 38.62  E-value: 3.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRVP 419
Cdd:cd16501    8 CVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICRQPISRVVR 51
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
466-514 3.63e-04

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 38.66  E-value: 3.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767999017 466 DIKEQTMCPVCLDRLKNMIFL-CGHGTCQLCGDRMSE---------CPICRKAIERRIL 514
Cdd:cd16583    1 DSDEEGVCPICQEPLKEAVSTdCGHLFCRMCLTQHAKkasasgvfsCPVCRKPCSEGVL 59
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
467-507 3.74e-04

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 38.59  E-value: 3.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 467 IKEQTMCPVCLDRLKNMIFL-CGHGTCQLCGDRMSE-------CPICRK 507
Cdd:cd16611    1 LTEELHCPLCLDFFRDPVMLsCGHNFCQSCITGFWElqaedttCPECRE 49
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
375-411 4.14e-04

Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins; This subfamily corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis.


Pssm-ID: 438311 [Multi-domain]  Cd Length: 40  Bit Score: 38.07  E-value: 4.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 375 ECVVCSDKKAAVLFQPCGHMCACENCANLM--KKCVQCR 411
Cdd:cd16649    2 LCVVCLENPASVLLLPCRHLCLCEVCAKGLrgKTCPICR 40
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
468-512 4.58e-04

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 38.44  E-value: 4.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767999017 468 KEQTMCPVCLDRLKNMIFL-CGHGTCQLC-------GDRMSECPICRKAIERR 512
Cdd:cd16594    3 QEELTCPICLDYFTDPVTLdCGHSFCRACiarcweePETSASCPQCRETCPQR 55
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
473-505 5.17e-04

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 37.85  E-value: 5.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 473 CPVCLDRLKNMIFL-CGHGTCQLCGDRMSE-----CPIC 505
Cdd:cd16449    3 CPICLERLKDPVLLpCGHVFCRECIRRLLEsgsikCPIC 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
131-183 5.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 5.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767999017  131 RPWIVDEKKDDGYTALHLAALNNHVEVAELLvHQGNANLDIQNVNQQTALHLA 183
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVL-LAYGVDLNLKDEEGLTALDLA 56
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
376-419 5.96e-04

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 37.83  E-value: 5.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLM---KKCVQCRAVVERRVP 419
Cdd:cd16648    4 CVICLSNPRSCVFLECGHVCSCIECYEALpspKKCPICRSFIKRVVP 50
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
141-171 6.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 6.41e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767999017   141 DGYTALHLAALNNHVEVAELLVHQGnANLDI 171
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
470-516 6.98e-04

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 37.83  E-value: 6.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999017 470 QTMCPVCLDRLKNMIFL-CGHG-TCQLCGDRMSE---CPICRKAIERRILLY 516
Cdd:cd16648    1 DNACVICLSNPRSCVFLeCGHVcSCIECYEALPSpkkCPICRSFIKRVVPLY 52
PHA02741 PHA02741
hypothetical protein; Provisional
99-230 8.80e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.41  E-value: 8.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  99 VTITNNNGFNALHHAALRGNPSAMRVLLSKLP---RPWIVDEKKDDGYTALHLAALNNH----VEVAELLVHQGnANLDI 171
Cdd:PHA02741  14 IAEKNSEGENFFHEAARCGCFDIIARFTPFIRgdcHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELG-ADINA 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767999017 172 QN-VNQQTALHLAVERQHTQIVRLLVR-AGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQD 230
Cdd:PHA02741  93 QEmLEGDTALHLAAHRRDHDLAEWLCCqPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
RING-HC_UNK-like cd16614
RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and ...
328-364 8.91e-04

RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and similar proteins; UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. Both UNK and UNKL contain several tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438276  Cd Length: 38  Bit Score: 37.15  E-value: 8.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767999017 328 ECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 364
Cdd:cd16614    2 KCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH 38
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
329-368 1.00e-03

RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) and similar proteins; MYLIP, also known as inducible degrader of the low-density lipoprotein (LDL)-receptor (IDOL), or MIR, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR, and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains an ERM-homology domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438186 [Multi-domain]  Cd Length: 52  Bit Score: 37.17  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQ 368
Cdd:cd16523    5 CMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCRSRVE 44
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
72-104 1.02e-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: 36.50  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767999017   72 EGDTPLHDAISKKRD-DILAVLLEAGADVTITNN 104
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
376-411 1.12e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 36.95  E-value: 1.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767999017 376 CVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16566    5 CTLCFDKVADTELRPCGHSGFCMECALQLETCPLCR 40
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
465-506 1.19e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.


Pssm-ID: 438252 [Multi-domain]  Cd Length: 61  Bit Score: 37.32  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 465 QDIKEQTMCPVCLDRLKNMIFL-CGHGTCQLC-------GDRMSECPICR 506
Cdd:cd16590    1 EDIQEELTCPICLDYFQDPVSIeCGHNFCRGClhrnwapGGGPFPCPECR 50
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
372-415 1.25e-03

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling through working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. NEURL1B contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438440 [Multi-domain]  Cd Length: 57  Bit Score: 37.23  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 372 KIEECVVCSDKKAAVLFQPCGHMCACENCANLMKK-----CVQCRAVVE 415
Cdd:cd16786    1 KNGECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKRqinacCPICRRVIK 49
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
374-411 1.29e-03

Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING finger domain protein 1 (CGRRF1) and similar proteins; CGRRF1, also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. CGRRF1 contains a C-terminal modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438441 [Multi-domain]  Cd Length: 38  Bit Score: 36.58  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16787    1 KDCVVCQNAPVNRVLLPCRHACVCDECFKRLQRCPMCR 38
PHA02946 PHA02946
ankyin-like protein; Provisional
3-168 1.30e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   3 LDKDGDRAVHHAAFG----DEGAVIEVLHRGSADlNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLH 78
Cdd:PHA02946  32 IEPSGNYHILHAYCGikglDERFVEELLHRGYSP-NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017  79 dAISKKRDDILA---VLLEAGADVT---------------------------------ITNNNGFNALHHAALRGNPSAM 122
Cdd:PHA02946 111 -YLSGTDDEVIErinLLVQYGAKINnsvdeegcgpllactdpservfkkimsigfearIVDKFGKNHIHRHLMSDNPKAS 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767999017 123 RVllSKLPRPWIVDEKKD-DGYTALHLAALNN--HVEVAELLVHQGNAN 168
Cdd:PHA02946 190 TI--SWMMKLGISPSKPDhDGNTPLHIVCSKTvkNVDIINLLLPSTDVN 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
178-288 1.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 178 TALHLAVERQH---TQIVRLLVRAGAKLDIQDKDGDTPLHEALRHH-TLSQLRQLQDM-QDVGKVDAAwepSKNTLIMGL 252
Cdd:PHA03095  49 TPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAgADVNAKDKV---GRTPLHVYL 125
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767999017 253 GTQGAEKKsaasIACFLAANGADLSIRNKKGQSPLD 288
Cdd:PHA03095 126 SGFNINPK----VIRLLLRKGADVNALDLYGMTPLA 157
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
375-411 1.79e-03

RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the third RING-HC finger of MIB1, as well as the second RING-HC finger of MIB2. In addition to MIB1 and MIB2, the RING-HC fingers of RING domain ligase RGLG1, RGLG2 and similar proteins from plant are also included in this model. RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. All RGLG proteins contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438183 [Multi-domain]  Cd Length: 39  Bit Score: 36.11  E-value: 1.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767999017 375 ECVVCSDKKAAVLFQpCGHmCACENCANLMKKCVQCR 411
Cdd:cd16520    2 LCPICMERKKNVVFL-CGH-GTCQKCAEKLKKCPICR 36
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
329-367 1.98e-03

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) and similar proteins; CARP-2, also known as rififylin, caspase regulator CARP2, FYVE-RING finger protein Sakura (Fring), RING finger and FYVE-like domain-containing protein 1, RING finger protein 189 (RNF189), or RING finger protein 34-like, is an endosome-associated E3 ubiquitin-protein ligase that targets internalized receptor interacting kinase (RIP) for proteasome-mediated degradation. It acts as a negative regulator of tumor necrosis factor (TNF)-induced nuclear factor (NF)-kappaB activation. It also regulates the p53 signaling pathway by degrading 14-3-3sigma and stabilizing MDM2. As a caspase regulator, CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP2 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438367 [Multi-domain]  Cd Length: 50  Bit Score: 36.49  E-value: 1.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQV 367
Cdd:cd16707    5 CKICMDSPIDCVLLECGHMVTCTKCGKRMSECPICRQYV 43
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
328-373 1.99e-03

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling through working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. NEURL1B contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438440 [Multi-domain]  Cd Length: 57  Bit Score: 36.46  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767999017 328 ECMVCSDMKRDTLFGPCGHIATCSLCSPRVKK-----CLICKEQVQSRTKI 373
Cdd:cd16786    4 ECTVCFDSEVDTVIYTCGHMCLCNSCGLKLKRqinacCPICRRVIKDVIKI 54
RING-HC_SIAH2 cd16752
RING finger, HC subclass, found in seven in absentia homolog 2 (SIAH2) and similar proteins; ...
473-509 2.07e-03

RING finger, HC subclass, found in seven in absentia homolog 2 (SIAH2) and similar proteins; SIAH2 is an E3 ubiquitin-protein ligase that contributes to proteasome-mediated degradation of multiple targets in numerous cellular processes. It targets the ubiquitylation and degradation of tumor necrosis factor receptor-associated factor 2 (TRAF2) under stress conditions, which is required for the cell to commit to undergoing apoptosis. It is, therefore, a key regulator of TRAF2-dependent signaling in response to tumor necrosis factor-alpha (TNF-alpha) treatment and UV irradiation. SIAH2 modulates the polyubiquitination of G protein pathway suppressor 2 (GPS2), and targets it for proteasomal degradation. It is also a regulator of NF-E2-related factor 2 (Nrf2), a key regulator of cellular oxidative response, and contributes to the degradation of Nrf2 irrespective of its phosphorylation status. Moreover, SIAH2 contributes to castration-resistant prostate cancer (CRPC) by regulation of androgen receptor (AR) transcriptional activity. It enhances AR transcriptional activity and prostate cancer cell growth. Its stability can be regulated by AKR1C3. SIAH2 also inhibits tyrosine kinase-2 (TYK2)-STAT3 signaling in lung carcinoma cells. Furthermore, SIAH2 regulates obesity-induced adipose tissue inflammation by altering peroxisome proliferator-activated receptor gamma (PPAR gamma) protein levels and selectively regulating PPAR gamma activity. It also functions as a regulator of the nuclear hormone receptor RevErbalpha (Nr1d1) stability and rhythmicity, and overall circadian oscillator function. In addition, SIAH2 is an essential component of the hypoxia response Hippo signaling pathway and has been implicated in normal development and tumorigenesis. It modulates the hypoxia pathway upstream of hypoxia-induced transcription factor subunit HIF-1alpha, and therefore may play an important role in angiogenesis in response to hypoxic stress in endothelial cells. It also stimulates transcriptional coactivator YAP1 by destabilizing serine/threonine-protein kinase LATS2, a critical component of the Hippo pathway, in response to hypoxia. Meanwhile, SIAH2 is involved in regulation of tight junction integrity and cell polarity under hypoxia, through its regulation of apoptosis-stimulating proteins of p53 subunit 2 (ASPP2) stability. SIAH2 contains an N-terminal C3HC4-type RING-HC finger, two zinc-finger subdomains, and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD) responsible for dimer formation.


Pssm-ID: 438410 [Multi-domain]  Cd Length: 51  Bit Score: 36.51  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 473 CPVCLDRLKNMIFLC--GHGTCQLCGDRMSECPICRKAI 509
Cdd:cd16752    6 CPVCFDYVLPPILQCqaGHLVCNQCRQKLSCCPTCRGPL 44
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
473-506 2.08e-03

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141/ZNF230 gene mutations may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 438207 [Multi-domain]  Cd Length: 40  Bit Score: 35.91  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 473 CPVCLDRLKNMIFLCGHGTCQLCGDRMSE----CPICR 506
Cdd:cd16545    3 CCICMDRKADLILPCAHSYCQKCIDKWSDrhrtCPICR 40
RING-HC_SIAHs cd16571
RING finger, HC subclass, found in Drosophila melanogaster protein Seven-in-Absentia (sina) ...
473-506 2.21e-03

RING finger, HC subclass, found in Drosophila melanogaster protein Seven-in-Absentia (sina) and its homologs; This subfamily includes the Drosophila melanogaster protein Seven-in-Absentia (sina), its mammalian orthologs, SIAH1 and SIAH2, plant SINA-related proteins, and similar proteins. Sina plays an important role in the phyllopod-dependent degradation of the transcriptional repressor tramtrack to allow the formation of the R7 photoreceptor in the developing eye of Drosophila melanogaster. Both SIAH1 and SIAH2 are E3 ubiquitin-protein ligases, mediating the ubiquitinylation and subsequent proteasomal degradation of biologically important target proteins that regulate general functions, such as cell cycle control, apoptosis, and DNA repair. They are inducible by the tumor suppressor and transcription factor p53. SIAH2 can also be regulated by sex hormones and cytokine signaling. Moreover, they share high sequence similarity, but possess contrary roles in cancer, with SIAH1 more often acting as a tumor suppressor while SIAH2 functions as a proto-oncogene. Plant SINAT1-5 are putative E3 ubiquitin ligases involved in the regulation of stress responses. All subfamily members possess two characteristic domains, an N-terminal C3HC4-type RING-HC finger and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD).


Pssm-ID: 438233 [Multi-domain]  Cd Length: 39  Bit Score: 35.70  E-value: 2.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767999017 473 CPVCLDRLKNMIFLC--GHGTCQLCGDRMS-ECPICR 506
Cdd:cd16571    3 CPVCFEPLLPPIYQCsnGHLLCSSCRSKLTnKCPTCR 39
RING-HC_SPL2-like cd23145
RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar ...
374-417 2.29e-03

RING finger, HC subclass, found in Arabidopsis thaliana SP1-like protein 2 (SPL2) and similar proteins; SPL2, also known as RING-type E3 ubiquitin transferase SPL2, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. SPL2 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438507 [Multi-domain]  Cd Length: 47  Bit Score: 36.02  E-value: 2.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERR 417
Cdd:cd23145    4 ELCVVCLLRRRRVAFIECGHRVCCELCARRVTREANPRCPVCRQ 47
PHA02743 PHA02743
Viral ankyrin protein; Provisional
142-203 2.47e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767999017 142 GYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLD 203
Cdd:PHA02743  94 GNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVCD 155
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
141-171 2.49e-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: 35.31  E-value: 2.49e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767999017  141 DGYTALHLAALNNHVEVAELLVHQGnANLDI 171
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
72-101 3.00e-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: 35.26  E-value: 3.00e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 767999017    72 EGDTPLHDAISKKRDDILAVLLEAGADVTI 101
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
467-511 3.05e-03

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 36.30  E-value: 3.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017 467 IKEQTMCPVCLDRLKNMIFL-CGHGTCQLC---------GDRMSECPICRKAIER 511
Cdd:cd16598    1 LEEEVTCSICLDYLRDPVTIdCGHNFCRSCitdycpisgGHERPVCPLCRKPFKK 55
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
329-367 3.11e-03

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) and similar proteins; CARP1, also known as caspase regulator CARP1, FYVE-RING finger protein Momo, RING finger homologous to inhibitor of apoptosis protein (RFI), RING finger protein 34 (RNF34), or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell which negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric, and colorectal cancers, suggesting a possible association with the development of digestive tract cancers. It regulates the p53 signaling pathway by degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10. CARP1 contains an N-terminal FYVE-like domain and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438366 [Multi-domain]  Cd Length: 54  Bit Score: 35.77  E-value: 3.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQV 367
Cdd:cd16706    7 CRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYV 45
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
467-514 3.16e-03

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 36.28  E-value: 3.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767999017 467 IKEQTMCPVCLDRLKNMIFL-CGHGTCQLCGDRMSE------CPICRKAIERRIL 514
Cdd:cd16599    1 FKEELLCPICYEPFREAVTLrCGHNFCKGCVSRSWErqprapCPVCKEASSSDDL 55
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
329-367 3.25e-03

Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase (MAPL) and similar proteins; MAPL, also known as MULAN, mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, growth inhibition and death E3 ligase (GIDE), putative NF-kappa-B-activating protein 266, or RING finger protein 218 (RNF218), is a multifunctional mitochondrial outer membrane protein involved in several processes specific to metazoan (multicellular animal) cells, such as NF-kappaB activation, innate immunity and antiviral signaling, suppression of PINK1/parkin defects, mitophagy in skeletal muscle, and caspase-dependent apoptosis. MAPL contains a unique BAM (beside a membrane)/GIDE (growth inhibition death E3 ligase) domain and a C-terminal modified cytosolic C3HC5-type RING-HC finger which is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438310 [Multi-domain]  Cd Length: 52  Bit Score: 35.91  E-value: 3.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767999017 329 CMVCSDMKRDTLFGPCGHIATCSLC---SPRVKKCLICKEQV 367
Cdd:cd16648    4 CVICLSNPRSCVFLECGHVCSCIECyeaLPSPKKCPICRSFI 45
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
466-512 3.28e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 36.13  E-value: 3.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767999017 466 DIKEQTMCPVCLDRLKNMIFL-CGHGTCQLC--------GDRMSECPICRKAIERR 512
Cdd:cd16597    1 DLEEELTCSICLELFKDPVTLpCGHNFCGVCiektwdsqHGSEYSCPQCRATFPRR 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
42-63 3.76e-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: 34.87  E-value: 3.76e-03
                           10        20
                   ....*....|....*....|..
gi 767999017    42 TPLHIAVNKGHLQVVKTLLDFG 63
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKG 25
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
470-506 4.13e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 35.47  E-value: 4.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767999017 470 QTMCPVCLDRLKNMIFL--CGHGTCQLCGDRM----SECPICR 506
Cdd:cd16711    1 EETCPICLGEIQNKKTLdkCKHSFCEDCITRAlqvkKACPMCG 43
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
108-202 4.34e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.84  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 108 NALHHAALRGNPSAMRVLLSKLPR--PWIVDEKKDD---GYTALHLAALN-----NHVEVAELLVHQGNAN----LDIQN 173
Cdd:cd22197    8 DRLFSVVSRGNPEELAGLLEYLRRtsKYLTDSEYTEgstGKTCLMKAVLNlqdgvNACIMPLLEIDKDSGNpkplVNAQC 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767999017 174 VNQ----QTALHLAVERQHTQIVRLLVRAGAKL 202
Cdd:cd22197   88 TDEyyrgHSALHIAIEKRSLQCVKLLVENGADV 120
PHA02917 PHA02917
ankyrin-like protein; Provisional
64-110 4.71e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.60  E-value: 4.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999017  64 CHPSLQD-----SEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNAL 110
Cdd:PHA02917 438 CLPYLKDinmidKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCI 489
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
374-411 4.86e-03

RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar proteins; UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. It shows high sequence similarity with RING finger protein unkempt (UNK), which is a metazoan-specific zinc finger protein enriched in embryonic brains, and may play a broad regulatory role during the formation of the central nervous system (CNS). UNKL contains several CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438428  Cd Length: 44  Bit Score: 35.15  E-value: 4.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767999017 374 EECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCR 411
Cdd:cd16772    1 KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCK 38
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
175-204 4.95e-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: 4.95e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 767999017   175 NQQTALHLAVERQHTQIVRLLVRAGAKLDI 204
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
473-516 5.08e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 35.32  E-value: 5.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 473 CPVCLDRLKNMIFL-CGH-GTCQLCGDRM----SECPICRKAIERRILLY 516
Cdd:cd23129    5 CVVCMDAPRDAVCVpCGHvAGCMSCLKALmqssPLCPICRAPVRQVIKVY 54
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
473-509 5.16e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 35.03  E-value: 5.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767999017 473 CPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAI 509
Cdd:cd16566    5 CTLCFDKVADTELRpCGHsGFCMECALQLETCPLCRQPI 43
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
375-411 5.51e-03

Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1), RING finger protein 157 (RNF157) and similar proteins; MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. MGRN1 also interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. Both MGRN1 and RNF157 contain a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438443 [Multi-domain]  Cd Length: 42  Bit Score: 34.97  E-value: 5.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767999017 375 ECVVC--SDKKAAVLfqPCGHMCACENCANLMK----KCVQCR 411
Cdd:cd16789    2 ECVIClsDPRDTAVL--PCRHLCLCSDCAEVLRyqsnKCPICR 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
41-67 5.58e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 5.58e-03
                          10        20
                  ....*....|....*....|....*..
gi 767999017   41 QTPLHIAVNKGHLQVVKTLLDFGCHPS 67
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
327-373 5.72e-03

RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant; RGLG1 is a ubiquitously expressed E3 ubiquitin-protein ligase that interacts with UBC13 and, together with UBC13, catalyzes the formation of K63-linked polyubiquitin chains, which is involved in DNA damage repair. RGLG1 mediates the formation of canonical, K48-linked polyubiquitin chains that target proteins for degradation. It also regulates apical dominance by acting on the auxin transport proteins abundance. RGLG1 has overlapping functions with its closest sequelog, RGLG2. They both function as RING E3 ligases that interact with ethylene response factor 53 (ERF53) in the nucleus and negatively regulate the plant drought stress response. Members of this subfamily contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438389  Cd Length: 48  Bit Score: 35.15  E-value: 5.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767999017 327 EECMVCSDMKRDTLFGpCGHiATCSLCSPRVKKCLICKEQVQSRTKI 373
Cdd:cd16729    3 QLCPICLSNPKDMAFG-CGH-QTCCECGQSLTHCPICRQPITTRIKL 47
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
131-207 5.72e-03

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: 39.39  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017 131 RPWIVDEK---KDDGYTALHLAALNNHVEVAE-----LLVHQGNANLDiQNVNQ---------QTALHLAVERQHTQIVR 193
Cdd:cd22193   15 RKDLTDSEfteSSTGKTCLMKALLNLNPGTNDtirilLDIAEKTDNLK-RFINAeytdeyyegQTALHIAIERRQGDIVA 93
                         90
                 ....*....|....
gi 767999017 194 LLVRAGAKLDIQDK 207
Cdd:cd22193   94 LLVENGADVHAHAK 107
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
326-372 5.86e-03

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins; NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438439 [Multi-domain]  Cd Length: 59  Bit Score: 35.34  E-value: 5.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999017 326 LEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKK-----CLICKEQVQSRTK 372
Cdd:cd16785    4 SDECTICYENAVDTVIYTCGHMCLCYACGLRLKKmlnacCPICRRAIKDIIK 55
RING-HC_Bre1-like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
465-508 7.45e-03

RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, the Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438162 [Multi-domain]  Cd Length: 59  Bit Score: 34.84  E-value: 7.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 465 QDIKEQTMCPVCLDRLKN-MIFLCGHGTCQLCGD-----RMSECPICRKA 508
Cdd:cd16499    1 KDLRELLKCSVCNDRFKDvIITKCGHVFCNECVQkrletRQRKCPGCGKA 50
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
7-128 7.58e-03

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: 38.97  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999017   7 GDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRR--------------QTPLHIAVNKGHLQVVKTLLDFGCHP-SLQDS 71
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTSQDS 220
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767999017  72 EGDTPLH-------------DAISKKRDDILAVL----LEagadvTITNNNGFNALHHAALRGNPSAMRVLLSK 128
Cdd:cd22194  221 RGNTVLHalvtvaedsktqnDFVKRMYDMILLKSenknLE-----TIRNNEGLTPLQLAAKMGKAEILKYILSR 289
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
464-507 7.69e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 35.65  E-value: 7.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767999017 464 LQDIKEQTMCPVCLDRL-KNMIFLCGHGTCQLC-----GDRMSECPICRK 507
Cdd:cd16596    3 LTMMWEEVTCPICLDPFvEPVSIECGHSFCQECisqvgKGGGSVCPVCRQ 52
RING-HC_NEURL3 cd16552
RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins; ...
327-368 8.40e-03

RING finger, HC subclass, found in neuralized-like protein 3 (NEURL3) and similar proteins; NEURL3, also known as lung-inducible neuralized-related C3HC4 RING domain protein (LINCR), is a novel inflammation-induced E3 ubiquitin-protein ligase encoded by LINCR, a glucocorticoid-attenuated response gene induced in the lung during endotoxemia. It is expressed in alveolar epithelial type II cells, preferentially interacts with the ubiquitin-conjugating enzyme UbcH6, and generates polyubiquitin chains linked via non-canonical lysine residues. Overexpression of NEURL3 in the developing lung epithelium inhibits distal differentiation and induces cystic changes in the Notch signaling pathway. NEURL3 contains an N-terminal neuralized homology repeat (NHR) domain similar to the SPRY (SPla and the RYanodine receptor) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438214 [Multi-domain]  Cd Length: 50  Bit Score: 34.52  E-value: 8.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767999017 327 EECMVCSDMKRDTLFGPCGHIATCSLCSPRV----KKCLICKEQVQ 368
Cdd:cd16552    2 EECAICFHHTANTRLVPCGHSHFCGSCAWHIfrdtARCPVCRWQIE 47
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
466-506 9.14e-03

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 34.88  E-value: 9.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767999017 466 DIKEQTMCPVCLDRLKNMIFL-CGHGTCQLCGDRMSE-----------CPICR 506
Cdd:cd16593    1 SLADEVNCPICQGTLREPVTIdCGHNFCRACLTRYCEipgpdleepptCPLCK 53
 
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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